|
Name |
Accession |
Description |
Interval |
E-value |
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-1454 |
0e+00 |
|
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: 2527.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1 WTKPILKKGYRRRLELSDIYQIPSADSADNLSEKLEREWDRELATSKKKPKLINALRRCFFWKFMFYGIILYLGEVTKSV 80
Cdd:TIGR01271 19 WTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELASAKKNPKLLNALRRCFFWRFVFYGILLYFGEATKAV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 81 QPLLLGRIIASYDPDNSDERSIAYYLGIGLCLLFLVRTLLIHPAIFGLHHIGMQMRIAMFSLIYKKILKLSSRVLDKIST 160
Cdd:TIGR01271 99 QPLLLGRIIASYDPFNAPEREIAYYLALGLCLLFIVRTLLLHPAIFGLHHLGMQMRIALFSLIYKKTLKLSSRVLDKIST 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 161 GQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLLWDMLEASAFSGLAFLIVLAFFQAWLGQMMMKYRNKRAGKINE 240
Cdd:TIGR01271 179 GQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQACLGQKMMPYRDKRAGKISE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 241 RLVITSEIIENIQSVKAYCWEDAMEKMIESIRETELKLTRKAAYVRYFNSSAFFFSGFFVVFLAVLPYAVIKGIILRKIF 320
Cdd:TIGR01271 259 RLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAYLRYFYSSAFFFSGFFVVFLSVVPYALIKGIILRRIF 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 321 TTISFCIVLRMTVTRQFPGSVQTWYDSIGAINKIQDFLLKKEYKALEYNLTTTGVELDKVTAFWDEGIGELFVQANQENN 400
Cdd:TIGR01271 339 TTISYCIVLRMTVTRQFPGAIQTWYDSLGAITKIQDFLCKEEYKTLEYNLTTTEVEMVNVTASWDEGIGELFEKIKQNNK 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 401 NSKAPSTDNNLFFSNFPLHASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGRISFSPQVSWI 480
Cdd:TIGR01271 419 ARKQPNGDDGLFFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWI 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 481 MPGTIKENIIFGVSYDEYRYKSVIKACQLEEDISKFPEKDYTVLGEGGIILSGGQRARISLARAVYKDADLYLLDSPFGH 560
Cdd:TIGR01271 499 MPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 561 LDIFTEKEIFESCVCKLMANKTRILVTSKLEHLKIADKILILHEGSCYFYGTFSELQGQRPDFSSELMGFDSFDQFSAER 640
Cdd:TIGR01271 579 LDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLLGLEAFDNFSAER 658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 641 RNSILTETLRRFSIEGEG-MGSRNEIKKQSFKQT-SDFNDKRKSSIIINPLNANRKFSVVQKNGMQ---VGVEDGHNDPP 715
Cdd:TIGR01271 659 RNSILTETLRRVSIDGDStVFSGPETIKQSFKQPpPEFAEKRKQSIILNPIASARKFSFVQMGPQKaqaTTIEDAVREPS 738
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 716 ERRLSLIPDLEQGDVGLLRSNMLSTDHMLQSRRRQSVLNLMTGTSSvsyGPNVSKKGSTTFRKMSMVPQTN-LASEIDIY 794
Cdd:TIGR01271 739 ERKFSLVPEDEQGEESLPRGNQYHHGLQHQAQRRQSVLQLMTHSNR---GENRREQLQTSFRKKSSITQQNeLASELDIY 815
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 795 TRRLSRDSVLDITDEINEEDLKVCE**********TTWNTYFRYVTIHKNLIFVLILCVTVFLIEVAASLAGLWFLKKTA 874
Cdd:TIGR01271 816 SRRLSKDSVYEISEEINEEDLKECFADERENVFETTTWNTYLRYITTNRNLVFVLIFCLVIFLAEVAASLLGLWLITDNP 895
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 875 LKANATQSENSTSDKP----PVIVTDTSAYYIIYIYVGVADTLLAMGIFRGLPLVHTLITVSKTLHQKMVHAVLHAPMST 950
Cdd:TIGR01271 896 SAPNYVDQQHANASSPdvqkPVIITPTSAYYIFYIYVGTADSVLALGFFRGLPLVHTLLTVSKRLHEQMLHSVLQAPMAV 975
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 951 FNSWKAGGMLNRFAKDTAVLDDLLPLTVFDFVQLILIVIGAITVVSILQPYIFLASVPVIAAFIVLRAYFLHTSQQLKQL 1030
Cdd:TIGR01271 976 LNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQL 1055
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1031 ESEARSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEIIFVVFFVAVAFISIITTG 1110
Cdd:TIGR01271 1056 ESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDIIFVFFFIAVTFIAIGTNQ 1135
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1111 DGPGRVGIILTLAMNIMGTLQWAVNSSIDVDSLMRSVGRIFKFIDMPTEEMKNIKPQKKNQLSDALVIENRHAKEEknWP 1190
Cdd:TIGR01271 1136 DGEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEPRPSGGGGKYQLSTVLVIENPHAQKC--WP 1213
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1191 SGGKMTVKDLTAKYGEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLNTEGDIQIDGVSWNTVSVQQWRKA 1270
Cdd:TIGR01271 1214 SGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDGVSWNSVTLQTWRKA 1293
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1271 FGVIPQKVFIFSGTFRMNLDPYGQWNDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSRAK 1350
Cdd:TIGR01271 1294 FGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAK 1373
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1351 ILLLDEPSAHLDPVTSQVIRKTLKHAFANCTVILSEHRLEAMLECQRFLVIEDNKLRQYESIQKLLNEKSSFRQAISHAD 1430
Cdd:TIGR01271 1374 ILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAMSAAD 1453
|
1450 1460
....*....|....*....|....
gi 1631900066 1431 RLKLLPVHHRNSSKRKPRPKITAL 1454
Cdd:TIGR01271 1454 RLKLFPLHRRNSSKRKPQPKITAL 1477
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
372-653 |
0e+00 |
|
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: 580.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 372 TTGVELDKVTAFWDEGIGELFVQANQENNNSKAPSTDNNLFFSNFPLHASPVLQDINFRIEKGQLLAVSGSTGAGKTSLL 451
Cdd:cd03291 1 TTGVIMENVTAFWDEGFGELLEKAKQENNDRKHSSDDNNLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 452 MMIMGELEPSQGKIKHSGRISFSPQVSWIMPGTIKENIIFGVSYDEYRYKSVIKACQLEEDISKFPEKDYTVLGEGGIIL 531
Cdd:cd03291 81 MLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 532 SGGQRARISLARAVYKDADLYLLDSPFGHLDIFTEKEIFESCVCKLMANKTRILVTSKLEHLKIADKILILHEGSCYFYG 611
Cdd:cd03291 161 SGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYG 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1631900066 612 TFSELQGQRPDFSSELMGFDSFDQFSAERRNSILTETLRRFS 653
Cdd:cd03291 241 TFSELQSLRPDFSSKLMGYDTFDQFSAERRNSILTETLRRFS 282
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
830-1154 |
0e+00 |
|
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: 568.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 830 TTWNTYFRYVTIHKNLIFVLILCVTVFLIEVAASLAGLWFLKKTALkANATQSENSTSDKPPVIVTDTSAYYIIYIYVGV 909
Cdd:cd18600 1 TTWNTYLRYITSHKSLIFVLILCLVIFAIEVAASLVGLWLLRSQAD-RVNTTRPESSSNTYAVIVTFTSSYYVFYIYVGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 910 ADTLLAMGIFRGLPLVHTLITVSKTLHQKMVHAVLHAPMSTFNSWKAGGMLNRFAKDTAVLDDLLPLTVFDFVQLILIVI 989
Cdd:cd18600 80 ADSLLAMGFFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 990 GAITVVSILQPYIFLASVPVIAAFIVLRAYFLHTSQQLKQLESEARSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKAL 1069
Cdd:cd18600 160 GAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1070 NLHTANWFLYLSTLRWFQMRIEIIFVVFFVAVAFISIITTGDGPGRVGIILTLAMNIMGTLQWAVNSSIDVDSLMRSVGR 1149
Cdd:cd18600 240 NLHTANWFLYLSTLRWFQMRIEMIFVIFFTAVTFISIGTTGDGEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVSR 319
|
....*
gi 1631900066 1150 IFKFI 1154
Cdd:cd18600 320 IFKFI 324
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1193-1454 |
1.40e-175 |
|
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: 524.42 E-value: 1.40e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1193 GKMTVKDLTAKYGEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLNTEGDIQIDGVSWNTVSVQQWRKAFG 1272
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVPLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1273 VIPQKVFIFSGTFRMNLDPYGQWNDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSRAKIL 1352
Cdd:cd03289 81 VIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1353 LLDEPSAHLDPVTSQVIRKTLKHAFANCTVILSEHRLEAMLECQRFLVIEDNKLRQYESIQKLLNEKSSFRQAISHADRL 1432
Cdd:cd03289 161 LLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAISPSDRL 240
|
250 260
....*....|....*....|..
gi 1631900066 1433 KLLPVHHRNSSKRKPRPKITAL 1454
Cdd:cd03289 241 KLFPRRNSSKSKRKPRPQIQAL 262
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1-1422 |
4.59e-164 |
|
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: 534.53 E-value: 4.59e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1 WTKPILKKGYRRRLELSDIYQIPSADSADNLSEKLEREWDRELATSKK-------------------------------- 48
Cdd:TIGR00957 217 WITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPVLVENWKKECKKTRKqpvsavygkkdpskpkgssqldaneevealiv 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 49 -------KPKLINALRRCFFWKFMFYGIILYLGEVTKSVQPLLLGRIIASY-DPDNSDERsiAYYLGIGLCLLFLVRTLL 120
Cdd:TIGR00957 297 ksphkprKPSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFVnDPMAPDWQ--GYFYTGLLFVCACLQTLI 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 121 IHPAIFGLHHIGMQMRIAMFSLIYKKILKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLLWD 200
Cdd:TIGR00957 375 LHQYFHICFVSGMRIKTAVMGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 201 MLEASAFSGLAFLIVLAFFQAWLGQMMMKYRNKRAGKINERLVITSEIIENIQSVKAYCWEDAMEKMIESIRETELKLTR 280
Cdd:TIGR00957 455 NLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLK 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 281 KAAYVRYFNSSAFFFS--GFFVVFLAVLPYAVIKGII-LRKIFTTISFCIVLRMTVTrQFPGSVQTWYDSIGAINKIQDF 357
Cdd:TIGR00957 535 KSAYLHAVGTFTWVCTpfLVALITFAVYVTVDENNILdAEKAFVSLALFNILRFPLN-ILPMVISSIVQASVSLKRLRIF 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 358 LLKKEykaleynLTTTGVELDKVTAFWDEGIgelfvqanqennnskapsTDNNLFFSnFPLHASPVLQDINFRIEKGQLL 437
Cdd:TIGR00957 614 LSHEE-------LEPDSIERRTIKPGEGNSI------------------TVHNATFT-WARDLPPTLNGITFSIPEGALV 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 438 AVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGRISFSPQVSWIMPGTIKENIIFGVSYDEYRYKSVIKACQLEEDISKFP 517
Cdd:TIGR00957 668 AVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILP 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 518 EKDYTVLGEGGIILSGGQRARISLARAVYKDADLYLLDSPFGHLDIFTEKEIFESCVCK--LMANKTRILVTSKLEHLKI 595
Cdd:TIGR00957 748 SGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPegVLKNKTRILVTHGISYLPQ 827
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 596 ADKILILHEGSCYFYGTFSELQgqrpdfsselmgfdsfdqfsaeRRNSILTETLRRFSiegegmgsrneikkqSFKQTSD 675
Cdd:TIGR00957 828 VDVIIVMSGGKISEMGSYQELL----------------------QRDGAFAEFLRTYA---------------PDEQQGH 870
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 676 FNDKRKSSIiinplnanrkfSVVQKNGMQVgvEDGhndpperrlslipdleqgdvgllrsnMLSTDHMLQSRRRQSvlnl 755
Cdd:TIGR00957 871 LEDSWTALV-----------SGEGKEAKLI--ENG--------------------------MLVTDVVGKQLQRQL---- 907
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 756 mtgTSSVSYGPNVSkkgsttfrkmsmvpqtnlaseidiytRRLSRDSVLDITdEINEEDLKVCE**********TT--WN 833
Cdd:TIGR00957 908 ---SASSSDSGDQS--------------------------RHHGSSAELQKA-EAKEETWKLMEADKAQTGQVELSvyWD 957
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 834 tYFRYVTIhknliFVLILCVTVFLIEVAASLAGLWFLKKTALKANATQSENSTSDKppvivtdTSAYYIIYIYVGVADTL 913
Cdd:TIGR00957 958 -YMKAIGL-----FITFLSIFLFVCNHVSALASNYWLSLWTDDPMVNGTQNNTSLR-------LSVYGALGILQGFAVFG 1024
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 914 LAMGIFRGLplvhtlITVSKTLHQKMVHAVLHAPMSTFNSWKAGGMLNRFAKDTAVLDDLLPLTVFDFVQLILIVIGAIT 993
Cdd:TIGR00957 1025 YSMAVSIGG------IQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALI 1098
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 994 VVSILQPYIFLASVPVIAAFIVLRAYFLHTSQQLKQLESEARSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHT 1073
Cdd:TIGR00957 1099 VILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQ 1178
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1074 ANWFLYLSTLRWFQMRIEIIFVVFFVAVAFISIITTGD-GPGRVGIILTLAMNIMGTLQWAVNSSIDVDSLMRSVGRIFK 1152
Cdd:TIGR00957 1179 KAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSlSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKE 1258
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1153 FIDMPTEEmknikpqkknqlsdALVIENRHAKEekNWPSGGKMTVKDLTAKYGEGGAAVLENISFSIDSGQRVGLLGRTG 1232
Cdd:TIGR00957 1259 YSETEKEA--------------PWQIQETAPPS--GWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTG 1322
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1233 SGKSTLLFAFLRLLNT-EGDIQIDGVSWNTVSVQQWRKAFGVIPQKVFIFSGTFRMNLDPYGQWNDEEIWKVAEEVGLKS 1311
Cdd:TIGR00957 1323 AGKSSLTLGLFRINESaEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKT 1402
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1312 VIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFANCTVILSEHRLEA 1391
Cdd:TIGR00957 1403 FVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNT 1482
|
1450 1460 1470
....*....|....*....|....*....|.
gi 1631900066 1392 MLECQRFLVIEDNKLRQYESIQKLLNEKSSF 1422
Cdd:TIGR00957 1483 IMDYTRVIVLDKGEVAEFGAPSNLLQQRGIF 1513
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-1422 |
6.81e-155 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 508.75 E-value: 6.81e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1 WTKPILKKGYRRRLELSDIYQIPSADSADNLSEKLEREWDRElaTSKKKPKLINALRRCFFWKFMFYGIILYLGEVTKSV 80
Cdd:PLN03232 242 WMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWTEE--SRRPKPWLLRALNNSLGGRFWLGGIFKIGHDLSQFV 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 81 QPLLLGRIIASYDPDNSDERSIAYYLGIGLCLLFLVrtlLIHPAIF-GLHHIGMQMRIAMFSLIYKKILKLSSRVLDKIS 159
Cdd:PLN03232 320 GPVILSHLLQSMQEGDPAWVGYVYAFLIFFGVTFGV---LCESQYFqNVGRVGFRLRSTLVAAIFHKSLRLTHEARKNFA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 160 TGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLLWDMLEASAFSGLAFLIVLAFFQAWLGQMMMKYRNKRAGKIN 239
Cdd:PLN03232 397 SGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTD 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 240 ERLVITSEIIENIQSVKAYCWEDAMEKMIESIRETELKLTRKAAYVRYFNSSAFFFSGFFVVFLAVLPYAVIKG-IILRK 318
Cdd:PLN03232 477 KRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLVSFGVFVLLGGdLTPAR 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 319 IFTTISFCIVLRMTVTrQFPGSVQTWYDSIGAINKIQDFLLKKEykaleynltttgveldkvtafwdegigELFVQANQE 398
Cdd:PLN03232 557 AFTSLSLFAVLRSPLN-MLPNLLSQVVNANVSLQRIEELLLSEE---------------------------RILAQNPPL 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 399 NNNSKAPSTDNNLFFSNFPLhASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQ-GKIKHSGRISFSPQV 477
Cdd:PLN03232 609 QPGAPAISIKNGYFSWDSKT-SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtSSVVIRGSVAYVPQV 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 478 SWIMPGTIKENIIFGVSYDEYRYKSVIKACQLEEDISKFPEKDYTVLGEGGIILSGGQRARISLARAVYKDADLYLLDSP 557
Cdd:PLN03232 688 SWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDP 767
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 558 FGHLDIFTEKEIFESCVCKLMANKTRILVTSKLEHLKIADKILILHEGSCYFYGTFSELQgqrpdfsselmgfdsfdqfs 637
Cdd:PLN03232 768 LSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELS-------------------- 827
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 638 aerRNSILTETLRrfsiegEGMGSRNEikKQSFKQTSDFNDKRKSSIIINPlnANRKFSVVQkngmqvgvedghndpper 717
Cdd:PLN03232 828 ---KSGSLFKKLM------ENAGKMDA--TQEVNTNDENILKLGPTVTIDV--SERNLGSTK------------------ 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 718 rlslipdleqgdvgllrsnmlstdhmlQSRRRQSVLnlmtgtssvsygpnvskkgsttfrkmsmvpqtnlaseidiytrr 797
Cdd:PLN03232 877 ---------------------------QGKRGRSVL-------------------------------------------- 885
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 798 lsrdsvldITDEINEEDLkvce**********TTWNTYFRYVTIHKNLIFVLILCVTVFLIEVAASLAGLWFlkktalka 877
Cdd:PLN03232 886 --------VKQEERETGI--------------ISWNVLMRYNKAVGGLWVVMILLVCYLTTEVLRVSSSTWL-------- 935
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 878 nATQSENSTSDkppvivtDTSAYYIIYIYVGVADTLLAMGIFRGLPLVHTLITVSKTLHQKMVHAVLHAPMSTFNSWKAG 957
Cdd:PLN03232 936 -SIWTDQSTPK-------SYSPGFYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTG 1007
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 958 GMLNRFAKDTAVLDDLLPLTVFDFVQLILIVIGAITVVSILQPYIFLASVPVIAAFIVLRAYFLHTSQQLKQLESEARSP 1037
Cdd:PLN03232 1008 RVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSP 1087
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1038 IFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEIIFVVFFVAVAFISIITTGDGPGRV- 1116
Cdd:PLN03232 1088 IYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLRNGNAENQAg 1167
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1117 -----GIILTLAMNIMGTLQWAVNSSIDVDSLMRSVGRIFKFIDMPTEemknikpqkknqlSDALVIENRHAKeekNWPS 1191
Cdd:PLN03232 1168 fastmGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSE-------------ATAIIENNRPVS---GWPS 1231
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1192 GGKMTVKDLTAKYGEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLNTE-GDIQIDGVSWNTVSVQQWRKA 1270
Cdd:PLN03232 1232 RGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEkGRIMIDDCDVAKFGLTDLRRV 1311
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1271 FGVIPQKVFIFSGTFRMNLDPYGQWNDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSRAK 1350
Cdd:PLN03232 1312 LSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSK 1391
|
1370 1380 1390 1400 1410 1420 1430
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1631900066 1351 ILLLDEPSAHLDPVTSQVIRKTLKHAFANCTVILSEHRLEAMLECQRFLVIEDNKLRQYESIQKLL-NEKSSF 1422
Cdd:PLN03232 1392 ILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLsRDTSAF 1464
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1-1422 |
1.33e-145 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 485.78 E-value: 1.33e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1 WTKPILKKGYRRRLELSDIYQIPSADSADNLSEKLEREWDRELatSKKKPKLINALRRCFFWKFMFYGIILYLGEVTKSV 80
Cdd:PLN03130 242 WMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEEL--KKPKPWLLRALNNSLGGRFWLGGFFKIGNDLSQFV 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 81 QPLLLGRIIASYDPDNSDERSIAYYLGIGLCLLFLVrtlLIHPAIF-GLHHIGMQMRIAMFSLIYKKILKLSSRVLDKIS 159
Cdd:PLN03130 320 GPLLLNLLLESMQNGEPAWIGYIYAFSIFVGVVLGV---LCEAQYFqNVMRVGFRLRSTLVAAVFRKSLRLTHEGRKKFT 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 160 TGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLLWDMLEASAFSGLAFLIVLAFFQAWLGQMMMKYRNKRAGKIN 239
Cdd:PLN03130 397 SGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIGSLMLVLMFPIQTFIISKMQKLTKEGLQRTD 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 240 ERLVITSEIIENIQSVKAYCWEDAMEKMIESIRETELKLTRKAAYVRYFNSSAFFFSGFFVVFLAVLPYAVIKGIIL-RK 318
Cdd:PLN03130 477 KRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSFILNSIPVLVTVVSFGVFTLLGGDLTpAR 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 319 IFTTISFCIVLRMTVTrQFPGSVQTWYDSIGAINKIQDFLLKKEyKALEYNLTttgveldkvtafwdegigelfVQANQe 398
Cdd:PLN03130 557 AFTSLSLFAVLRFPLF-MLPNLITQAVNANVSLKRLEELLLAEE-RVLLPNPP---------------------LEPGL- 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 399 nnnsKAPSTDNNlFFSNFPLHASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEP-SQGKIKHSGRISFSPQV 477
Cdd:PLN03130 613 ----PAISIKNG-YFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVIRGTVAYVPQV 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 478 SWIMPGTIKENIIFGVSYDEYRYKSVIKACQLEEDISKFPEKDYTVLGEGGIILSGGQRARISLARAVYKDADLYLLDSP 557
Cdd:PLN03130 688 SWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDP 767
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 558 FGHLDIFTEKEIFESCVCKLMANKTRILVTSKLEHLKIADKILILHEGSCYFYGTFSELQGQRPDFSsELMgfdsfdqfs 637
Cdd:PLN03130 768 LSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQ-KLM--------- 837
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 638 aerrnsiltetlrrfsiegEGMGSRNEIKKQSFkqtsDFNDKRKSSIIInplnANRKFSVVQKNGmqvgvedGHNDPPER 717
Cdd:PLN03130 838 -------------------ENAGKMEEYVEENG----EEEDDQTSSKPV----ANGNANNLKKDS-------SSKKKSKE 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 718 RLSLIPDLEQGDVGLLRSNMLStdhmlqsrRRQsvlNLMTGTSSVSygpnvskkgsttfrkmsMVPQTNLASEidiyTRR 797
Cdd:PLN03130 884 GKSVLIKQEERETGVVSWKVLE--------RYK---NALGGAWVVM-----------------ILFLCYVLTE----VFR 931
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 798 LSRDSVLDI-TDEINEEdlkvce**********ttwntyfryvtIHKNLIFVLILcvtvflievaaslAGLWFLKktalk 876
Cdd:PLN03130 932 VSSSTWLSEwTDQGTPK---------------------------THGPLFYNLIY-------------ALLSFGQ----- 966
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 877 anatqsenstsdkppVIVTDTSAYYiiyiyvgvadtllamgifrglpLVHTLITVSKTLHQKMVHAVLHAPMSTFNSWKA 956
Cdd:PLN03130 967 ---------------VLVTLLNSYW----------------------LIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPL 1009
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 957 GGMLNRFAKDTAVLDDLLPLTVFDFV----QLI--LIVIGAITVVSILqpyiflASVPVIAAFIVLRAYFLHTSQQLKQL 1030
Cdd:PLN03130 1010 GRIINRFAKDLGDIDRNVAVFVNMFLgqifQLLstFVLIGIVSTISLW------AIMPLLVLFYGAYLYYQSTAREVKRL 1083
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1031 ESEARSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEIIFVVFFVAVAFISIITTG 1110
Cdd:PLN03130 1084 DSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTLVNMSSNRWLAIRLETLGGLMIWLTASFAVMQNG 1163
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1111 DGPGRV------GIILTLAMNIMGTLQWAVNSSIDVDSLMRSVGRIFKFIDMPTEEmknikpqkknqlsdALVIENRhaK 1184
Cdd:PLN03130 1164 RAENQAafastmGLLLSYALNITSLLTAVLRLASLAENSLNAVERVGTYIDLPSEA--------------PLVIENN--R 1227
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1185 EEKNWPSGGKMTVKDLTAKYGEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLNTE-GDIQIDGVSWNTVS 1263
Cdd:PLN03130 1228 PPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELErGRILIDGCDISKFG 1307
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1264 VQQWRKAFGVIPQKVFIFSGTFRMNLDPYGQWNDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLAR 1343
Cdd:PLN03130 1308 LMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLAR 1387
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1344 SVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFANCTVILSEHRLEAMLECQRFLVIEDNKLRQYESIQKLL-NEKSSF 1422
Cdd:PLN03130 1388 ALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLsNEGSAF 1467
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
66-355 |
2.35e-129 |
|
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 1 (TMD1) of the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), which belongs to the ABCC subfamily. CFTR functions as a chloride channel, in contrast to other ABC transporters, and controls ion and water secretion and absorption in epithelial tissues. ABC proteins are formed from two homologous halves each containing a transmembrane domain (TMD) and a cytosolic nucleotide binding domain (NBD). In CFTR, these two TMD-NBD halves are linked by the unique regulatory (R) domain, which is not present in other ABC transporters. The ion channel only opens when its R-domain is phosphorylated by cyclic AMP-dependent protein kinase (PKA) and ATP is bound at the NBDs. Mutations in CFTR cause cystic fibrosis, the most common lethal genetic disorder in populations of Northern European descent.
Pssm-ID: 350038 [Multi-domain] Cd Length: 291 Bit Score: 402.40 E-value: 2.35e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 66 FYGIILYLGEVTKSVQPLLLGRIIASYDPDNSDERSIAYYLGIGLCLLFLVRTLLIHPAIFGLHHIGMQMRIAMFSLIYK 145
Cdd:cd18594 1 LLGILLFLEESLKIVQPLLLGRLVAYFVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 146 KILKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLLWDMLEASAFSGLAFLIVLAFFQAWLGQ 225
Cdd:cd18594 81 KTLKLSSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 226 MMMKYRNKRAGKINERLVITSEIIENIQSVKAYCWEDAMEKMIESIRETELKLTRKAAYVRYFNSSAFFFSGFFVVFLAV 305
Cdd:cd18594 161 LFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 306 LPYAVIKGII-LRKIFTTISFCIVLRMTVTRQFPGSVQTWYDSIGAINKIQ 355
Cdd:cd18594 241 VPYVLTGNTLtARKVFTVISLLNALRMTITRFFPESIQTLSESRVSLKRIQ 291
|
|
| CFTR_R |
pfam14396 |
Cystic fibrosis TM conductance regulator (CFTR), regulator domain; |
622-835 |
1.12e-121 |
|
Cystic fibrosis TM conductance regulator (CFTR), regulator domain;
Pssm-ID: 464164 Cd Length: 213 Bit Score: 378.31 E-value: 1.12e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 622 DFSSELMGFDSFDQFSAERRNSILTETLRRFSIEGEGMGSRNEIKKQSFKQTSDFNDKRKSSIIINPLNANRKFSVVQKN 701
Cdd:pfam14396 1 DFSSLLMGLEAFDNFSAERRNSILTETLRRFSVDEDAGGSRNEPKKQSFKQTDDFNEKRKNSVILNPLAASRKFSIIQKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 702 GMQV-GVEDGHNDPPERRLSLIPDLEQGDVGLLRSNMLSTDHMLQSRRRQSVLNLMTGTssVSYGPNVSKKGSTTFRKMS 780
Cdd:pfam14396 81 QLQMnGIEEGLSELPERRLSLVPESEQGEAALPRSNVLNTGPTLQGQRRQSVLALMTNT--VAQGQGRREKGQSSFRKMS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1631900066 781 MVPQTNLASEIDIYTRRLSRDSVLDITDEINEEDLKVCE**********TTWNTY 835
Cdd:pfam14396 159 VVPQSNLASELDIYARRLSKDSVLDITEEINEEDLKECFADDIENVFETTTWNTY 213
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
52-1423 |
3.14e-121 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 415.72 E-value: 3.14e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 52 LINALRRCFFWKFMFygiiLYLGEVTKSVQPLLLGRIIASYDPDNSderSIAYylGIGLCLLFLVRTLLIHPAIFGLHHI 131
Cdd:PTZ00243 238 LFAALPYYVWWQIPF----KLLSDVCTLTLPVLLKYFVKFLDADNA---TWGR--GLGLVLTLFLTQLIQSVCLHRFYYI 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 132 ----GMQMRIAMFSLIYKKILKLSSRVLDK--ISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLLWDMLEAS 205
Cdd:PTZ00243 309 sircGLQYRSALNALIFEKCFTISSKSLAQpdMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWC 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 206 AFSGLAFLIVLAFFQAWLGQMMMKYRNKRAGKINERLVITSEIIENIQSVKAYCWEDAMEKMIESIRETELKLTRKAAYV 285
Cdd:PTZ00243 389 ALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQLA 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 286 RYFNSSAFFFSGFFVVFLAVLPYAVIkGIILRK--IFTTISFCIVLRMTVtRQFPGSVQTWYDSIGAINKIQDFLL---- 359
Cdd:PTZ00243 469 RVATSFVNNATPTLMIAVVFTVYYLL-GHELTPevVFPTIALLGVLRMPF-FMIPWVFTTVLQFLVSIKRISTFLEcdna 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 360 -------KKEYKALEYNLTTTG-----VELDKVTAFW------------------------------------------- 384
Cdd:PTZ00243 547 tcstvqdMEEYWREQREHSTACqlaavLENVDVTAFVpvklprapkvktsllsralrmlcceqcrptkrhpspsvvvedt 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 385 -------------DEGIGELFVQANQENNNSKAPSTDNNLFFSnfpLHASPVLQDINFRIEKGQLLAVSGSTGAGKTSLL 451
Cdd:PTZ00243 627 dygspssasrhivEGGTGGGHEATPTSERSAKTPKMKTDDFFE---LEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLL 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 452 MMIMGELEPSQGKIKHSGRISFSPQVSWIMPGTIKENIIFGVSYDEYRYKSVIKACQLEEDISKFPEKDYTVLGEGGIIL 531
Cdd:PTZ00243 704 QSLLSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNL 783
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 532 SGGQRARISLARAVYKDADLYLLDSPFGHLDIFTEKEIFESCVCKLMANKTRILVTSKLEHLKIADKILILHEGSCYFYG 611
Cdd:PTZ00243 784 SGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSG 863
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 612 TfselqgqrpdfsselmgfdsfdqfSAERRNSILTETLRrfsieGEGMGSRNEIKKQSFKQTSDFNDKRKSSIIINPlna 691
Cdd:PTZ00243 864 S------------------------SADFMRTSLYATLA-----AELKENKDSKEGDADAEVAEVDAAPGGAVDHEP--- 911
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 692 nrkfSVVQKNGMQVGVEDGHNDPPERRLSLipdLEQGDVGllrsnmlstdhmlqsrrrqsvlnlmtgtssvsygpnvskk 771
Cdd:PTZ00243 912 ----PVAKQEGNAEGGDGAALDAAAGRLMT---REEKASG---------------------------------------- 944
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 772 gsttfrkmsMVPqtnlaseidiytrrlsrdsvlditdeineedlkvce**********ttWNTYFRYVTIHKNLIFVLIL 851
Cdd:PTZ00243 945 ---------SVP------------------------------------------------WSTYVAYLRFCGGLHAAGFV 967
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 852 CVTVFLIEVAASLAGLWflkktaLKANATQSEnstsdkppvivtDTSAYYIIYIYVGVadtlLAMGIFrGLPL-----VH 926
Cdd:PTZ00243 968 LATFAVTELVTVSSGVW------LSMWSTRSF------------KLSAATYLYVYLGI----VLLGTF-SVPLrfflsYE 1024
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 927 TLITVSKTLHQKMVHAVLHAPMSTFNSWKAGGMLNRFAKDTAVLDDLLPLTVFDFVQLILIVIGAITVVSILQPYIFLAS 1006
Cdd:PTZ00243 1025 AMRRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVAL 1104
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1007 VPVIAAFIVLRAYFLHTSQQLKQLESEARSPIFTHLVTSLKGLWTLRAFGRQpyfETLFHKALN----LHTANwFLYLST 1082
Cdd:PTZ00243 1105 VPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKA---HLVMQEALRrldvVYSCS-YLENVA 1180
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1083 LRWFQMRIEIIFVVFFVAVAFISIITTGDGPGR--VGII---LTLAMNIMGTLQWAVNSSIDVDSLMRSVGRIFKFID-M 1156
Cdd:PTZ00243 1181 NRWLGVRVEFLSNIVVTVIALIGVIGTMLRATSqeIGLVslsLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTDeV 1260
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1157 PTEEMKNIKpqkknQLSDALVIENRHAKE-------EKNWPSG--------GKMTVKDLTAKYGEGGAAVLENISFSIDS 1221
Cdd:PTZ00243 1261 PHEDMPELD-----EEVDALERRTGMAADvtgtvviEPASPTSaaphpvqaGSLVFEGVQMRYREGLPLVLRGVSFRIAP 1335
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1222 GQRVGLLGRTGSGKSTLLFAFLRLLNT-EGDIQIDGVSWNTVSVQQWRKAFGVIPQKVFIFSGTFRMNLDPYGQWNDEEI 1300
Cdd:PTZ00243 1336 REKVGIVGRTGSGKSTLLLTFMRMVEVcGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEV 1415
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1301 WKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSR-AKILLLDEPSAHLDPVTSQVIRKTLKHAFAN 1379
Cdd:PTZ00243 1416 WAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKgSGFILMDEATANIDPALDRQIQATVMSAFSA 1495
|
1450 1460 1470 1480
....*....|....*....|....*....|....*....|....*
gi 1631900066 1380 CTVILSEHRLEAMLECQRFLVIEDNKLRQYESIQKL-LNEKSSFR 1423
Cdd:PTZ00243 1496 YTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFH 1540
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1193-1411 |
2.40e-92 |
|
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: 297.48 E-value: 2.40e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1193 GKMTVKDLTAKYGEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLL-NTEGDIQIDGVSWNTVSVQQWRKAF 1271
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVeLSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1272 GVIPQKVFIFSGTFRMNLDPYGQWNDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSRAKI 1351
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1352 LLLDEPSAHLDPVTSQVIRKTLKHAFANCTVILSEHRLEAMLECQRFLVIEDNKLRQYES 1411
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
417-606 |
9.03e-92 |
|
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: 295.15 E-value: 9.03e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 417 PLHASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGRISFSPQVSWIMPGTIKENIIFGVSYD 496
Cdd:cd03250 14 EQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNGTIRENILFGKPFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 497 EYRYKSVIKACQLEEDISKFPEKDYTVLGEGGIILSGGQRARISLARAVYKDADLYLLDSPFGHLDIFTEKEIFESCVCK 576
Cdd:cd03250 94 EERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILG 173
|
170 180 190
....*....|....*....|....*....|.
gi 1631900066 577 -LMANKTRILVTSKLEHLKIADKILILHEGS 606
Cdd:cd03250 174 lLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
831-1424 |
2.26e-77 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 268.19 E-value: 2.26e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 831 TWNTYFRYVTIHKNLIFVLILCVtvfLIEVAASLAGLWFLKKTALKANATQsenstsdkppvivtDTSA-YYIIYIYVGV 909
Cdd:COG1132 8 LLRRLLRYLRPYRGLLILALLLL---LLSALLELLLPLLLGRIIDALLAGG--------------DLSAlLLLLLLLLGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 910 ADTLLAMGIFRGLPLVHTLITVSKTLHQKMVHAVLHAPMSTFNSWKAGGMLNRFAKDTAVLDDLLPLTVFDFVQLILIVI 989
Cdd:COG1132 71 ALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 990 GAITVVSILQPYIFLASVPVIAAFIVLRAYFLHTSQQLKQLESEARSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKAL 1069
Cdd:COG1132 151 GALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREAN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1070 NLHTANWFLYLSTLRWFQMRIEIIFVVFFVAVAFISIITTGDG---PGRVGIILTLAMNIMGTLQWAVNSSIDVDSLMRS 1146
Cdd:COG1132 231 EELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGsltVGDLVAFILYLLRLFGPLRQLANVLNQLQRALAS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1147 VGRIFKFIDMPTEemknikpqkknqlsdalVIENRHAKEEKnwPSGGKMTVKDLTAKYGeGGAAVLENISFSIDSGQRVG 1226
Cdd:COG1132 311 AERIFELLDEPPE-----------------IPDPPGAVPLP--PVRGEIEFENVSFSYP-GDRPVLKDISLTIPPGETVA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1227 LLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSVQQWRKAFGVIPQKVFIFSGTFRMNLDpYGQWN--DEEIWKV 1303
Cdd:COG1132 371 LVGPSGSGKSTLVNLLLRFYDpTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIR-YGRPDatDEEVEEA 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1304 AEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFANCTVI 1383
Cdd:COG1132 450 AKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTI 529
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1631900066 1384 LSEHRLEAMLECQRFLVIEDNKLRQYESIQKLLNEKSSFRQ 1424
Cdd:COG1132 530 VIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYAR 570
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
846-1150 |
7.10e-75 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350045 [Multi-domain] Cd Length: 314 Bit Score: 251.86 E-value: 7.10e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 846 IFVLILCVTVFLIEVAASLAGLWFL---KKTALKANATQSENSTSDKPPVIVTDTSAYYIIYIYVGVADTLLAMGIFRGL 922
Cdd:cd18601 2 VFVFILLVLLNIAAQVLYVLSDWWLsywANLEEKLNDTTDRVQGENSTNVDIEDLDRDFNLGIYAGLTAATFVFGFLRSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 923 PLVHTLITVSKTLHQKMVHAVLHAPMSTFNSWKAGGMLNRFAKDTAVLDDLLPLTVFDFVQLILIVIGAITVVSILQPYI 1002
Cdd:cd18601 82 LFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPWV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1003 FLASVPVIAAFIVLRAYFLHTSQQLKQLESEARSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLST 1082
Cdd:cd18601 162 LIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFLAT 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1631900066 1083 LRWFQMRIEIIFVVFFVAVAFISIITTGD-GPGRVGIILTLAMNIMGTLQWAVNSSIDVDSLMRSVGRI 1150
Cdd:cd18601 242 SRWLAVRLDALCALFVTVVAFGSLFLAESlDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERV 310
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
845-1154 |
6.72e-72 |
|
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: 242.41 E-value: 6.72e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 845 LIFVLILCVTVFLIEVAASLAGLWFLKKTALKANatqsenstsdkppvivtDTSAYYIIYIYVGVADTLLAMGIFRGLPL 924
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPN-----------------SSSGYYLGVYAALLVLASVLLVLLRWLLF 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 925 VHTLITVSKTLHQKMVHAVLHAPMSTFNSWKAGGMLNRFAKDTAVLDDLLPLTVFDFVQLILIVIGAITVVSILQPYIFL 1004
Cdd:cd18580 64 VLAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1005 ASVPVIAAFIVLRAYFLHTSQQLKQLESEARSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLR 1084
Cdd:cd18580 144 VLPPLLVVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQR 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 1085 WFQMRIEIIFVVFFVAVAFISIITTGD-GPGRVGIILTLAMNIMGTLQWAVNSSIDVDSLMRSVGRIFKFI 1154
Cdd:cd18580 224 WLGLRLDLLGALLALVVALLAVLLRSSiSAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
66-354 |
2.67e-69 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350037 [Multi-domain] Cd Length: 291 Bit Score: 234.81 E-value: 2.67e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 66 FYGIILYLGEVTKSVQPLLLGRIIASYDPDNS-DERSIAYYLGIGLCLLFLVRTLLIHPAIFGLHHIGMQMRIAMFSLIY 144
Cdd:cd18593 1 LLGIFLFLEEAIRVVQPIFLGKLIRYFEGNGSsISLTEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSLIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 145 KKILKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLLWDMLEASAFSGLAFLIVLAFFQAWLG 224
Cdd:cd18593 81 RKALRLSQAALGKTTVGQIVNLLSNDVNRFDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 225 QMMMKYRNKRAGKINERLVITSEIIENIQSVKAYCWEDAMEKMIESIRETELKLTRKAAYVRYFNSSAFFFSGFFVVFLA 304
Cdd:cd18593 161 KLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFLT 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 305 VLPYAVIKGIIL-RKIFTTISFCIVLRMTVTRQFPGSVQTWYDSIGAINKI 354
Cdd:cd18593 241 FLAYILLGNILTaERVFVTMALYNAVRLTMTLFFPFAIQFGSELSVSIRRI 291
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
914-1424 |
3.18e-69 |
|
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: 248.21 E-value: 3.18e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 914 LAMGIFRGLPLVHTLITVSKTLHQKMVHAVLHAPMSTFNSWKAGGMLNRFaKDTAVLDDLLPLTVFDFVQLILIVIGAIT 993
Cdd:COG2274 210 GLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLI 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 994 VVSILQPYIFLASVPVIAAFIVLRAYFLHTSQQLKQLESEARSPIFTHLVTSLKGLWTLRAFGRQPYF----ETLFHKAL 1069
Cdd:COG2274 289 VLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFrrrwENLLAKYL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1070 NL-----HTANWFLYLSTLrwFQMrieiifvvffvavaFISIITTGdgpgrVGIILTLAMNI-MGTL------QWAVNSS 1137
Cdd:COG2274 369 NArfklrRLSNLLSTLSGL--LQQ--------------LATVALLW-----LGAYLVIDGQLtLGQLiafnilSGRFLAP 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1138 ID--VDSLMR------SVGRIFKFIDMPTEEMKNIKPQKKNQLSdalvienrhakeeknwpsgGKMTVKDLTAKYGEGGA 1209
Cdd:COG2274 428 VAqlIGLLQRfqdakiALERLDDILDLPPEREEGRSKLSLPRLK-------------------GDIELENVSFRYPGDSP 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1210 AVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLL-NTEGDIQIDGVSWNTVSVQQWRKAFGVIPQKVFIFSGTFRMN 1288
Cdd:COG2274 489 PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYePTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIREN 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1289 L---DPygQWNDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSRAKILLLDEPSAHLDPVT 1365
Cdd:COG2274 569 ItlgDP--DATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAET 646
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1631900066 1366 SQVIRKTLKHAFANCTVILSEHRLEAMLECQRFLVIEDNKLRQYESIQKLLNEKSSFRQ 1424
Cdd:COG2274 647 EAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAE 705
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
68-354 |
5.26e-68 |
|
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: 231.22 E-value: 5.26e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 68 GIILYLGEVTKSVQPLLLGRIIASYDPDNSDERSIAYYLGIGLCLLFLVRTLLIHPAIFGLHHIGMQMRIAMFSLIYKKI 147
Cdd:cd18579 3 GLLKLLEDLLSLAQPLLLGLLISYLSSYPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 148 LKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLLWDMLEASAFSGLAFLIVLAFFQAWLGQMM 227
Cdd:cd18579 83 LRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKLI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 228 MKYRNKRAGKINERLVITSEIIENIQSVKAYCWEDAMEKMIESIRETELKLTRKAAYVRYFNSSAFFFSGFFVVFLAVLP 307
Cdd:cd18579 163 SKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATFAT 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1631900066 308 YAVIKGII-LRKIFTTISFCIVLRMtVTRQFPGSVQTWYDSIGAINKI 354
Cdd:cd18579 243 YVLLGNPLtAAKVFTALSLFNLLRF-PLLMLPQAISSLIEALVSLKRI 289
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
954-1428 |
4.71e-64 |
|
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: 228.88 E-value: 4.71e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 954 WKAGGMLNRFAKDTAVLDDLLPLTVFDFVQLILIVIGAITVVSILQPYI--FLASVPVIAAFIV-LRAYFL--HTSQQLK 1028
Cdd:COG4987 109 LRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALalVLALGLLLAGLLLpLLAARLgrRAGRRLA 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1029 QLESEARspifTHLVTSLKGLWTLRAFGRQPYFEtlfhKALNLHTANWFLYLSTLRWFQMRIEIIFVVFFVAVAFISIIT 1108
Cdd:COG4987 189 AARAALR----ARLTDLLQGAAELAAYGALDRAL----ARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWL 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1109 TGD--GPGRVGIILtLAMNIMGTLqwavnSSIDV-----------DSLMRSVGRIFKFIDMPTEEmknikpqkknqlsda 1175
Cdd:COG4987 261 AAPlvAAGALSGPL-LALLVLAAL-----ALFEAlaplpaaaqhlGRVRAAARRLNELLDAPPAV--------------- 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1176 lvienRHAKEEKNWPSGGKMTVKDLTAKYGEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQI 1254
Cdd:COG4987 320 -----TEPAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDpQSGSITL 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1255 DGVSWNTVSVQQWRKAFGVIPQKVFIFSGTFRMNL---DPygQWNDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVL 1331
Cdd:COG4987 395 GGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLrlaRP--DATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRL 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1332 SHGHKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFANCTVILSEHRLEAMLECQRFLVIEDNKLRQYES 1411
Cdd:COG4987 473 SGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGT 552
|
490
....*....|....*..
gi 1631900066 1412 IQKLLNEKSSFRQAISH 1428
Cdd:COG4987 553 HEELLAQNGRYRQLYQR 569
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
46-605 |
2.43e-59 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 215.41 E-value: 2.43e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 46 SKKKPKLINALRRCF--FWKFMFYGIILYLGE-VTKSVQPLLLGRIIASYDpdNSDERSIAYYLGIGLCLLFLVRTLLIH 122
Cdd:COG1132 2 SKSPRKLLRRLLRYLrpYRGLLILALLLLLLSaLLELLLPLLLGRIIDALL--AGGDLSALLLLLLLLLGLALLRALLSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 123 PAIFGLHHIGMQMRIAMFSLIYKKILKLSSRVLDKISTGQLVSLLSNNLNKFDEGLA-LAHFVWIAPLQVALLMGLL--- 198
Cdd:COG1132 80 LQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAhGLPQLVRSVVTLIGALVVLfvi 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 199 -WDMLEASAFSGLAFLIVLAFFQAWLGQMMMKYRnKRAGKINERLVitsEIIENIQSVKAYCWEDAMEKMIESIRETELK 277
Cdd:COG1132 160 dWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQ-EALAELNGRLQ---ESLSGIRVVKAFGREERELERFREANEELRR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 278 LTRKAAYVRyFNSSAFFFSGFFVVFLAVLPYA---VIKGIIlrKIFTTISFCIVLRMTVT--RQFPGSVQTWYDSIGAIN 352
Cdd:COG1132 236 ANLRAARLS-ALFFPLMELLGNLGLALVLLVGgllVLSGSL--TVGDLVAFILYLLRLFGplRQLANVLNQLQRALASAE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 353 KIQDFL-----LKKEYKALEYNLTTTGVELDKVTAFWDEGigelfvqanqennnskapstdnnlffsnfplhaSPVLQDI 427
Cdd:COG1132 313 RIFELLdeppeIPDPPGAVPLPPVRGEIEFENVSFSYPGD---------------------------------RPVLKDI 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 428 NFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG-------------RISFSPQVSWIMPGTIKENIIFG-- 492
Cdd:COG1132 360 SLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGvdirdltleslrrQIGVVPQDTFLFSGTIRENIRYGrp 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 493 -VSYDEyryksVIKAC---QLEEDISKFPEKDYTVLGEGGIILSGGQRARISLARAVYKDADLYLLDSPFGHLDIFTEKE 568
Cdd:COG1132 440 dATDEE-----VEEAAkaaQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEAL 514
|
570 580 590
....*....|....*....|....*....|....*..
gi 1631900066 569 IFEScVCKLMANKTRILVTSKLEHLKIADKILILHEG 605
Cdd:COG1132 515 IQEA-LERLMKGRTTIVIAHRLSTIRNADRILVLDDG 550
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1189-1411 |
3.30e-58 |
|
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: 199.56 E-value: 3.30e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1189 WPSGGKMTVKDLTAKYGEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSVQQW 1267
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEaEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1268 RKAFGVIPQKVFIFSGTFRMNLDPYGQWNDEEIWKVAEevglksvieqfpgqldfvLVDGGCVLSHGHKQLMCLARSVLS 1347
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1631900066 1348 RAKILLLDEPSAHLDPVTSQVIRKTLKHAFANCTVILSEHRLEAMLECQRFLVIEDNKLRQYES 1411
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1149-1419 |
4.57e-53 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 196.52 E-value: 4.57e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1149 RIFKFIDMPTEEMknikpqkknqlsdalvienRHAKEEKNWPSGGKMTVKDLTAKYgEGGAAVLENISFSIDSGQRVGLL 1228
Cdd:COG4988 310 KIFALLDAPEPAA-------------------PAGTAPLPAAGPPSIELEDVSFSY-PGGRPALDGLSLTIPPGERVALV 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1229 GRTGSGKSTLLFAFLRLL-NTEGDIQIDGVSWNTVSVQQWRKAFGVIPQKVFIFSGTFRMNLDPYG-QWNDEEIWKVAEE 1306
Cdd:COG4988 370 GPSGAGKSTLLNLLLGFLpPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRpDASDEELEAALEA 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1307 VGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFANCTVILSE 1386
Cdd:COG4988 450 AGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILIT 529
|
250 260 270
....*....|....*....|....*....|...
gi 1631900066 1387 HRLEAMLECQRFLVIEDNKLRQYESIQKLLNEK 1419
Cdd:COG4988 530 HRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1195-1405 |
8.97e-52 |
|
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: 179.89 E-value: 8.97e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTAKYGEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLL-NTEGDIQIDGVSWNTVSVQQWRKAFGV 1273
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYdPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1274 IPQKVFIFSGTFRMNLdpygqwndeeiwkvaeevglksvieqfpgqldfvlvdggcvLSHGHKQLMCLARSVLSRAKILL 1353
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1631900066 1354 LDEPSAHLDPVTSQVIRKTLKHAFANCTVILSEHRLEAMLECQRFLVIEDNK 1405
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
106-623 |
1.43e-50 |
|
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: 191.97 E-value: 1.43e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 106 LGIGLCLLFLVRTLLIHPAIFGLHHIGMQMRIAMFSLIYKKILKLSSRVLDKISTGQLVSLLS--NNLNKFDEGLALAhf 183
Cdd:COG2274 198 LAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRdvESIREFLTGSLLT-- 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 184 VWIAPLQVALLMGLL----WDMLEASAFSGLAFLIVLAFFQAWLGQMMMKyRNKRAGKINERLVitsEIIENIQSVKAYC 259
Cdd:COG2274 276 ALLDLLFVLIFLIVLffysPPLALVVLLLIPLYVLLGLLFQPRLRRLSRE-ESEASAKRQSLLV---ETLRGIETIKALG 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 260 WEDAM----EKMIESIRETELKLTRKAAYVRYFNSSAFFFSGFFVVFLAVlpYAVIKGIIlrkifTT---ISFCIVLRMT 332
Cdd:COG2274 352 AESRFrrrwENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGA--YLVIDGQL-----TLgqlIAFNILSGRF 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 333 VTR--QFPGSVQTWYDSIGAINKIQDFLLKKeykaLEYNLTTTGVELDKVTafwdegiGELFVQanqennnskapstdnN 410
Cdd:COG2274 425 LAPvaQLIGLLQRFQDAKIALERLDDILDLP----PEREEGRSKLSLPRLK-------GDIELE---------------N 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 411 LFFSnFPLHASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG-------------RISFSPQV 477
Cdd:COG2274 479 VSFR-YPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlrqidpaslrrQIGVVLQD 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 478 SWIMPGTIKENIIFG---VSYDEyryksVIKACQ---LEEDISKFPEKDYTVLGEGGIILSGGQRARISLARAVYKDADL 551
Cdd:COG2274 558 VFLFSGTIRENITLGdpdATDEE-----IIEAARlagLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRI 632
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1631900066 552 YLLDSPFGHLDIFTEKEIFEScVCKLMANKTRILVTSKLEHLKIADKILILHEGSCYFYGTFSELQGQRPDF 623
Cdd:COG2274 633 LILDEATSALDAETEAIILEN-LRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLY 703
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
850-1150 |
3.54e-50 |
|
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: 179.97 E-value: 3.54e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 850 ILCVTVFLIEVAASLAGLWFLKKtalkanATQSENSTSDKPPvivTDTSAYYIIYIYVGVADTLLAMGIFRGLPLVHTLI 929
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGI------WASAYETSSALPP---SEVSVLYYLGIYALISLLSVLLGTLRYLLFFFGSL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 930 TVSKTLHQKMVHAVLHAPMSTFNSWKAGGMLNRFAKDTAVLDDLLPLTVFDFVQLILIVIGAITVVSILQPYIFLASVPV 1009
Cdd:cd18604 73 RASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1010 IAAFIVLRAYFLHTSQQLKQLESEARSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMR 1089
Cdd:cd18604 153 AALYVYIGRLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVR 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 1090 IEIIFVVFFVAVAFISIITTGDGPGRVGIILTLAMNIMGTLQWAVNSSIDVDSLMRSVGRI 1150
Cdd:cd18604 233 IDLLGALFSFATAALLVYGPGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERI 293
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1192-1431 |
2.74e-48 |
|
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: 173.17 E-value: 2.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1192 GGKMTVKDLTAKYGEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLNT-EGDIQIDGVSWNTVSVQQWRKA 1270
Cdd:cd03288 17 GGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIfDGKIVIDGIDISKLPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1271 FGVIPQKVFIFSGTFRMNLDPYGQWNDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSRAK 1350
Cdd:cd03288 97 LSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1351 ILLLDEPSAHLDPVTSQVIRKTLKHAFANCTVILSEHRLEAMLECQRFLVIEDNKLRQYESIQKLLNEKSSFRQAISHAD 1430
Cdd:cd03288 177 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVRTD 256
|
.
gi 1631900066 1431 R 1431
Cdd:cd03288 257 K 257
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
846-1154 |
3.95e-47 |
|
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: 171.98 E-value: 3.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 846 IFVLILCVTVFLIEVAASLAGLWFLK---------KTALKANATQSENSTSDKPpvivtDTSAYYIIYIYVGVADTLLam 916
Cdd:cd18599 2 YVVFLFVLLLFILSVGSTVFSDWWLSywlkqgsgnTTNNVDNSTVDSGNISDNP-----DLNFYQLVYGGSILVILLL-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 917 GIFRGLPLVHTLITVSKTLHQKMVHAVLHAPMSTFNSWKAGGMLNRFAKDTAVLDDLLPLTVFDFVQLILIVIGAITVVS 996
Cdd:cd18599 75 SLIRGFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 997 ILQPYIFLASVPVIAAFIVLRAYFLHTSQQLKQLESEARSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANW 1076
Cdd:cd18599 155 IVFPWFLIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAF 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1631900066 1077 FLYLSTLRWFQMRIEIIFVVFFVAVAFISIITTGD-GPGRVGIILTLAMNIMGTLQWAVNSSIDVDSLMRSVGRIFKFI 1154
Cdd:cd18599 235 FLFNCAMRWLAVRLDILAVLITLITALLVVLLKGSiSPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
80-619 |
1.37e-45 |
|
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: 174.18 E-value: 1.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 80 VQPLLLGRIIASYDPDNSDERSIAYYLGiGLCLLFLVRTLLIHPAIFGLHHIGMQMRIAMFSLIYKKILKLSSRVLDKIS 159
Cdd:COG4988 35 AQAWLLASLLAGLIIGGAPLSALLPLLG-LLLAVLLLRALLAWLRERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 160 TGQLVSLLSNNLNKFDEGLAL---AHFVW-IAPLqvALLMGLLWdmleASAFSGLAFLIVLA---FFQAWLGqmmmkyrn 232
Cdd:COG4988 114 TGELATLLTEGVEALDGYFARylpQLFLAaLVPL--LILVAVFP----LDWLSGLILLVTAPlipLFMILVG-------- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 233 KRAGKINER----LVITS----EIIENIQSVKAYcweDAMEKMIESIRETELKLtRKAAyvryfnssafffsgffvvfLA 304
Cdd:COG4988 180 KGAAKASRRqwraLARLSghflDRLRGLTTLKLF---GRAKAEAERIAEASEDF-RKRT-------------------MK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 305 VLPYAVIKGIILrKIFTTISFCIV--------LRMTVT------------------RQFPGSVQTWYDSIGAINKIQDFL 358
Cdd:COG4988 237 VLRVAFLSSAVL-EFFASLSIALVavyigfrlLGGSLTlfaalfvlllapefflplRDLGSFYHARANGIAAAEKIFALL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 359 LKKEYKALEYNLTTTG-----VELDKVTAFWDEGigelfvqanqennnskapstdnnlffsnfplhaSPVLQDINFRIEK 433
Cdd:COG4988 316 DAPEPAAPAGTAPLPAagppsIELEDVSFSYPGG---------------------------------RPALDGLSLTIPP 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 434 GQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG-------------RISFSPQVSWIMPGTIKENIIFG-VSYDEYR 499
Cdd:COG4988 363 GERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGvdlsdldpaswrrQIAWVPQNPYLFAGTIRENLRLGrPDASDEE 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 500 YKSVIKACQLEEDISKFPEKDYTVLGEGGIILSGGQRARISLARAVYKDADLYLLDSPFGHLDIFTEKEIFEScVCKLMA 579
Cdd:COG4988 443 LEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQA-LRRLAK 521
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1631900066 580 NKTRILVTSKLEHLKIADKILILHEGSCYFYGTFSELQGQ 619
Cdd:COG4988 522 GRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
850-1150 |
2.39e-45 |
|
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: 166.63 E-value: 2.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 850 ILCVTVFLIEVAASLAGLWFLKKTALKANATQSENSTSDKPPVivTDTSAYYIIYIYVGVADTLLAMGIFRGLPLVHTLI 929
Cdd:cd18602 2 ALVLALALLKQGLRVATDFWLADWTEANHDVASVVFNITSSSL--EDDEVSYYISVYAGLSLGAVILSLVTNLAGELAGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 930 TVSKTLHQKMVHAVLHAPMSTFNSWKAGGMLNRFAKDTAVLDDLLPLTVFDFVQLILIVIGAITVVSILQPYIFLASVPV 1009
Cdd:cd18602 80 RAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1010 IAAFIVLRAYFLHTSQQLKQLESEARSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMR 1089
Cdd:cd18602 160 IIVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIR 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1631900066 1090 IEIIFVVFFVAVAFISIITTGDG---PGRVGIILTLAMNIMGTLQWAVNSSIDVDSLMRSVGRI 1150
Cdd:cd18602 240 LDYLGAVIVFLAALSSLTAALAGyisPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERV 303
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
886-1150 |
4.08e-45 |
|
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: 165.34 E-value: 4.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 886 TSDKPPVivtdTSAYYI-IYIYVGVADTLLAMGIFrgLPLVHTLITVSKTLHQKMVHAVLHAPMSTFNSWKAGGMLNRFA 964
Cdd:cd18606 26 TEDFFGL----SQGFYIgIYAGLGVLQAIFLFLFG--LLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 965 KDTAVLDDLLPLTVFDFVQLILIVIGAITVVSILQPYIFLASVPVIAAFIVLRAYFLHTSQQLKQLESEARSPIFTHLVT 1044
Cdd:cd18606 100 KDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYYRASSRELKRLESILRSFVYANFSE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1045 SLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEIIFVVFFVAVAFISIITTGD-GPGRVGIILTLA 1123
Cdd:cd18606 180 SLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSLLVLIVALLCVTRRFSiSPSSTGLVLSYV 259
|
250 260
....*....|....*....|....*..
gi 1631900066 1124 MNIMGTLQWAVNSSIDVDSLMRSVGRI 1150
Cdd:cd18606 260 LQITQVLSWLVRQFAEVENNMNSVERL 286
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
409-606 |
4.41e-45 |
|
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: 162.50 E-value: 4.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 409 NNLFFSNFPlhASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKI-----------------KHSGRI 471
Cdd:cd03290 4 TNGYFSWGS--GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsRNRYSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 472 SFSPQVSWIMPGTIKENIIFGVSYDEYRYKSVIKACQLEEDISKFPEKDYTVLGEGGIILSGGQRARISLARAVYKDADL 551
Cdd:cd03290 82 AYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1631900066 552 YLLDSPFGHLDIFTEKEIFESCVCKLMAN--KTRILVTSKLEHLKIADKILILHEGS 606
Cdd:cd03290 162 VFLDDPFSALDIHLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
895-1150 |
1.55e-44 |
|
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: 163.80 E-value: 1.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 895 TDTSAYYI-IYIYVGVADTLLAMGIFrglpLVHTLITV--SKTLHQKMVHAVLHAPMSTFNSWKAGGMLNRFAKDTAVLD 971
Cdd:cd18603 37 TEQRDYRLgVYGALGLGQAIFVFLGS----LALALGCVraSRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 972 DLLPLTVFDFVQLILIVIGAITVVSILQPYIFLASVPVIAAFIVLRAYFLHTSQQLKQLESEARSPIFTHLVTSLKGLWT 1051
Cdd:cd18603 113 NTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQRFYVATSRQLKRLESVSRSPIYSHFSETLQGAST 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1052 LRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEIIFVVFFVAVAFISIITTGDG-PGRVGIILTLAMNIMGTL 1130
Cdd:cd18603 193 IRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLIVLFAALFAVLSRDSLsPGLVGLSISYALQITQTL 272
|
250 260
....*....|....*....|
gi 1631900066 1131 QWAVNSSIDVDSLMRSVGRI 1150
Cdd:cd18603 273 NWLVRMTSELETNIVSVERI 292
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
68-354 |
5.50e-44 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350041 [Multi-domain] Cd Length: 293 Bit Score: 161.85 E-value: 5.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 68 GIILYLGEVTKSVQPLLLGRII------ASYDPDNSDERSIAYylGIGLCLLFLVRTLLIHPAIFGLHHIGMQMRIAMFS 141
Cdd:cd18597 3 GLLKLLADVLQVLSPLLLKYLInfvedaYLGGPPPSIGYGIGY--AIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 142 LIYKKILKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLLWDMLEASAFSGLAFLIVLAFFQA 221
Cdd:cd18597 81 AIYRKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 222 WLGQMMMKYRNKRAGKINERLVITSEIIENIQSVKAYCWEDAMEKMIESIRETELKLTRKAAYVRYFNSSAFFFSGFFVV 301
Cdd:cd18597 161 FLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLAS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1631900066 302 FLAVLPYAVIKGiILR--KIFTTISFCIVLRMTVTrQFPGSVQTWYDSIGAINKI 354
Cdd:cd18597 241 MLSFITYYATGH-TLDpaNIFSSLALFNVLRMPLM-FLPLALSSLADALVALKRI 293
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
409-605 |
6.18e-44 |
|
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: 157.54 E-value: 6.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 409 NNLFFSnFPLHASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG-------------RISFSP 475
Cdd:cd03228 4 KNVSFS-YPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldleslrkNIAYVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 476 QVSWIMPGTIKENIifgvsydeyryksvikacqleediskfpekdytvlgeggiiLSGGQRARISLARAVYKDADLYLLD 555
Cdd:cd03228 83 QDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1631900066 556 SPFGHLDIFTEKEIFEScVCKLMANKTRILVTSKLEHLKIADKILILHEG 605
Cdd:cd03228 122 EATSALDPETEALILEA-LRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
848-1134 |
2.18e-43 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 159.73 E-value: 2.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 848 VLILCVTVFLIEVAASLAGLWFlkktalkANATQSENSTSDKPPVivtDTSAYYIIYIYVGVADTLLAMGIFRGLplVHT 927
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVL-------GRILDVLLPDGDPETQ---ALNVYSLALLLLGLAQFILSFLQSYLL--NHT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 928 LITVSKTLHQKMVHAVLHAPMSTFNSWKAGGMLNRFAKDTAVLDDLLPLTVFDFVQLILIVIGAITVVSILQPYIFLASV 1007
Cdd:pfam00664 69 GERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1008 PVIAAFIVLRAYFLHTSQQLKQLESEARSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQ 1087
Cdd:pfam00664 149 AVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSF 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1631900066 1088 MRIEIIFVVFFVAVAFISIITTGDGPGRVGIILTLAMnIMGTLQWAV 1134
Cdd:pfam00664 229 GITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLS-LFAQLFGPL 274
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1193-1416 |
3.59e-43 |
|
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: 157.39 E-value: 3.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1193 GKMTVKDLTAKYGEGgAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSVQQWRKAF 1271
Cdd:cd03254 1 GEIEFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDpQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1272 GVIPQKVFIFSGTFRMNLDpYGQWN--DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSRA 1349
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIR-LGRPNatDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1631900066 1350 KILLLDEPSAHLDPVTSQVIRKTLKHAFANCTVILSEHRLEAMLECQRFLVIEDNKLRQYESIQKLL 1416
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1196-1424 |
2.88e-41 |
|
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: 152.00 E-value: 2.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1196 TVKDLTAKYGEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSVQQWRKAFGVI 1274
Cdd:cd03251 2 EFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDvDSGRILIDGHDVRDYTLASLRRQIGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1275 PQKVFIFSGTFRMNLdPYGQWN--DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSRAKIL 1352
Cdd:cd03251 82 SQDVFLFNDTVAENI-AYGRPGatREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1631900066 1353 LLDEPSAHLDPVTSQVIRKTLKHAFANCTVILSEHRLEAMLECQRFLVIEDNKLRQYESIQKLLNEKSSFRQ 1424
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAK 232
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1190-1424 |
1.57e-40 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 159.22 E-value: 1.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1190 PSGGKMTVKDLTAKYGEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLfaflRLLN-----TEGDIQIDGVSWNTVSV 1264
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLL----QLLTrawdpQQGEILLNGQPIADYSE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1265 QQWRKAFGVIPQKVFIFSGTFRMNL---DPygQWNDEEIWKVAEEVGLKSVIEQFPGqLDFVLVDGGCVLSHGHKQLMCL 1341
Cdd:PRK11160 410 AALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGLEKLLEDDKG-LNAWLGEGGRQLSGGEQRRLGI 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1342 ARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFANCTVILSEHRLEAMLECQRFLVIEDNKLRQYESIQKLLNEKSS 1421
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGR 566
|
...
gi 1631900066 1422 FRQ 1424
Cdd:PRK11160 567 YYQ 569
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
409-623 |
2.79e-40 |
|
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: 158.39 E-value: 2.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 409 NNLFFSnFPLHASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG-------------RISFSP 475
Cdd:COG4987 337 EDVSFR-YPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGvdlrdldeddlrrRIAVVP 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 476 QVSWIMPGTIKENIIFG---VSYDEYRykSVIKACQLEEDISKFPEKDYTVLGEGGIILSGGQRARISLARAVYKDADLY 552
Cdd:COG4987 416 QRPHLFDTTLRENLRLArpdATDEELW--AALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPIL 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 553 LLDSPFGHLDIFTEKEIFEScVCKLMANKTRILVTSKLEHLKIADKILILHEGSCYFYGTFSELQGQRPDF 623
Cdd:COG4987 494 LLDEPTEGLDAATEQALLAD-LLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRY 563
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1193-1406 |
9.93e-40 |
|
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: 147.35 E-value: 9.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1193 GKMTVKDLTAKYGEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSVQQWRKAF 1271
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKpTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1272 GVIPQKVFIFSGTFRMNL---DPYGqwNDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSR 1348
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNItlgAPLA--DDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1631900066 1349 AKILLLDEPSAHLDPVTSQVIRKTLKHAFANCTVILSEHRLeAMLE-CQRFLVIEDNKL 1406
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRP-SLLDlVDRIIVMDSGRI 216
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
957-1389 |
1.14e-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: 155.98 E-value: 1.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 957 GGMLNRFAKDTAVLDDLLPLTVFDFVQ---LILIVIGAITVVSIlqPYIFLASVPVIAAFIVLRAYFLHTSQQLKQLESE 1033
Cdd:TIGR02868 110 GDLLGRLGADVDALQDLYVRVIVPAGValvVGAAAVAAIAVLSV--PAALILAAGLLLAGFVAPLVSLRAARAAEQALAR 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1034 ARSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKA-LNLHTAN----WFLYLSTlrwfqmrieIIFVVFFVAVAFISIIT 1108
Cdd:TIGR02868 188 LRGELAAQLTDALDGAAELVASGALPAALAQVEEAdRELTRAErraaAATALGA---------ALTLLAAGLAVLGALWA 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1109 TGDG--PGRVG-------IILTLAM-NIMGTLQWAVnssidvDSLMRSVG---RIFKFIDMPTEEMKNIKPQKKNQLSDA 1175
Cdd:TIGR02868 259 GGPAvaDGRLApvtlavlVLLPLAAfEAFAALPAAA------QQLTRVRAaaeRIVEVLDAAGPVAEGSAPAAGAVGLGK 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1176 LVIEnrhakeeknwpsggkmtVKDLTAKYgEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLNT-EGDIQI 1254
Cdd:TIGR02868 333 PTLE-----------------LRDLSAGY-PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPlQGEVTL 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1255 DGVSWNTVSVQQWRKAFGVIPQKVFIFSGTFRMNLD-PYGQWNDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSH 1333
Cdd:TIGR02868 395 DGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRlARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSG 474
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1631900066 1334 GHKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFANCTVILSEHRL 1389
Cdd:TIGR02868 475 GERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
422-620 |
1.22e-39 |
|
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: 147.37 E-value: 1.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG-------------RISFSPQVSWIMPGTIKEN 488
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslrsMIGVVLQDTFLFSGTIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 489 IIFGVSY-DEYRYKSVIKACQLEEDISKFPEKDYTVLGEGGIILSGGQRARISLARAVYKDADLYLLDSPFGHLDIFTEK 567
Cdd:cd03254 97 IRLGRPNaTDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1631900066 568 EIfESCVCKLMANKTRILVTSKLEHLKIADKILILHEGSCYFYGTFSELQGQR 620
Cdd:cd03254 177 LI-QEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
59-286 |
3.50e-39 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 1 (TMD1) 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: 350039 [Multi-domain] Cd Length: 290 Bit Score: 148.00 E-value: 3.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 59 CFFWKFmFYGIILYlgevtksVQPLLLGRIIaSYDPDNSDERSIAYYLGIGLCLLFLVRTLLIHPAIFGLHHIGMQMRIA 138
Cdd:cd18595 2 AALLKL-LSDILLF-------ASPQLLKLLI-NFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 139 MFSLIYKKILKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLLWDMLEASAFSGLAFLIVLAF 218
Cdd:cd18595 73 LTSAIYRKALRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1631900066 219 FQAWLGQMMMKYRNKRAGKINERLVITSEIIENIQSVKAYCWEDAMEKMIESIRETELKLTRKAAYVR 286
Cdd:cd18595 153 LNAVLARKIKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLN 220
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
64-286 |
9.49e-39 |
|
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: 146.25 E-value: 9.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 64 FMFYGIILYLGEVTKSVQPLLLGRIIASYDPDNS--DERSIAYYLGIGLCLLFLVRTLLIHPAIFglHHIGMQMRIAMFS 141
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDpeTQALNVYSLALLLLGLAQFILSFLQSYLL--NHTGERLSRRLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 142 LIYKKILKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVAL-LMGLLWDMLEASAFSGLAFLIVLAFFQ 220
Cdd:pfam00664 79 KLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVgGIIVMFYYGWKLTLVLLAVLPLYILVS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1631900066 221 AWLGQMMMKYRNKRAGKINERLVITSEIIENIQSVKAYCWEDAMEKMIESIRETELKLTRKAAYVR 286
Cdd:pfam00664 159 AVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVAN 224
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1182-1401 |
1.68e-38 |
|
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: 152.44 E-value: 1.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1182 HAKEEKNWPSGGKMTVKDLTAKYgEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWN 1260
Cdd:TIGR02857 309 AGKAPVTAAPASSLEFSGVSVAY-PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDpTEGSIAVNGVPLA 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1261 TVSVQQWRKAFGVIPQKVFIFSGTFRMNL---DPYGqwNDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQ 1337
Cdd:TIGR02857 388 DADADSWRDQIAWVPQHPFLFAGTIAENIrlaRPDA--SDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQ 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1631900066 1338 LMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFANCTVILSEHRLEAMLECQRFLVI 1401
Cdd:TIGR02857 466 RLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
420-602 |
1.60e-37 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 149.36 E-value: 1.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 420 ASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG-------------RISFSPQVSWIMPGTIK 486
Cdd:TIGR02857 334 RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadswrdQIAWVPQHPFLFAGTIA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 487 ENIIFGVSY-DEYRYKSVIKACQLEEDISKFPEKDYTVLGEGGIILSGGQRARISLARAVYKDADLYLLDSPFGHLDIFT 565
Cdd:TIGR02857 414 ENIRLARPDaSDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAET 493
|
170 180 190
....*....|....*....|....*....|....*..
gi 1631900066 566 EKEIFEScVCKLMANKTRILVTSKLEHLKIADKILIL 602
Cdd:TIGR02857 494 EAEVLEA-LRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1198-1424 |
1.60e-37 |
|
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: 141.21 E-value: 1.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1198 KDLTAKYgEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSVQQWRKAFGVIPQ 1276
Cdd:cd03253 4 ENVTFAY-DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDvSSGSILIDGQDIREVTLDSLRRAIGVVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1277 KVFIFSGTFRMNLDpYGQWN--DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSRAKILLL 1354
Cdd:cd03253 83 DTVLFNDTIGYNIR-YGRPDatDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1355 DEPSAHLDPVTSQVIRKTLKHAFANCTVILSEHRLEAMLECQRFLVIEDNKLRQYESIQKLLNEKSSFRQ 1424
Cdd:cd03253 162 DEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAE 231
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
409-620 |
4.48e-36 |
|
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: 136.98 E-value: 4.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 409 NNLFFSnFPLHASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGR-------------ISFSP 475
Cdd:cd03251 4 KNVTFR-YPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdytlaslrrqIGLVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 476 QVSWIMPGTIKENIIFGVS-YDEYRYKSVIKACQLEEDISKFPEKDYTVLGEGGIILSGGQRARISLARAVYKDADLYLL 554
Cdd:cd03251 83 QDVFLFNDTVAENIAYGRPgATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILIL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1631900066 555 DSPFGHLDIFTEKEIFEScVCKLMANKTRILVTSKLEHLKIADKILILHEGSCYFYGTFSELQGQR 620
Cdd:cd03251 163 DEATSALDTESERLVQAA-LERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQG 227
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
848-1154 |
4.86e-35 |
|
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: 136.51 E-value: 4.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 848 VLILCVTVFLIEVAASLAGLWFlkktalkanATQSENSTSDKPPVIVTDTSAYYIIYIYVGVADTLLAmgIFRGLPLVHT 927
Cdd:cd18605 1 LILILLSLILMQASRNLIDFWL---------SYWVSHSNNSFFNFINDSFNFFLTVYGFLAGLNSLFT--LLRAFLFAYG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 928 LITVSKTLHQKMVHAVLHAPMSTFNSWKAGGMLNRFAKDTAVLDDLLPLTVFDFVQLILIVIGAITVVSILQPYIFLASV 1007
Cdd:cd18605 70 GLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1008 PVIAAFIVLRAYFLHTSQQLKQLESEARSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQ 1087
Cdd:cd18605 150 PLAFIYYRIQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLS 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 1088 MRIEIIFVVFFVAVAFISIITTGDG----PGRVGIILTLAMNIMGTLQWAVNSSIDVDSLMRSVGRIFKFI 1154
Cdd:cd18605 230 IRLQLLGVLIVTFVALTAVVQHFFGlsidAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQYF 300
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
931-1406 |
8.31e-35 |
|
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: 141.78 E-value: 8.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 931 VSKTLHQKMVHAVLHAPMSTFNSWKAGGMLNRFAKDT-----AVLDDLLPLtvfdfVQLILIVIGAITVVSILQ---PYI 1002
Cdd:TIGR02203 85 VVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSeqvasAATDAFIVL-----VRETLTVIGLFIVLLYYSwqlTLI 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1003 FLASVPVIAafIVLRAYflhtSQQLKQLESEARSPI--FTHLVT-SLKGLWTLRAFGRQPYFETLFHKALNlhtanwfly 1079
Cdd:TIGR02203 160 VVVMLPVLS--ILMRRV----SKRLRRISKEIQNSMgqVTTVAEeTLQGYRVVKLFGGQAYETRRFDAVSN--------- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1080 lsTLRWFQMRIEIIFVVFFVAVAFISIIT-----------TGDG---PGRVGIILTLAMNIMGTLQWAVNSSIDVDSLMR 1145
Cdd:TIGR02203 225 --RNRRLAMKMTSAGSISSPITQLIASLAlavvlfialfqAQAGsltAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLA 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1146 SVGRIFKFIDMPTEemknikpqkknqlsdalVIENRHAKEEKNwpsgGKMTVKDLTAKYGEGGAAVLENISFSIDSGQRV 1225
Cdd:TIGR02203 303 AAESLFTLLDSPPE-----------------KDTGTRAIERAR----GDVEFRNVTFRYPGRDRPALDSISLVIEPGETV 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1226 GLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSVQQWRKAFGVIPQKVFIFSGTFRMNLdPYG---QWNDEEIW 1301
Cdd:TIGR02203 362 ALVGRSGSGKSTLVNLIPRFYEpDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNI-AYGrteQADRAEIE 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1302 KVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFANCT 1381
Cdd:TIGR02203 441 RALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRT 520
|
490 500
....*....|....*....|....*
gi 1631900066 1382 VILSEHRLEAMLECQRFLVIEDNKL 1406
Cdd:TIGR02203 521 TLVIAHRLSTIEKADRIVVMDDGRI 545
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1197-1406 |
1.25e-34 |
|
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: 132.84 E-value: 1.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKYgEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLN-----TEGDIQIDGVSWNTVSVQQWRKAF 1271
Cdd:COG1122 3 LENLSFSY-PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTL----LRLLNgllkpTSGEVLVDGKDITKKNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1272 GVipqkVF------IFSGT------F---RMNLDPygqwndEEIWKVAEE----VGLKSVIEQFPGQldfvlvdggcvLS 1332
Cdd:COG1122 78 GL----VFqnpddqLFAPTveedvaFgpeNLGLPR------EEIRERVEEalelVGLEHLADRPPHE-----------LS 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1631900066 1333 HGHKQLMCLArSVLS-RAKILLLDEPSAHLDPVTSQVIRKTLKH-AFANCTVILSEHRLEAMLE-CQRFLVIEDNKL 1406
Cdd:COG1122 137 GGQKQRVAIA-GVLAmEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAElADRVIVLDDGRI 212
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1212-1359 |
2.74e-34 |
|
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: 128.92 E-value: 2.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1212 LENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSVQQWRKAFGVIPQKVFIFSG-TFRMNL 1289
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSpTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1631900066 1290 -------DPYGQWNDEEIWKVAEEVGLksvieqfPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSRAKILLLDEPSA 1359
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEKLGL-------GDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1150-1428 |
4.05e-34 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 139.98 E-value: 4.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1150 IFKFIDMPTEEMknikPQKKNQLSDALVIEnrhakeeknwpsggkMTVKDLTAkYGEGGAAVLENISFSIDSGQRVGLLG 1229
Cdd:PRK11174 324 LVTFLETPLAHP----QQGEKELASNDPVT---------------IEAEDLEI-LSPDGKTLAGPLNFTLPAGQRIALVG 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1230 RTGSGKSTLLFAFLRLLNTEGDIQIDGVSWNTVSVQQWRKAFGVIPQKVFIFSGTFRMNL---DPygQWNDEEIWKVAEE 1306
Cdd:PRK11174 384 PSGAGKTSLLNALLGFLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVllgNP--DASDEQLQQALEN 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1307 VGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFANCTVILSE 1386
Cdd:PRK11174 462 AWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVT 541
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1631900066 1387 HRLEAMLECQRFLVIEDNKLRQYESIQKLLNEKSSFRQAISH 1428
Cdd:PRK11174 542 HQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAH 583
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1197-1405 |
4.23e-34 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 130.66 E-value: 4.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKYGEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLN-----TEGDIQIDGVSWNTVSVQQWRKAF 1271
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTL----LRLLNgllgpTSGEVLVDGKDLTKLSLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1272 GVIPQ--KVFIFSGTFR-------MNLdpygQWNDEEIWK----VAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQL 1338
Cdd:cd03225 78 GLVFQnpDDQFFGPTVEeevafglENL----GLPEEEIEErveeALELVGLEGLRDRSPFT-----------LSGGQKQR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 1339 MCLArSVLS-RAKILLLDEPSAHLDPVTSQVIRKTLK--HAfANCTVILSEHRLEAMLE-CQRFLVIEDNK 1405
Cdd:cd03225 143 VAIA-GVLAmDPDILLLDEPTAGLDPAGRRELLELLKklKA-EGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
409-616 |
1.93e-33 |
|
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: 129.66 E-value: 1.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 409 NNLFFSNFPlhASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIK-----------HSGR--ISFSP 475
Cdd:cd03253 4 ENVTFAYDP--GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILidgqdirevtlDSLRraIGVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 476 QVSWIMPGTIKENIIFG---VSyDEYRYKSViKACQLEEDISKFPEKDYTVLGEGGIILSGGQRARISLARAVYKDADLY 552
Cdd:cd03253 82 QDTVLFNDTIGYNIRYGrpdAT-DEEVIEAA-KAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1631900066 553 LLDSPFGHLDIFTEKEIFEScVCKLMANKTRILVTSKLEHLKIADKILILHEGSCYFYGTFSEL 616
Cdd:cd03253 160 LLDEATSALDTHTEREIQAA-LRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEEL 222
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1211-1424 |
2.18e-33 |
|
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: 129.58 E-value: 2.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1211 VLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSVQQWRKAFGVIPQKVFIFSGTFRMNL 1289
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDpTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1290 DpYGQWN--DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQ 1367
Cdd:cd03249 98 R-YGKPDatDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1631900066 1368 VIRKTLKHAFANCTVILSEHRLEAMLECQRFLVIEDNKLRQYESIQKLLNEKSSFRQ 1424
Cdd:cd03249 177 LVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAK 233
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1196-1405 |
1.47e-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: 124.28 E-value: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1196 TVKDLTAKYGEGgaAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSVQQWRKAFGVI 1274
Cdd:cd00267 1 EIENLSFRYGGR--TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKpTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1275 PQkvfifsgtfrmnldpygqwndeeiwkvaeevglksvieqfpgqldfvlvdggcvLSHGHKQLMCLARSVLSRAKILLL 1354
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1631900066 1355 DEPSAHLDPVTSQVIRKTLKHAFA-NCTVILSEHRLE-AMLECQRFLVIEDNK 1405
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPElAELAADRVIVLKDGK 157
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1196-1418 |
4.31e-32 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 125.56 E-value: 4.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1196 TVKDLTAKYGegGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSvQQWRKAFGVI 1274
Cdd:COG1131 2 EVRGLTKRYG--DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRpTSGEVRVLGEDVARDP-AEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1275 PQKVFIFSG-TFRMNLDPYGQ-------WNDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVL 1346
Cdd:COG1131 79 PQEPALYPDlTVRENLRFFARlyglprkEARERIDELLELFGLTDAADRKVGTL-----------SGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1631900066 1347 SRAKILLLDEPSAHLDPVTSQVIRKTLKHAFA-NCTVILSEHRL-EAMLECQRFLVIEDNKLRQYESIQKLLNE 1418
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRELAAeGKTVLLSTHYLeEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1195-1424 |
6.69e-32 |
|
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: 125.29 E-value: 6.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTAKYGEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRL-LNTEGDIQIDGVSWNTVSVQQWRKAFGV 1273
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1274 IPQKVFIFSGTFRMNL---DPygQWNDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSRAK 1350
Cdd:cd03252 81 VLQENVLFNRSIRDNIalaDP--GMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1631900066 1351 ILLLDEPSAHLDPVTSQVIRKTLKHAFANCTVILSEHRLEAMLECQRFLVIEDNKLRQYESIQKLLNEKSSFRQ 1424
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAY 232
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
409-605 |
1.29e-31 |
|
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: 123.85 E-value: 1.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 409 NNLFFSnFPLHASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG-------------RISFSP 475
Cdd:cd03245 6 RNVSFS-YPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 476 QVSWIMPGTIKENIIFGVSY-DEYRYKSVIKACQLEEDISKFPEKDYTVLGEGGIILSGGQRARISLARAVYKDADLYLL 554
Cdd:cd03245 85 QDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 555 DSPFGHLDIFTEKEIFEScVCKLMANKTRILVTSKLEHLKIADKILILHEG 605
Cdd:cd03245 165 DEPTSAMDMNSEERLKER-LRQLLGDKTLIIITHRPSLLDLVDRIIVMDSG 214
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1197-1406 |
4.39e-31 |
|
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: 120.78 E-value: 4.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKYGEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSVQQWRKAFGVIP 1275
Cdd:cd03246 3 VENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRpTSGRVRLDGADISQWDPNELGDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1276 QKVFIFSGTFRMNldpygqwndeeiwkvaeevglksvieqfpgqldfvlvdggcVLSHGHKQLMCLARSVLSRAKILLLD 1355
Cdd:cd03246 83 QDDELFSGSIAEN-----------------------------------------ILSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1631900066 1356 EPSAHLDPVTSQVIRKTLKHA-FANCTVILSEHRLEAMLECQRFLVIEDNKL 1406
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
68-277 |
5.83e-31 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350042 [Multi-domain] Cd Length: 288 Bit Score: 124.20 E-value: 5.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 68 GIILYLGEVTKSVQPLLLGRIIaSYDPDNSDERSIAYYLGIGLCLLFLVRTLLIHPAIFGLHHIGMQMRIAMFSLIYKKI 147
Cdd:cd18598 3 GLLKLLADVLGFAGPLLLNKLV-EFLEDSSEPLSDGYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTAVYRKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 148 LKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLLWDMLEASAFSGLAFLIVLAFFQAWLGQMM 227
Cdd:cd18598 82 LRVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAKRI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1631900066 228 MKYRNKRAGKINERLVITSEIIENIQSVKAYCWEDAMEKMIESIRETELK 277
Cdd:cd18598 162 GALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELK 211
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
422-605 |
1.72e-30 |
|
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: 118.86 E-value: 1.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIK-------------HSGRISFSPQVSWIMPGTIKEN 488
Cdd:cd03246 16 PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRldgadisqwdpneLGDHVGYLPQDDELFSGSIAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 489 IifgvsydeyryksvikacqleediskfpekdytvlgeggiiLSGGQRARISLARAVYKDADLYLLDSPFGHLDIFTEKE 568
Cdd:cd03246 96 I-----------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERA 134
|
170 180 190
....*....|....*....|....*....|....*..
gi 1631900066 569 IFESCVCKLMANKTRILVTSKLEHLKIADKILILHEG 605
Cdd:cd03246 135 LNQAIAALKAAGATRIVIAHRPETLASADRILVLEDG 171
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
419-605 |
2.14e-30 |
|
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: 120.29 E-value: 2.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 419 HASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG-------------RISFSPQVSWIMPGTI 485
Cdd:cd03244 15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRISIIPQDPVLFSGTI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 486 KENI-IFGVSYDEYRYkSVIKACQLEEDISKFPEKDYTVLGEGGIILSGGQRARISLARAVYKDADLYLLDSPFGHLDIF 564
Cdd:cd03244 95 RSNLdPFGEYSDEELW-QALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1631900066 565 TEKEIFEScVCKLMANKTRILVTSKLEHLKIADKILILHEG 605
Cdd:cd03244 174 TDALIQKT-IREAFKDCTVLTIAHRLDTIIDSDRILVLDKG 213
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1196-1406 |
2.20e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 119.92 E-value: 2.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1196 TVKDLTakYGEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLL-NTEGDIQIDGVSWNTVSVQQWRKAFGVI 1274
Cdd:COG4619 2 ELEGLS--FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDpPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1275 PQKVFIFSGTFRMNLD-PYG----QWNDEEIWKVAEEVGL------KSVIEqfpgqldfvlvdggcvLSHGHKQLMCLAR 1343
Cdd:COG4619 80 PQEPALWGGTVRDNLPfPFQlrerKFDRERALELLERLGLppdildKPVER----------------LSGGERQRLALIR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1631900066 1344 SVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFA--NCTVILSEH-RLEAMLECQRFLVIEDNKL 1406
Cdd:COG4619 144 ALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAeeGRAVLWVSHdPEQIERVADRVLTLEAGRL 209
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
424-558 |
2.37e-30 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 117.75 E-value: 2.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 424 LQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIK-------------HSGRISFSPQVSWIMPG-TIKENI 489
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILldgqdltdderksLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 490 IFGVsyDEYRYKSVIKACQLEEDISKFPEKD--YTVLGEGGIILSGGQRARISLARAVYKDADLYLLDSPF 558
Cdd:pfam00005 81 RLGL--LLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1197-1406 |
4.04e-30 |
|
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: 117.88 E-value: 4.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKYGEGgaAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLL-NTEGDIQIDGVSWNTVSVQqWRKAFGVIP 1275
Cdd:cd03230 3 VRNLSKRYGKK--TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLkPDSGEIKVLGKDIKKEPEE-VKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1276 QKVFIFSG-TFRMNLDpygqwndeeiwkvaeevglksvieqfpgqldfvlvdggcvLSHGHKQLMCLARSVLSRAKILLL 1354
Cdd:cd03230 80 EEPSLYENlTVRENLK----------------------------------------LSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1631900066 1355 DEPSAHLDPVTSQVIRKTLKH-AFANCTVILSEHRLEAMLE-CQRFLVIEDNKL 1406
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
417-622 |
1.02e-29 |
|
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: 126.02 E-value: 1.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 417 PLHASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGK-------IKHSGRISFS------PQVSWIMPG 483
Cdd:COG4618 341 PGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSvrldgadLSQWDREELGrhigylPQDVELFDG 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 484 TIKENII-FGVSYDEyrykSVIKACQL---EEDISKFPeKDY-TVLGEGGIILSGGQRARISLARAVYKDADLYLLDSPF 558
Cdd:COG4618 421 TIAENIArFGDADPE----KVVAAAKLagvHEMILRLP-DGYdTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPN 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1631900066 559 GHLDIFTEKeifescvcKLMA--------NKTRILVTSKLEHLKIADKILILHEGSCYFYGT----FSELQGQRPD 622
Cdd:COG4618 496 SNLDDEGEA--------ALAAairalkarGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPrdevLARLARPAAA 563
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
422-616 |
2.19e-29 |
|
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: 118.03 E-value: 2.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKI-------------KHSGRISFSPQVSWIMPGTIKEN 488
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIlldgvdirdlnlrWLRSQIGLVSQEPVLFDGTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 489 IIFGVSY--DEYRyKSVIKACQLEEDISKFPEKDYTVLGEGGIILSGGQRARISLARAVYKDADLYLLDSPFGHLDIFTE 566
Cdd:cd03249 97 IRYGKPDatDEEV-EEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1631900066 567 KEIFESCVcKLMANKTRILVTSKLEHLKIADKILILHEGSCYFYGTFSEL 616
Cdd:cd03249 176 KLVQEALD-RAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDEL 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
420-590 |
2.24e-29 |
|
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: 124.78 E-value: 2.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 420 ASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG-------------RISFSPQVSWIMPGTIK 486
Cdd:TIGR02868 347 APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGvpvssldqdevrrRVSVCAQDAHLFDTTVR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 487 ENIIFG---VSYDEYRykSVIKACQLEEDISKFPEKDYTVLGEGGIILSGGQRARISLARAVYKDADLYLLDSPFGHLDI 563
Cdd:TIGR02868 427 ENLRLArpdATDEELW--AALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDA 504
|
170 180
....*....|....*....|....*..
gi 1631900066 564 FTEKEIFEScVCKLMANKTRILVTSKL 590
Cdd:TIGR02868 505 ETADELLED-LLAALSGRTVVLITHHL 530
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
421-624 |
3.01e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 124.96 E-value: 3.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 421 SPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELePSQGKIKHSG-------RISFSPQVSWI------MPGTIKE 487
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGielreldPESWRKHLSWVgqnpqlPHGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 488 NIIFG-VSYDEYRYKSVIKACQLEEDISKFPEKDYTVLGEGGIILSGGQRARISLARAVYKDADLYLLDSPFGHLDIFTE 566
Cdd:PRK11174 442 NVLLGnPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSE 521
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1631900066 567 KEIFEScVCKLMANKTRILVTSKLEHLKIADKILILHEGSCYFYGTFSELQGQRPDFS 624
Cdd:PRK11174 522 QLVMQA-LNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFA 578
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1196-1420 |
3.11e-29 |
|
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: 117.65 E-value: 3.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1196 TVKDLTAKYGEGgaAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSwNTVSVQQWRKAFGVI 1274
Cdd:COG4555 3 EVENLSKKYGKV--PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKpDSGSILIDGED-VRKEPREARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1275 PQKVFIFSG-TFRMNLDPYG---QWNDEEIWKVAEEVglksvIEQFpgQLDFVL---VDGgcvLSHGHKQLMCLARSVLS 1347
Cdd:COG4555 80 PDERGLYDRlTVRENIRYFAelyGLFDEELKKRIEEL-----IELL--GLEEFLdrrVGE---LSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1631900066 1348 RAKILLLDEPSAHLDPVTSQVIRKTLK-HAFANCTVILSEHRLEAMLE-CQRFLVIEDNKLRQYESIQKLLNEKS 1420
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRaLKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1195-1406 |
7.36e-29 |
|
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: 114.33 E-value: 7.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTAKYGEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVswNTVSVQ-QWRKAFG 1272
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKpQQGEITLDGV--PVSDLEkALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1273 VIPQKVFIFSGTFRMNLdpygqwndeeiwkvaeevglksvieqfpgqldfvlvdgGCVLSHGHKQLMCLARSVLSRAKIL 1352
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1631900066 1353 LLDEPSAHLDPVTSQVIRKTLKHAFANCTVILSEHRLEAMLECQRFLVIEDNKL 1406
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKI 174
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1193-1416 |
1.15e-28 |
|
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: 122.93 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1193 GKMTVKDLTAKYGEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLfaflRLL-----NTEGDIQIDGVSwntvsVQQW 1267
Cdd:COG4618 329 GRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLA----RLLvgvwpPTAGSVRLDGAD-----LSQW 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1268 RKA-----FGVIPQKVFIFSGTFRMNLDPYGQWNDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLA 1342
Cdd:COG4618 400 DREelgrhIGYLPQDVELFDGTIAENIARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLA 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1631900066 1343 RSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFA-NCTVILSEHRLEAMLECQRFLVIEDNKLRQY----ESIQKLL 1416
Cdd:COG4618 480 RALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGRVQAFgprdEVLARLA 558
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1191-1424 |
3.78e-28 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 121.75 E-value: 3.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1191 SGGKMTVKDLTAKYGEGgAAVLENISFSIDSGQRVGLLGRTGSGKSTL---LFAFLRLlnTEGDIQIDGVSWNTVSVQQW 1267
Cdd:PRK10790 337 QSGRIDIDNVSFAYRDD-NLVLQNINLSVPSRGFVALVGHTGSGKSTLaslLMGYYPL--TEGEIRLDGRPLSSLSHSVL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1268 RKAFGVIPQKVFIFSGTFRMNLDPYGQWNDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLS 1347
Cdd:PRK10790 414 RQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQ 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1631900066 1348 RAKILLLDEPSAHLDPVTSQVIRKTLKHAFANCTVILSEHRLEAMLECQRFLVIEDNKLRQYESIQKLLNEKSSFRQ 1424
Cdd:PRK10790 494 TPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQ 570
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
422-602 |
6.83e-28 |
|
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: 113.01 E-value: 6.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG--------RISFSPQ---VSWIMPGTIKE--- 487
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekerkRIGYVPQrrsIDRDFPISVRDvvl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 488 -----NIIFGVSYDEYRYKSVIKAcqLEE-DISKFPEKDytvLGEggiiLSGGQRARISLARAVYKDADLYLLDSPFGHL 561
Cdd:cd03235 93 mglygHKGLFRRLSKADKAKVDEA--LERvGLSELADRQ---IGE----LSGGQQQRVLLARALVQDPDLLLLDEPFAGV 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1631900066 562 DIFTEKEIFEsCVCKL-MANKTRILVTSKLEH-LKIADKILIL 602
Cdd:cd03235 164 DPKTQEDIYE-LLRELrREGMTILVVTHDLGLvLEYFDRVLLL 205
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
68-286 |
7.79e-28 |
|
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 1 (TMD1) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and they 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: 350035 [Multi-domain] Cd Length: 309 Bit Score: 115.41 E-value: 7.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 68 GIILYLGEVTKSVQPLLLGRII-----ASYDPDNSDERSIAYYL--------GIGLCLLFLVRTLLIHPAIFGLHHI--- 131
Cdd:cd18591 3 GILKLLGDLLGFVGPLCISGIVdyveeNTYSSSNSTDKLSVSYVtveeffsnGYVLAVILFLALLLQATFSQASYHIvir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 132 -GMQMRIAMFSLIYKKILKLSSRVLD--KISTGQLVSLLS---NNLNKFdegLALAHFVWIAPLQVALLMGLLWDMLEAS 205
Cdd:cd18591 83 eGIRLKTALQAMIYEKALRLSSWNLSsgSMTIGQITNHMSedaNNIMFF---FWLIHYLWAIPLKIIVGLILLYLKLGVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 206 AFSGLAFLIVLAFFQAWLGQMMMKYRNKRAGKINERLVITSEIIENIQSVKAYCWEDAMEKMIESIRETELKLTRKAAYV 285
Cdd:cd18591 160 ALIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVY 239
|
.
gi 1631900066 286 R 286
Cdd:cd18591 240 W 240
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1196-1450 |
1.17e-27 |
|
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: 119.24 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1196 TVKDLTAKYGEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLL----NTEGDIQIDGVSWNTVSVQQWRKAF 1271
Cdd:COG1123 6 EVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLphggRISGEVLLDGRDLLELSEALRGRRI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1272 GVIPQkvfifsgtfrmnlDPYGQWN----------------------DEEIWKVAEEVGLKSVIEQFPGQldfvlvdggc 1329
Cdd:COG1123 86 GMVFQ-------------DPMTQLNpvtvgdqiaealenlglsraeaRARVLELLEAVGLERRLDRYPHQ---------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1330 vLSHGHKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLK--HAFANCTVILSEHRLEAMLE-CQRFLVIEDNKL 1406
Cdd:COG1123 143 -LSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVAEiADRVVVMDDGRI 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1631900066 1407 RqyesiqkllnEKSSFRQAISHADRLKLLPVHHRNSSKRKPRPK 1450
Cdd:COG1123 222 V----------EDGPPEEILAAPQALAAVPRLGAARGRAAPAAA 255
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1197-1417 |
4.31e-27 |
|
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: 111.82 E-value: 4.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKYGEGGAA--VLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLL-NTEGDIQIDGVSWNTVSVQQWRKAFGV 1273
Cdd:COG1124 4 VRNLSVSYGQGGRRvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLErPWSGEVTFDGRPVTRRRRKAFRRRVQM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1274 IPQkvfifsgtfrmnlDPYGQWN---------------------DEEIWKVAEEVGL-KSVIEQFPGQldfvlvdggcvL 1331
Cdd:COG1124 84 VFQ-------------DPYASLHprhtvdrilaeplrihglpdrEERIAELLEQVGLpPSFLDRYPHQ-----------L 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1332 SHGHKQLMCLARSVLSRAKILLLDEPSAHLDPVT-SQVIR--KTLKHAFaNCTVILSEHRLEAMLE-CQRFLVIEDNKLR 1407
Cdd:COG1124 140 SGGQRQRVAIARALILEPELLLLDEPTSALDVSVqAEILNllKDLREER-GLTYLFVSHDLAVVAHlCDRVAVMQNGRIV 218
|
250
....*....|
gi 1631900066 1408 QYESIQKLLN 1417
Cdd:COG1124 219 EELTVADLLA 228
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1195-1408 |
5.88e-27 |
|
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: 110.30 E-value: 5.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTAKYGegGAAVLENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLN-----TEGDIQIDGVSWNTVSVQqwRK 1269
Cdd:cd03259 1 LELKGLSKTYG--SVRALDDLSLTVEPGEFLALLGPSGCGKTTL----LRLIAglerpDSGEILIDGRDVTGVPPE--RR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1270 AFGVIPQK--------VF--IFSGtFRMNLDPYGQWNDEEIWkVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLM 1339
Cdd:cd03259 73 NIGMVFQDyalfphltVAenIAFG-LKLRGVPKAEIRARVRE-LLELVGLEGLLNRYPHE-----------LSGGQQQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1631900066 1340 CLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFAN--CTVILSEHRL-EAMLECQRFLVIEDNKLRQ 1408
Cdd:cd03259 140 ALARALAREPSLLLLDEPLSALDAKLREELREELKELQRElgITTIYVTHDQeEALALADRIAVMNEGRIVQ 211
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
409-611 |
9.25e-27 |
|
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: 108.29 E-value: 9.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 409 NNLFFSnfpLHASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKhsgrisfspqvswimpgtiken 488
Cdd:cd03214 3 ENLSVG---YGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIL---------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 489 iIFGVSYDEYRYKSVIKAC----Q-LEE-DISKFPEKDYTVLgeggiilSGGQRARISLARAVYKDADLYLLDSPFGHLD 562
Cdd:cd03214 58 -LDGKDLASLSPKELARKIayvpQaLELlGLAHLADRPFNEL-------SGGERQRVLLARALAQEPPILLLDEPTSHLD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1631900066 563 IFTEKEIFEScVCKLMA--NKTRILVTSKLEH-LKIADKILILHEGSCYFYG 611
Cdd:cd03214 130 IAHQIELLEL-LRRLARerGKTVVMVLHDLNLaARYADRVILLKDGRIVAQG 180
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
422-628 |
1.33e-26 |
|
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: 109.95 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG------------RISFSPQVSWIMPG-TIKEN 488
Cdd:COG4555 15 PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkeprearrQIGVLPDERGLYDRlTVREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 489 I-----IFGVSYDEYRYK--SVIKACQLEEDIskfpekDYTVLGeggiiLSGGQRARISLARAVYKDADLYLLDSPFGHL 561
Cdd:COG4555 95 IryfaeLYGLFDEELKKRieELIELLGLEEFL------DRRVGE-----LSTGMKKKVALARALVHDPKVLLLDEPTNGL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 562 DIFTeKEIFESCVCKLMANKTRILVTSKLEHL--KIADKILILHEGSCYFYGTFSEL--QGQRPDFSSELM 628
Cdd:COG4555 164 DVMA-RRLLREILRALKKEGKTVLFSSHIMQEveALCDRVVILHKGKVVAQGSLDELreEIGEENLEDAFV 233
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1196-1406 |
1.33e-26 |
|
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: 107.91 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1196 TVKDLTAKYGegGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSVQQWRKAFGVI 1274
Cdd:cd03214 1 EVENLSVGYG--GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKpSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1275 PQkvfifsgtfrmnldpygqwndeeiwkVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSRAKILLL 1354
Cdd:cd03214 79 PQ--------------------------ALELLGLAHLADRPFNE-----------LSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1631900066 1355 DEPSAHLDPvTSQV----IRKTLKHAFaNCTVILSEHRLE-AMLECQRFLVIEDNKL 1406
Cdd:cd03214 122 DEPTSHLDI-AHQIelleLLRRLARER-GKTVVMVLHDLNlAARYADRVILLKDGRI 176
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1195-1406 |
1.38e-26 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 110.52 E-value: 1.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTAKYGegGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSVQQWRKAFGV 1273
Cdd:COG1120 2 LEAENLSVGYG--GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKpSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1274 IPQKvfiFSGTFRMN------------LDPYGQWNDEE---IWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQL 1338
Cdd:COG1120 80 VPQE---PPAPFGLTvrelvalgryphLGLFGRPSAEDreaVEEALERTGLEHLADRPVDE-----------LSGGERQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1631900066 1339 MCLARSVLSRAKILLLDEPSAHLDPvTSQV-IRKTLKH--AFANCTVILSEHRLE-AMLECQRFLVIEDNKL 1406
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDL-AHQLeVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRI 216
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
422-619 |
1.76e-26 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 109.38 E-value: 1.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG------------RISFSPQVSWIMPG-TIKEN 488
Cdd:COG1131 14 TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIGYVPQEPALYPDlTVREN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 489 I-----IFGVSYDEY--RYKSVIKACQLEEDISKFPEKdytvlgeggiiLSGGQRARISLARAVYKDADLYLLDSPFGHL 561
Cdd:COG1131 94 LrffarLYGLPRKEAreRIDELLELFGLTDAADRKVGT-----------LSGGMKQRLGLALALLHDPELLILDEPTSGL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1631900066 562 DIFTEKEIFEsCVCKLMANKTRILVTSkleHL-----KIADKILILHEGSCYFYGTFSELQGQ 619
Cdd:COG1131 163 DPEARRELWE-LLRELAAEGKTVLLST---HYleeaeRLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
423-616 |
2.54e-26 |
|
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: 109.11 E-value: 2.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 423 VLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG-------------RISFSPQVSWIMPGTIKENI 489
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGVVLQENVLFNRSIRDNI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 490 IFG-VSYDEYRYKSVIKACQLEEDISKFPEKDYTVLGEGGIILSGGQRARISLARAVYKDADLYLLDSPFGHLDIFTEKE 568
Cdd:cd03252 97 ALAdPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1631900066 569 IFEScVCKLMANKTRILVTSKLEHLKIADKILILHEGSCYFYGTFSEL 616
Cdd:cd03252 177 IMRN-MHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1193-1424 |
3.97e-26 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 115.12 E-value: 3.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1193 GKMTVKDLTAKYGEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSVQQWRKAF 1271
Cdd:PRK11176 340 GDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDiDEGEILLDGHDLRDYTLASLRNQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1272 GVIPQKVFIFSGTFRMNLdPY---GQWNDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSR 1348
Cdd:PRK11176 420 ALVSQNVHLFNDTIANNI-AYartEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRD 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1631900066 1349 AKILLLDEPSAHLDPVTSQVIRKTLKHAFANCTVILSEHRLEAMLECQRFLVIEDNKLRQYESIQKLLNEKSSFRQ 1424
Cdd:PRK11176 499 SPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQ 574
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1197-1405 |
5.26e-26 |
|
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: 107.17 E-value: 5.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKYGEG---GAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLrllnteGDIQ-IDGvswntvSVqQWRKAFG 1272
Cdd:cd03250 3 VEDASFTWDSGeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALL------GELEkLSG------SV-SVPGSIA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1273 VIPQKVFIFSGTFRMNL---DPYgqwNDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSRA 1349
Cdd:cd03250 70 YVSQEPWIQNGTIRENIlfgKPF---DEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 1350 KILLLDEPSAHLDPVTS-----QVIRKTLKHafaNCTVILSEHRLEAMLECQRFLVIEDNK 1405
Cdd:cd03250 147 DIYLLDDPLSAVDAHVGrhifeNCILGLLLN---NKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1196-1394 |
7.92e-26 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 107.87 E-value: 7.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1196 TVKDLTAKYGegGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGvswntVSVQQWRKAFGVI 1274
Cdd:COG1121 8 ELENLTVSYG--GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPpTSGTVRLFG-----KPPRRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1275 PQKvFIFSGTF--------RMNLDPYGQW-------NDEEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLM 1339
Cdd:COG1121 81 PQR-AEVDWDFpitvrdvvLMGRYGRRGLfrrpsraDREAVDEALERVGLEDLADRPIGE-----------LSGGQQQRV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1631900066 1340 CLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKH-AFANCTVILSEHRLEAMLE 1394
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVRE 204
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
80-281 |
8.18e-26 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350040 [Multi-domain] Cd Length: 309 Bit Score: 109.51 E-value: 8.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 80 VQPLLLGRIIASYDPDNSDERSIAYYLGIGLCLLFLVRTLLIHPAIFGLHHIGMQMRIAMFSLIYKKILKL--------- 150
Cdd:cd18596 15 APPFFLNRLLRYLEDPGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFEKALRRrdksgssks 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 151 ----------SSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLLWDMLEASAFSGLAFLIVLAFFQ 220
Cdd:cd18596 95 seskkkdkeeDEDEKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSALVGLAVMVLLLPLN 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 221 AWLGQMMMKYRNKRAGKINERLVITSEIIENIQSVKAYCWEDAMEKMIESIRETELKLTRK 281
Cdd:cd18596 175 GYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRK 235
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
415-605 |
8.33e-26 |
|
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: 105.02 E-value: 8.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 415 NFPLHASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGRisfspQVSWIMPGTIKENIIFgvs 494
Cdd:cd00267 6 SFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK-----DIAKLPLEELRRRIGY--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 495 ydeyryksvikacqleediskfpekdytVLGeggiiLSGGQRARISLARAVYKDADLYLLDSPFGHLDIFTEKEIFESCV 574
Cdd:cd00267 78 ----------------------------VPQ-----LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLR 124
|
170 180 190
....*....|....*....|....*....|..
gi 1631900066 575 CKLMANKTRILVTSKLEHL-KIADKILILHEG 605
Cdd:cd00267 125 ELAEEGRTVIIVTHDPELAeLAADRVIVLKDG 156
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
409-611 |
2.18e-25 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 104.32 E-value: 2.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 409 NNLFFSnFPLHASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG------------RISFSPQ 476
Cdd:cd03247 4 NNVSFS-YPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGvpvsdlekalssLISVLNQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 477 VSWIMPGTIKENIifgvsydeyryksvikacqleediskfpekdytvlgegGIILSGGQRARISLARAVYKDADLYLLDS 556
Cdd:cd03247 83 RPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDE 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1631900066 557 PFGHLDIFTEKEIFEScVCKLMANKTRILVTSKLEHLKIADKILILHEGSCYFYG 611
Cdd:cd03247 125 PTVGLDPITERQLLSL-IFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
422-605 |
3.66e-25 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 104.91 E-value: 3.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKI-----------KHSGRISFSPQVSWIMPG-TIKENI 489
Cdd:cd03259 14 RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlidgrdvtgvpPERRNIGMVFQDYALFPHlTVAENI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 490 IFG-----VSYDEY--RYKSVIKACQLEEDISKFPEKdytvlgeggiiLSGGQRARISLARAVYKDADLYLLDSPFGHLD 562
Cdd:cd03259 94 AFGlklrgVPKAEIraRVRELLELVGLEGLLNRYPHE-----------LSGGQQQRVALARALAREPSLLLLDEPLSALD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 563 ------IFTE-KEIFESCvcklmaNKTRILVTSKL-EHLKIADKILILHEG 605
Cdd:cd03259 163 aklreeLREElKELQREL------GITTIYVTHDQeEALALADRIAVMNEG 207
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1211-1403 |
4.88e-25 |
|
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: 112.22 E-value: 4.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1211 VLENISFSIDSGQRVGLLGRTGSGKST---LLFAFLRLlnTEGDIQIDGVSWNTVSVQQWRKAFGVIPQKVFIFSGTFRM 1287
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTlarLLFRFYDV--TSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAY 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1288 NLdPYGQWN--DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSRAKILLLDEPSAHLDPVT 1365
Cdd:COG5265 451 NI-AYGRPDasEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRT 529
|
170 180 190
....*....|....*....|....*....|....*...
gi 1631900066 1366 SQVIRKTLKHAFANCTVILSEHRLEAMLECQRFLVIED 1403
Cdd:COG5265 530 ERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEA 567
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1197-1406 |
5.45e-25 |
|
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: 104.49 E-value: 5.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKYGEGGAAV--LENISFSIDSGQRVGLLGRTGSGKSTLLfAFLRLLN--TEGDIQIDGVSWNTVSVQQW----R 1268
Cdd:cd03255 3 LKNLSKTYGGGGEKVqaLKGVSLSIEKGEFVAIVGPSGSGKSTLL-NILGGLDrpTSGEVRVDGTDISKLSEKELaafrR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1269 KAFGVIPQK---------------VFIFSGTFRMNldpygqwNDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSH 1333
Cdd:cd03255 82 RHIGFVFQSfnllpdltalenvelPLLLAGVPKKE-------RRERAEELLERVGLGDRLNHYPSEL-----------SG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1631900066 1334 GHKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLK--HAFANCTVILSEHRLEAMLECQRFLVIEDNKL 1406
Cdd:cd03255 144 GQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRelNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1172-1423 |
6.26e-25 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 111.34 E-value: 6.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1172 LSDALVIENrhakEEKNWPSG-GKMTVKDLTAKYGEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TE 1249
Cdd:PRK10789 294 LAEAPVVKD----GSEPVPEGrGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDvSE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1250 GDIQIDGVSWNTVSVQQWRKAFGVIPQKVFIFSGTFRMNLdPYGQWN--DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDG 1327
Cdd:PRK10789 370 GDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNI-ALGRPDatQQEIEHVARLASVHDDILRLPQGYDTEVGER 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1328 GCVLSHGHKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFANCTVILSEHRLEAMLECQRFLVIEDNKLR 1407
Cdd:PRK10789 449 GVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIA 528
|
250
....*....|....*.
gi 1631900066 1408 QYESIQKLLNEKSSFR 1423
Cdd:PRK10789 529 QRGNHDQLAQQSGWYR 544
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
409-621 |
9.17e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 111.07 E-value: 9.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 409 NNLFFSnFPLHASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGR-------------ISFSP 475
Cdd:PRK11160 342 NNVSFT-YPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpiadyseaalrqaISVVS 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 476 QVSWIMPGTIKENIIFGV--SYDEyRYKSVIKACQLEEDISKFPEKDyTVLGEGGIILSGGQRARISLARAVYKDADLYL 553
Cdd:PRK11160 421 QRVHLFSATLRDNLLLAApnASDE-ALIEVLQQVGLEKLLEDDKGLN-AWLGEGGRQLSGGEQRRLGIARALLHDAPLLL 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1631900066 554 LDSPFGHLDIFTEKEIFESCVcKLMANKTRILVTSKLEHLKIADKILILHEGSCYFYGTFSELQGQRP 621
Cdd:PRK11160 499 LDEPTEGLDAETERQILELLA-EHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQG 565
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
422-615 |
1.22e-24 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 104.40 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG--------RISFSPQ---VSWIMPGTIKENII 490
Cdd:COG1121 20 PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGkpprrarrRIGYVPQraeVDWDFPITVRDVVL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 491 FGvsydeyRY-------------KSVIKACqLEE-DISKFPEKDytvLGEggiiLSGGQRARISLARAVYKDADLYLLDS 556
Cdd:COG1121 100 MG------RYgrrglfrrpsradREAVDEA-LERvGLEDLADRP---IGE----LSGGQQQRVLLARALAQDPDLLLLDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1631900066 557 PFGHLDIFTEKEIFEscvckLMA-----NKTRILVTSKLEHL-KIADKILILHEGsCYFYGTFSE 615
Cdd:COG1121 166 PFAGVDAATEEALYE-----LLRelrreGKTILVVTHDLGAVrEYFDRVLLLNRG-LVAHGPPEE 224
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1195-1406 |
1.47e-24 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 103.58 E-value: 1.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTAKYGEGGAAV--LENISFSIDSGQRVGLLGRTGSGKSTllfaflrLLN--------TEGDIQIDGVSWNTVSV 1264
Cdd:COG1136 5 LELRNLTKSYGTGEGEVtaLRGVSLSIEAGEFVAIVGPSGSGKST-------LLNilggldrpTSGEVLIDGQDISSLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1265 QQW----RKAFGVIPQkvfifsgTFrmNLDPY-----------------GQWNDEEIWKVAEEVGLKSVIEQFPGQldfv 1323
Cdd:COG1136 78 RELarlrRRHIGFVFQ-------FF--NLLPEltalenvalplllagvsRKERRERARELLERVGLGDRLDHRPSQ---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1324 lvdggcvLSHGHKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLK--HAFANCTVILSEHRLEAMLECQRFLVI 1401
Cdd:COG1136 145 -------LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRelNRELGTTIVMVTHDPELAARADRVIRL 217
|
....*
gi 1631900066 1402 EDNKL 1406
Cdd:COG1136 218 RDGRI 222
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
419-631 |
1.55e-24 |
|
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: 103.92 E-value: 1.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 419 HASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG-------------RISFSPQVSWIMPG-T 484
Cdd:cd03295 12 GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGYVIQQIGLFPHmT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 485 IKENI-----IFGVSYDEY--RYKSVIKACQLEED--ISKFPEKdytvlgeggiiLSGGQRARISLARAVYKDADLYLLD 555
Cdd:cd03295 92 VEENIalvpkLLKWPKEKIreRADELLALVGLDPAefADRYPHE-----------LSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1631900066 556 SPFGHLDIFTEKEIFESCV-CKLMANKTRILVTSKL-EHLKIADKILILHEGSCYFYGTFSE-LQGQRPDFSSELMGFD 631
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKrLQQELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEiLRSPANDFVAEFVGAD 239
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1195-1405 |
1.59e-24 |
|
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: 101.88 E-value: 1.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTAKYGEggAAVLENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLN-----TEGDIQIDGVSWNTVS--VQQW 1267
Cdd:cd03229 1 LELKNVSKRYGQ--KTVLNDVSLNIEAGEIVALLGPSGSGKSTL----LRCIAgleepDSGSILIDGEDLTDLEdeLPPL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1268 RKAFGVIPQKVFIFSgtfRMNldpygqwndeeiwkVAEEVGLksvieqfpgqldfvlvdggcVLSHGHKQLMCLARSVLS 1347
Cdd:cd03229 75 RRRIGMVFQDFALFP---HLT--------------VLENIAL--------------------GLSGGQQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 1348 RAKILLLDEPSAHLDPVTSQVIRKTLKHAFAN--CTVILSEHRL-EAMLECQRFLVIEDNK 1405
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLdEAARLADRVVVLRDGK 178
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
897-1424 |
2.74e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 110.20 E-value: 2.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 897 TSAYYIIYIYvGVADTLLAMgiFRGLPLVHTLITVSKTLHQKMVHAVLHAPMSTFNSWKAGGMLNRFAKDTAVLDDLLPL 976
Cdd:TIGR00958 201 ASAIFFMCLL-SIASSVSAG--LRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 977 TVFDFVQLILIVIGAITVVSILQPYI----FLASVPVIAAFIVLRAYFLHTSQQLKqlESEARSpifTHLV-TSLKGLWT 1051
Cdd:TIGR00958 278 NVNVLLRNLVMLLGLLGFMLWLSPRLtmvtLINLPLVFLAEKVFGKRYQLLSEELQ--EAVAKA---NQVAeEALSGMRT 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1052 LRAFGRQPYFETLFHKALN-LHTANW------FLYLSTLRWFQMRIEIIFVVFFVAVAFISIITTGDgpgrvgiILTLAM 1124
Cdd:TIGR00958 353 VRSFAAEEGEASRFKEALEeTLQLNKrkalayAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGN-------LVSFLL 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1125 NIMGTLQWAVNSSIDVDSLMRSVG---RIFKFIDMpteemkniKPQKKNQLSDAlvienrhakeeknwPSG--GKMTVKD 1199
Cdd:TIGR00958 426 YQEQLGEAVRVLSYVYSGMMQAVGaseKVFEYLDR--------KPNIPLTGTLA--------------PLNleGLIEFQD 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1200 LTAKY-GEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSVQQWRKAFGVIPQK 1277
Cdd:TIGR00958 484 VSFSYpNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQpTGGQVLLDGVPLVQYDHHYLHRQVALVGQE 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1278 VFIFSGTFRMNLdPYG--QWNDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSRAKILLLD 1355
Cdd:TIGR00958 564 PVLFSGSVRENI-AYGltDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILD 642
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1631900066 1356 EPSAHLDPVTSQVIRKTLKhaFANCTVILSEHRLEAMLECQRFLVIEDNKLRQYESIQKLLNEKSSFRQ 1424
Cdd:TIGR00958 643 EATSALDAECEQLLQESRS--RASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKH 709
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1196-1406 |
2.80e-24 |
|
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: 102.97 E-value: 2.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1196 TVKDLTAKYGEGGAAV--LENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLL-NTEGDIQIDGVSWNTVSVQQ---WRK 1269
Cdd:cd03257 3 EVKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLkPTSGSIIFDGKDLLKLSRRLrkiRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1270 AFGVIPQKVF-----------IFSGTFRMNLDPYGQW-NDEEIWKVAEEVGL-KSVIEQFPGQldfvlvdggcvLSHGHK 1336
Cdd:cd03257 83 EIQMVFQDPMsslnprmtigeQIAEPLRIHGKLSKKEaRKEAVLLLLVGVGLpEEVLNRYPHE-----------LSGGQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1631900066 1337 QLMCLARSVLSRAKILLLDEPSAHLDPVT-SQVIR--KTLKHAFaNCTVILSEHRLEAMLE-CQRFLVIEDNKL 1406
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVSVqAQILDllKKLQEEL-GLTLLFITHDLGVVAKiADRVAVMYAGKI 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1197-1417 |
4.63e-24 |
|
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: 102.75 E-value: 4.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKYGegGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSVQQW---RKAFG 1272
Cdd:COG1127 8 VRNLTKSFG--DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRpDSGEILVDGQDITGLSEKELyelRRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1273 VipqkVF----IFSGtfrMN--------LDPYGQWNDEEIWKVAEE----VGLKSVIEQFPGQLdfvlvDGGcvlshghk 1336
Cdd:COG1127 86 M----LFqggaLFDS---LTvfenvafpLREHTDLSEAEIRELVLEklelVGLPGAADKMPSEL-----SGG-------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1337 qlMC----LARSVLSRAKILLLDEPSAHLDPVTSQVIR---KTLKHAFaNCTVILSEHRLEAMLE-CQRFLVIEDNKLRQ 1408
Cdd:COG1127 146 --MRkrvaLARALALDPEILLYDEPTAGLDPITSAVIDeliRELRDEL-GLTSVVVTHDLDSAFAiADRVAVLADGKIIA 222
|
....*....
gi 1631900066 1409 YESIQKLLN 1417
Cdd:COG1127 223 EGTPEELLA 231
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1197-1406 |
5.58e-24 |
|
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: 102.19 E-value: 5.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKYGegGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSV---QQWRKAFG 1272
Cdd:cd03261 3 LRGLTKSFG--GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRpDSGEVLIDGEDISGLSEaelYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1273 VIPQKVFIFSG-TFRMN----LDPYGQWNDEEIWKVAEE----VGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLAR 1343
Cdd:cd03261 81 MLFQSGALFDSlTVFENvafpLREHTRLSEEEIREIVLEkleaVGLRGAEDLYPAE-----------LSGGMKKRVALAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1631900066 1344 SVLSRAKILLLDEPSAHLDPVTSQVIR---KTLKHAFaNCTVILSEHRLEAMLE-CQRFLVIEDNKL 1406
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDPIASGVIDdliRSLKKEL-GLTSIMVTHDLDTAFAiADRIAVLYDGKI 215
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
415-619 |
6.26e-24 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 108.26 E-value: 6.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 415 NFPLHASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIK-HS------------GRISFSPQVSWIM 481
Cdd:PRK10789 322 TYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRfHDipltklqldswrSRLAVVSQTPFLF 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 482 PGTIKENIIFG---VSYDEYRYksVIKACQLEEDISKFPEKDYTVLGEGGIILSGGQRARISLARAVYKDADLYLLDSPF 558
Cdd:PRK10789 402 SDTVANNIALGrpdATQQEIEH--VARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDAL 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 559 GHLDIFTEKEIFEScVCKLMANKTRILVTSKLEHLKIADKILILHEGSCYFYGTFSELQGQ 619
Cdd:PRK10789 480 SAVDGRTEHQILHN-LRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQ 539
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1197-1394 |
9.76e-24 |
|
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: 100.69 E-value: 9.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKYGegGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLL-NTEGDIQIDGvswntVSVQQWRKAFGVIP 1275
Cdd:cd03235 2 VEDLTVSYG--GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLkPTSGSIRVFG-----KPLEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1276 QKvFIFSGTF--------RMNLDPY---GQWNDEEIWKVAEE----VGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMC 1340
Cdd:cd03235 75 QR-RSIDRDFpisvrdvvLMGLYGHkglFRRLSKADKAKVDEalerVGLSELADRQIGE-----------LSGGQQQRVL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1631900066 1341 LARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKH-AFANCTVILSEHRLEAMLE 1394
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLE 197
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1197-1406 |
1.51e-23 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 101.29 E-value: 1.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKYGeGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLfaflRLLN-----TEGDIQIDGVSWNTVS---VQQWR 1268
Cdd:COG3638 5 LRNLSKRYP-GGTPALDDVSLEIERGEFVALIGPSGAGKSTLL----RCLNglvepTSGEILVDGQDVTALRgraLRRLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1269 KAFGVIPQK--------VF--IFSG------TFRMNLdpyGQWNDEEIWKVA---EEVGLKSVIEQFPGQLdfvlvdggc 1329
Cdd:COG3638 80 RRIGMIFQQfnlvprlsVLtnVLAGrlgrtsTWRSLL---GLFPPEDRERALealERVGLADKAYQRADQL--------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1330 vlSHGHKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFA--NCTVILSEHRLE-AMLECQRFLVIEDNKL 1406
Cdd:COG3638 148 --SGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDlARRYADRIIGLRDGRV 225
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
422-605 |
3.64e-23 |
|
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: 97.85 E-value: 3.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKhsgrisfspqvswimpgtikeniIFGVSYDEYRYK 501
Cdd:cd03230 14 TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIK-----------------------VLGKDIKKEPEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 502 SVIKACQLEEDISKFPekDYTVlgEGGIILSGGQRARISLARAVYKDADLYLLDSPFGHLDIFTEKEIFESCVcKLMANK 581
Cdd:cd03230 71 VKRRIGYLPEEPSLYE--NLTV--RENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLR-ELKKEG 145
|
170 180
....*....|....*....|....*.
gi 1631900066 582 TRILVTS-KLEHL-KIADKILILHEG 605
Cdd:cd03230 146 KTILLSShILEEAeRLCDRVAILNNG 171
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1198-1406 |
5.55e-23 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 98.97 E-value: 5.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1198 KDLTAKYGeGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLfaflRLLN-----TEGDIQIDGVSWNTVS---VQQWRK 1269
Cdd:COG2884 5 ENVSKRYP-GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLL----KLLYgeerpTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1270 AFGVIPQkvfifsgTFR--MNLDPY----------GqWNDEEIWKVAEE----VGLKSVIEQFPGQLdfvlvdggcvlSH 1333
Cdd:COG2884 80 RIGVVFQ-------DFRllPDRTVYenvalplrvtG-KSRKEIRRRVREvldlVGLSDKAKALPHEL-----------SG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1631900066 1334 GHKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLK--HAfANCTVILSEHRLEAMLECQ-RFLVIEDNKL 1406
Cdd:COG2884 141 GEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEeiNR-RGTTVLIATHDLELVDRMPkRVLELEDGRL 215
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1196-1417 |
5.99e-23 |
|
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: 99.19 E-value: 5.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1196 TVKDLTAKYGEGGAAV--LENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLN-----TEGDIQIDGVSWNTVS---VQ 1265
Cdd:cd03258 3 ELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTL----IRCINglerpTSGSVLVDGTDLTLLSgkeLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1266 QWRKAFGVIPQKVFIFSG-TFRMN----LDPYGqWNDEEIWKVAEE----VGLKSVIEQFPGQldfvlvdggcvLSHGHK 1336
Cdd:cd03258 79 KARRRIGMIFQHFNLLSSrTVFENvalpLEIAG-VPKAEIEERVLEllelVGLEDKADAYPAQ-----------LSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1337 QLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLK--HAFANCTVILSEHRLEAMLE-CQRFLVIEDNKLRQYESIQ 1413
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPETTQSILALLRdiNRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVE 226
|
....
gi 1631900066 1414 KLLN 1417
Cdd:cd03258 227 EVFA 230
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
422-602 |
7.55e-23 |
|
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: 98.31 E-value: 7.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKI--------KHSGRISFSPQVSWIMP-GTIKENIIFG 492
Cdd:cd03293 18 TALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVlvdgepvtGPGPDRGYVFQQDALLPwLTVLDNVALG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 493 -----VSYDEYRYK--SVIKACQLEEDISKFPEKdytvlgeggiiLSGGQRARISLARAVYKDADLYLLDSPFGHLDIFT 565
Cdd:cd03293 98 lelqgVPKAEARERaeELLELVGLSGFENAYPHQ-----------LSGGMRQRVALARALAVDPDVLLLDEPFSALDALT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1631900066 566 EKEIFEScvckLMA-----NKTRILVTSKL-EHLKIADKILIL 602
Cdd:cd03293 167 REQLQEE----LLDiwretGKTVLLVTHDIdEAVFLADRVVVL 205
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
422-602 |
8.10e-23 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 99.39 E-value: 8.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGRI--SFSPQVSWI------MP-GTIKENIIFG 492
Cdd:COG1116 25 TALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPvtGPGPDRGVVfqepalLPwLTVLDNVALG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 493 -----VSYDEYRYK--SVIKACQLEEDISKFPekdytvlGEggiiLSGGQRARISLARAVYKDADLYLLDSPFGHLDIFT 565
Cdd:COG1116 105 lelrgVPKAERRERarELLELVGLAGFEDAYP-------HQ----LSGGMRQRVAIARALANDPEVLLMDEPFGALDALT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1631900066 566 eKEIFESCVCKLMA--NKTRILVTskleH-----LKIADKILIL 602
Cdd:COG1116 174 -RERLQDELLRLWQetGKTVLFVT----HdvdeaVFLADRVVVL 212
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
422-605 |
8.94e-23 |
|
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: 98.33 E-value: 8.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGR-----------------ISFSPQVSWIMPG- 483
Cdd:cd03255 18 QALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdisklsekelaafrrrhIGFVFQSFNLLPDl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 484 TIKENI-----IFGVSYDEY--RYKSVIKACQLEEDISKFPEKdytvlgeggiiLSGGQRARISLARAVYKDADLYLLDS 556
Cdd:cd03255 98 TALENVelpllLAGVPKKERreRAEELLERVGLGDRLNHYPSE-----------LSGGQQQRVAIARALANDPKIILADE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1631900066 557 PFGHLDIFTEKEIFEscvckLM------ANKTRILVTSKLEHLKIADKILILHEG 605
Cdd:cd03255 167 PTGNLDSETGKEVME-----LLrelnkeAGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1195-1403 |
1.11e-22 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 97.55 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTAKYGEggAAVLENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLL-----NTEGDIQIDGVSWNTvSVQQWRK 1269
Cdd:COG4133 3 LEAENLSCRRGE--RLLFSGLSFTLAAGEALALTGPNGSGKTTL----LRILagllpPSAGEVLWNGEPIRD-AREDYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1270 AFGVIPQKVFIFSG-TFRMNLDPY-----GQWNDEEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLAR 1343
Cdd:COG4133 76 RLAYLGHADGLKPElTVRENLRFWaalygLRADREAIDEALEAVGLAGLADLPVRQ-----------LSAGQKRRVALAR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 1344 SVLSRAKILLLDEPSAHLDPVTSQVIRKTLK-HAFANCTVILSEHRLEAMLECQRfLVIED 1403
Cdd:COG4133 145 LLLSPAPLWLLDEPFTALDAAGVALLAELIAaHLARGGAVLLTTHQPLELAAARV-LDLGD 204
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1196-1403 |
1.12e-22 |
|
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: 103.83 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1196 TVKDLTAKYGEGGA---AVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVS---VQQWR 1268
Cdd:COG1123 262 EVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRpTSGSILFDGKDLTKLSrrsLRELR 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1269 KAFGVIPQkvfifsgtfrmnlDPYGQ--------------------WNDEEIWKVAEE----VGL-KSVIEQFPGQldfv 1323
Cdd:COG1123 342 RRVQMVFQ-------------DPYSSlnprmtvgdiiaeplrlhglLSRAERRERVAEllerVGLpPDLADRYPHE---- 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1324 lvdggcvLSHGHKQLMCLARSVLSRAKILLLDEPSAHLDP-VTSQVIR--KTLKHAFaNCTVILSEHRLEAMLE-CQRFL 1399
Cdd:COG1123 405 -------LSGGQRQRVAIARALALEPKLLILDEPTSALDVsVQAQILNllRDLQREL-GLTYLFISHDLAVVRYiADRVA 476
|
....
gi 1631900066 1400 VIED 1403
Cdd:COG1123 477 VMYD 480
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
396-616 |
1.83e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 104.42 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 396 NQENNNSKAPSTDNNLF-FSN----FPLHAS-PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG 469
Cdd:TIGR00958 463 NIPLTGTLAPLNLEGLIeFQDvsfsYPNRPDvPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDG 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 470 -------------RISFSPQVSWIMPGTIKENIIFGVSY-DEYRYKSVIKACQLEEDISKFPEKDYTVLGEGGIILSGGQ 535
Cdd:TIGR00958 543 vplvqydhhylhrQVALVGQEPVLFSGSVRENIAYGLTDtPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQ 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 536 RARISLARAVYKDADLYLLDSPFGHLDIFTEKEIFEScvcKLMANKTRILVTSKLEHLKIADKILILHEGSCYFYGTFSE 615
Cdd:TIGR00958 623 KQRIAIARALVRKPRVLILDEATSALDAECEQLLQES---RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQ 699
|
.
gi 1631900066 616 L 616
Cdd:TIGR00958 700 L 700
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1197-1390 |
2.08e-22 |
|
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: 97.64 E-value: 2.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKYGEGgaAVLENISFSIDSGQRVGLLGRTGSGKSTllfaFLRLLN----------TEGDIQIDG--VSWNTVSV 1264
Cdd:cd03260 3 LRDLNVYYGDK--HALKDISLDIPKGEITALIGPSGCGKST----LLRLLNrlndlipgapDEGEVLLDGkdIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1265 QQWRKAFGVIPQKVFIFSGTFRMNLD----PYGQWNDEEIWKVAEEVgLKSVieQFPGQLDFVLVDGGcvLSHGHKQLMC 1340
Cdd:cd03260 77 LELRRRVGMVFQKPNPFPGSIYDNVAyglrLHGIKLKEELDERVEEA-LRKA--ALWDEVKDRLHALG--LSGGQQQRLC 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1341 LARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFANCTVILSEHRLE 1390
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQ 201
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
416-605 |
2.89e-22 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 96.42 E-value: 2.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 416 FPLHASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG-------------RISFSPQVSWIMP 482
Cdd:COG4619 8 FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkplsampppewrrQVAYVPQEPALWG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 483 GTIKENIIFGVSYDEYRY-----KSVIKACQLEEDISKFPEKDytvlgeggiiLSGGQRARISLARAVYKDADLYLLDSP 557
Cdd:COG4619 88 GTVRDNLPFPFQLRERKFdreraLELLERLGLPPDILDKPVER----------LSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 558 FGHLDIFTeKEIFESCVCKLMANKTR--ILVT-SKLEHLKIADKILILHEG 605
Cdd:COG4619 158 TSALDPEN-TRRVEELLREYLAEEGRavLWVShDPEQIERVADRVLTLEAG 207
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1195-1401 |
2.97e-22 |
|
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: 96.77 E-value: 2.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTAKYGEGGAA--VLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGvswntVSVQQWRKAF 1271
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERpTSGEVLVDG-----EPVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1272 GVIPQK--VF---------IFSgtFRMNLDPYGQWnDEEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMC 1340
Cdd:cd03293 76 GYVFQQdaLLpwltvldnvALG--LELQGVPKAEA-RERAEELLELVGLSGFENAYPHQ-----------LSGGMRQRVA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1341 LARSVLSRAKILLLDEPSAHLDPVT--------SQVIRKTLKhafancTVILSEHRL-EAMLECQRFLVI 1401
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDALTreqlqeelLDIWRETGK------TVLLVTHDIdEAVFLADRVVVL 205
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
409-605 |
4.05e-22 |
|
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: 96.00 E-value: 4.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 409 NNLFFSnFPLHASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKI-------------KHSGRISF-- 473
Cdd:cd03225 3 KNLSFS-YPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVlvdgkdltklslkELRRKVGLvf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 474 -SPQVSWIMPgTIKENIIFG-----VSYDEY--RYKSVIKACQLEEDISKFPEKdytvlgeggiiLSGGQRARISLARAV 545
Cdd:cd03225 82 qNPDDQFFGP-TVEEEVAFGlenlgLPEEEIeeRVEEALELVGLEGLRDRSPFT-----------LSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1631900066 546 YKDADLYLLDSPFGHLDIFTEKEIFEScVCKLMA-NKTRILVTSKLEHLK-IADKILILHEG 605
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLEL-LKKLKAeGKTIIIVTHDLDLLLeLADRVIVLEDG 210
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1196-1407 |
1.01e-21 |
|
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: 94.98 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1196 TVKDLTAKYGEGgaAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSvQQWRKAFGVI 1274
Cdd:cd03268 2 KTNDLTKTYGKK--RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKpDSGEITFDGKSYQKNI-EALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1275 PQKVFIFSGTFRMNLDPYG---QWNDEEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSRAKI 1351
Cdd:cd03268 79 EAPGFYPNLTARENLRLLArllGIRKKRIDEVLDVVGLKDSAKKKVKG-----------FSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1631900066 1352 LLLDEPSAHLDPVTSQVIRKTL-KHAFANCTVILSEHRLEAM-LECQRFLVIEDNKLR 1407
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELIlSLRDQGITVLISSHLLSEIqKVADRIGIINKGKLI 205
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
413-605 |
1.50e-21 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 97.91 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 413 FSNFPLhaspvLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGRISF---SPQ---VSWI------ 480
Cdd:COG1118 12 FGSFTL-----LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtnlPPRerrVGFVfqhyal 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 481 ---MpgTIKENIIFGVSyDEYRYKSVIKAC--------QLEEDISKFPEKdytvlgeggiiLSGGQRARISLARAVYKDA 549
Cdd:COG1118 87 fphM--TVAENIAFGLR-VRPPSKAEIRARveellelvQLEGLADRYPSQ-----------LSGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1631900066 550 DLYLLDSPFGHLDIFTEKEIfEScvcKLMA-----NKTRILVT-SKLEHLKIADKILILHEG 605
Cdd:COG1118 153 EVLLLDEPFGALDAKVRKEL-RR---WLRRlhdelGGTTVFVThDQEEALELADRVVVMNQG 210
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1196-1405 |
1.68e-21 |
|
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: 95.33 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1196 TVKDLTAKYGEGGAAvLENISFSIDSGQRVGLLGRTGSGKSTLLfaflRLLN-----TEGDIQIDGV---SWNTVSVQQW 1267
Cdd:cd03256 2 EVENLSKTYPNGKKA-LKDVSLSINPGEFVALIGPSGAGKSTLL----RCLNglvepTSGSVLIDGTdinKLKGKALRQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1268 RKAFGVIPQK--------VF--IFSGTF-RMNLDP--YGQWNDEEIWKVA---EEVGLKSVIEQFPGQLdfvlvdggcvl 1331
Cdd:cd03256 77 RRQIGMIFQQfnlierlsVLenVLSGRLgRRSTWRslFGLFPKEEKQRALaalERVGLLDKAYQRADQL----------- 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1631900066 1332 SHGHKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLK--HAFANCTVILSEHRLE-AMLECQRFLVIEDNK 1405
Cdd:cd03256 146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKriNREEGITVIVSLHQVDlAREYADRIVGLKDGR 222
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
422-588 |
2.31e-21 |
|
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: 93.70 E-value: 2.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG------RISFSPQVSWIMPG-------TIKEN 488
Cdd:COG4133 16 LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaREDYRRRLAYLGHAdglkpelTVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 489 IIF-----GVSYDEYRYKSVIKACQLEEDISKFPEKdytvlgeggiiLSGGQRARISLARAVYKDADLYLLDSPFGHLDI 563
Cdd:COG4133 96 LRFwaalyGLRADREAIDEALEAVGLAGLADLPVRQ-----------LSAGQKRRVALARLLLSPAPLWLLDEPFTALDA 164
|
170 180
....*....|....*....|....*
gi 1631900066 564 fTEKEIFESCVCKLMANKTRILVTS 588
Cdd:COG4133 165 -AGVALLAELIAAHLARGGAVLLTT 188
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
104-285 |
3.30e-21 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 1 (TMD1) 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: 350036 [Multi-domain] Cd Length: 287 Bit Score: 95.71 E-value: 3.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 104 YYLGIGLCL-LFL---VRTLLIHPAIFGLHHIGMQMRIAMFSLIYKKILKLSSrvLDKISTGQLVSLLSNNLNKFDEGLA 179
Cdd:cd18592 35 VWYGILLVLgLFLtelLRSLFFSLTWAISYRTGIRLRGAVLGLLYKKILRLRS--LGDKSVGELINIFSNDGQRLFDAAV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 180 LAHFVWIAPLQVALLMGLLWDMLEASAFSGLAFLIVLAFFQAWLGQMMMKYRNKRAGKINERLVITSEIIENIQSVKAYC 259
Cdd:cd18592 113 FGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAKLTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYA 192
|
170 180
....*....|....*....|....*.
gi 1631900066 260 WEDAMEKMIESIRETELKLTRKAAYV 285
Cdd:cd18592 193 WEKPFAKKIADIRKEERKILEKAGYL 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1196-1402 |
4.84e-21 |
|
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: 93.27 E-value: 4.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1196 TVKDLTAKYGEggAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSVQQwRKAFGV- 1273
Cdd:cd03224 2 EVENLNAGYGK--SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPpRSGSIRFDGRDITGLPPHE-RARAGIg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1274 -IPQKVFIFSG-TFRMNLD--PYGQWNDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdGGcVLSHGHKQLMCLARSVLSRA 1349
Cdd:cd03224 79 yVPEGRRIFPElTVEENLLlgAYARRRAKRKARLERVYELFPRLKERRKQL------AG-TLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1631900066 1350 KILLLDEPSAHLDPVTSQVIRKTLKH-AFANCTVILSEHRLEAMLE-CQRFLVIE 1402
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRElRDEGVTILLVEQNARFALEiADRAYVLE 206
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1196-1406 |
5.41e-21 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 94.83 E-value: 5.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1196 TVKDLTAKYGEGGA---AVLENISFSIDSGQRVGLLGRTGSGKSTLLfaflRLLN-----TEGDIQIDGVSWNT---VSV 1264
Cdd:TIGR04521 2 KLKNVSYIYQPGTPfekKALDDVSLTIEDGEFVAIIGHTGSGKSTLI----QHLNgllkpTSGTVTIDGRDITAkkkKKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1265 QQWRKAFGVipqkVF------IFSGTFR-------MNLDpygqWNDEEIWKVAEE----VGL-KSVIEQFPGQLdfvlvd 1326
Cdd:TIGR04521 78 KDLRKKVGL----VFqfpehqLFEETVYkdiafgpKNLG----LSEEEAEERVKEalelVGLdEEYLERSPFEL------ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1327 ggcvlSHGHKQLMCLArSVLS-RAKILLLDEPSAHLDPVTSQVIRKTLK--HAFANCTVILSEHRLEAMLE-CQRFLVIE 1402
Cdd:TIGR04521 144 -----SGGQMRRVAIA-GVLAmEPEVLILDEPTAGLDPKGRKEILDLFKrlHKEKGLTVILVTHSMEDVAEyADRVIVMH 217
|
....
gi 1631900066 1403 DNKL 1406
Cdd:TIGR04521 218 KGKI 221
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1193-1422 |
7.04e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 98.88 E-value: 7.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1193 GKMTVKDLTAKYGEGGAAVlENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSVQQWRKAF 1271
Cdd:PRK13657 333 GAVEFDDVSFSYDNSRQGV-EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDpQSGRILIDGTDIRTVTRASLRRNI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1272 GVIPQKVFIFSGTFRMNLDpYGQWN--DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSRA 1349
Cdd:PRK13657 412 AVVFQDAGLFNRSIEDNIR-VGRPDatDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDP 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1631900066 1350 KILLLDEPSAHLDPVTSQVIRKTLKHAFANCTVILSEHRLEAMLECQRFLVIEDNKLRQYESIQKLLNEKSSF 1422
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRF 563
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
423-630 |
8.78e-21 |
|
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: 93.17 E-value: 8.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 423 VLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG-----------RISFSPQVSWIMPG-TIKENII 490
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGkditnlppekrDISYVPQNYALFPHmTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 491 FGVsydeyRYKSVIKAcQLEE---DISKFPEKDYtVLGEGGIILSGGQRARISLARAVYKDADLYLLDSPFGHLDIFT-E 566
Cdd:cd03299 94 YGL-----KKRKVDKK-EIERkvlEIAEMLGIDH-LLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTkE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1631900066 567 KEIFESCVCKLMANKTRILVTSKLEHLKI-ADKILILHEGSCYFYGTFSE-LQGQRPDFSSELMGF 630
Cdd:cd03299 167 KLREELKKIRKEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEvFKKPKNEFVAEFLGF 232
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1197-1407 |
1.20e-20 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 93.26 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKYGEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLN-----TEGDIQIDGvsWNTVSVQQ-W--R 1268
Cdd:TIGR04520 3 VENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTL----AKLLNglllpTSGKVTVDG--LDTLDEENlWeiR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1269 KAFGVI---PQKVFIfSGTFR---------MNLDPygqwndEEIWK----VAEEVGLKSVIEQFPGQldfvlvdggcvLS 1332
Cdd:TIGR04520 77 KKVGMVfqnPDNQFV-GATVEddvafglenLGVPR------EEMRKrvdeALKLVGMEDFRDREPHL-----------LS 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1631900066 1333 HGHKQLMCLArSVLS-RAKILLLDEPSAHLDPVTSQVIRKTLK--HAFANCTVILSEHRLEAMLECQRFLVIEDNKLR 1407
Cdd:TIGR04520 139 GGQKQRVAIA-GVLAmRPDIIILDEATSMLDPKGRKEVLETIRklNKEEGITVISITHDMEEAVLADRVIVMNKGKIV 215
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
422-616 |
1.21e-20 |
|
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: 92.40 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG-------------RISF---SPQVSWIMPgTI 485
Cdd:COG1122 15 PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkknlrelrrKVGLvfqNPDDQLFAP-TV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 486 KENIIFG-----VSYDEYRyKSVIKAcqLEE-DISKFPEKD-YTvlgeggiiLSGGQRARISLARAVYKDADLYLLDSPF 558
Cdd:COG1122 94 EEDVAFGpenlgLPREEIR-ERVEEA--LELvGLEHLADRPpHE--------LSGGQKQRVAIAGVLAMEPEVLVLDEPT 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 559 GHLDIFTEKEIFEsCVCKL-MANKTRILVTSKLEHL-KIADKILILHEGSCYFYGTFSEL 616
Cdd:COG1122 163 AGLDPRGRRELLE-LLKRLnKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREV 221
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
410-616 |
2.69e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 97.01 E-value: 2.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 410 NLFFSnFPLHASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG-------------RISFSPQ 476
Cdd:PRK11176 346 NVTFT-YPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlrdytlaslrnQVALVSQ 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 477 VSWIMPGTIKENIIFGVSyDEYRYKSVIKACQLE---EDISKFPEKDYTVLGEGGIILSGGQRARISLARAVYKDADLYL 553
Cdd:PRK11176 425 NVHLFNDTIANNIAYART-EQYSREQIEEAARMAyamDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILI 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1631900066 554 LDSPFGHLDIFTEKEIfESCVCKLMANKTRILVTSKLEHLKIADKILILHEGSCYFYGTFSEL 616
Cdd:PRK11176 504 LDEATSALDTESERAI-QAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAEL 565
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1197-1415 |
3.78e-20 |
|
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: 90.64 E-value: 3.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKYGEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLN-----TEGDIQIDGVSWNTvSVQQWRKAF 1271
Cdd:cd03263 3 IRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTT----LKMLTgelrpTSGTAYINGYSIRT-DRKAARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1272 GVIPQKVFIFSG-TFRMNLDPYGQW-------NDEEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLAR 1343
Cdd:cd03263 78 GYCPQFDALFDElTVREHLRFYARLkglpkseIKEEVELLLRVLGLTDKANKRART-----------LSGGMKRKLSLAI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1631900066 1344 SVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFANCTVILSEHRL-EAMLECQRFLVIEDNKLRQYESIQKL 1415
Cdd:cd03263 147 ALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMdEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
422-605 |
4.03e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 93.60 E-value: 4.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGRIsfspqVSWIMPG-----------------T 484
Cdd:COG3839 17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRD-----VTDLPPKdrniamvfqsyalyphmT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 485 IKENIIFG-----VSYDEY--RYKSVIKACQLEEDISKFPEKdytvlgeggiiLSGGQRARISLARAVYKDADLYLLDSP 557
Cdd:COG3839 92 VYENIAFPlklrkVPKAEIdrRVREAAELLGLEDLLDRKPKQ-----------LSGGQRQRVALGRALVREPKVFLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 558 FGHLD------IFTE-KEIFEscvcKLmaNKTRILVTskleH-----LKIADKILILHEG 605
Cdd:COG3839 161 LSNLDaklrveMRAEiKRLHR----RL--GTTTIYVT----HdqveaMTLADRIAVMNDG 210
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
422-571 |
4.22e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 91.68 E-value: 4.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGRISFSP--------QVSWIMP-GTIKENIIF- 491
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPgaergvvfQNEGLLPwRNVQDNVAFg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 492 ----GVSYDEYRYKS--VIKACQLEEDISKFPEKdytvlgeggiiLSGGQRARISLARAVYKDADLYLLDSPFGHLDIFT 565
Cdd:PRK11248 95 lqlaGVEKMQRLEIAhqMLKKVGLEGAEKRYIWQ-----------LSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
|
....*.
gi 1631900066 566 EKEIFE 571
Cdd:PRK11248 164 REQMQT 169
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
422-612 |
4.96e-20 |
|
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: 91.26 E-value: 4.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG-------------RISFSPQVSwIMPG--TIK 486
Cdd:COG1120 15 PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrrelarRIAYVPQEP-PAPFglTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 487 ENIIFGvsydeyRY-------------KSVIKACqLEE-DISKFPEKDYTVLgeggiilSGGQRARISLARAVYKDADLY 552
Cdd:COG1120 94 ELVALG------RYphlglfgrpsaedREAVEEA-LERtGLEHLADRPVDEL-------SGGERQRVLIARALAQEPPLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1631900066 553 LLDSPFGHLDIFTEKEIFEsCVCKL--MANKTRILVTSKLEH-LKIADKILILHEGSCYFYGT 612
Cdd:COG1120 160 LLDEPTSHLDLAHQLEVLE-LLRRLarERGRTVVMVLHDLNLaARYADRLVLLKDGRIVAQGP 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
422-571 |
5.57e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 90.11 E-value: 5.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKI----KHSGRISFS------------PQVSWIMPG-T 484
Cdd:COG2884 16 EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVlvngQDLSRLKRReipylrrrigvvFQDFRLLPDrT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 485 IKENIIF-----GVSYDEYRYK--SVIKACQLEEDISKFPEKdytvlgeggiiLSGGQRARISLARAVYKDADLYLLDSP 557
Cdd:COG2884 96 VYENVALplrvtGKSRKEIRRRvrEVLDLVGLSDKAKALPHE-----------LSGGEQQRVAIARALVNRPELLLADEP 164
|
170
....*....|....
gi 1631900066 558 FGHLDIFTEKEIFE 571
Cdd:COG2884 165 TGNLDPETSWEIME 178
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1196-1432 |
8.84e-20 |
|
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: 90.44 E-value: 8.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1196 TVKDLTAKYGEGGAAVlENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSVQQWRKAFGVI 1274
Cdd:cd03295 2 EFENVTKRYGGGKKAV-NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEpTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1275 PQKVFIFSG-TFRMN--LDPYGQ-WNDEEIWKVAEE----VGL--KSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARS 1344
Cdd:cd03295 81 IQQIGLFPHmTVEENiaLVPKLLkWPKEKIRERADEllalVGLdpAEFADRYPHE-----------LSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1345 VLSRAKILLLDEPSAHLDPVTsqviRKTLKHAFANC------TVILSEHRL-EAMLECQRFLVIEDNKLRQYESIQKLL- 1416
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPIT----RDQLQEEFKRLqqelgkTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILr 225
|
250
....*....|....*.
gi 1631900066 1417 NEKSSFRQAISHADRL 1432
Cdd:cd03295 226 SPANDFVAEFVGADRL 241
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
413-616 |
1.63e-19 |
|
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: 89.32 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 413 FSNFPlhaspVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGR-----------ISFSPQVSWIM 481
Cdd:cd03296 12 FGDFV-----ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEdatdvpvqernVGFVFQHYALF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 482 PG-TIKENIIFGV---------SYDEYRYK--SVIKACQLEEDISKFPEKdytvlgeggiiLSGGQRARISLARAVYKDA 549
Cdd:cd03296 87 RHmTVFDNVAFGLrvkprserpPEAEIRAKvhELLKLVQLDWLADRYPAQ-----------LSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 550 DLYLLDSPFGHLDIFTEKEIfESCVCKLM--ANKTRILVT-SKLEHLKIADKILILHEGSCYFYGTFSEL 616
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKEL-RRWLRRLHdeLHVTTVFVThDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
423-605 |
1.79e-19 |
|
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: 87.63 E-value: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 423 VLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKI---------------KHSGRISFSPQVSWIMPG-TIK 486
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSIlidgedltdledelpPLRRRIGMVFQDFALFPHlTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 487 ENIIFGvsydeyryksvikacqleediskfpekdytvlgeggiiLSGGQRARISLARAVYKDADLYLLDSPFGHLDIFTE 566
Cdd:cd03229 95 ENIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITR 136
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1631900066 567 KEIfESCVCKLMAN--KTRILVTSKL-EHLKIADKILILHEG 605
Cdd:cd03229 137 REV-RALLKSLQAQlgITVVLVTHDLdEAARLADRVVVLRDG 177
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
423-605 |
1.80e-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: 88.47 E-value: 1.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 423 VLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGR-----------ISFSPQVSWIMPG-TIKENII 490
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtdlppkdrdIAMVFQNYALYPHmTVYDNIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 491 FG-----VSYDEY--RYKSVIKACQLEEDISKFPEKdytvlgeggiiLSGGQRARISLARAVYKDADLYLLDSPFGHLD- 562
Cdd:cd03301 95 FGlklrkVPKDEIdeRVREVAELLQIEHLLDRKPKQ-----------LSGGQRQRVALGRAIVREPKVFLMDEPLSNLDa 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1631900066 563 ---IFTEKEIfescvCKLMAN--KTRILVT-SKLEHLKIADKILILHEG 605
Cdd:cd03301 164 klrVQMRAEL-----KRLQQRlgTTTIYVThDQVEAMTMADRIAVMNDG 207
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
422-605 |
1.87e-19 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 88.95 E-value: 1.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGR-----------------ISFSPQVSWIMPG- 483
Cdd:COG1136 22 TALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQdisslserelarlrrrhIGFVFQFFNLLPEl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 484 TIKENI-----IFGVSYDEY--RYKSVIKACQLEEDISKFPEKdytvlgeggiiLSGGQRARISLARAVYKDADLYLLDS 556
Cdd:COG1136 102 TALENValpllLAGVSRKERreRARELLERVGLGDRLDHRPSQ-----------LSGGQQQRVAIARALVNRPKLILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1631900066 557 PFGHLDIFTEKEIFEscvckLMA------NKTRILVTSKLEHLKIADKILILHEG 605
Cdd:COG1136 171 PTGNLDSKTGEEVLE-----LLRelnrelGTTIVMVTHDPELAARADRVIRLRDG 220
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1208-1442 |
2.23e-19 |
|
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: 90.30 E-value: 2.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1208 GAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFL-RLLNTEGDIQIDGvswntvsvqqwRKAFGviPQKVFIFSGTFR 1286
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILgELEPSEGKIKHSG-----------RISFS--SQFSWIMPGTIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1287 MNLdPYGQWNDEEIWK-VAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSRAKILLLDEPSAHLDPVT 1365
Cdd:cd03291 116 ENI-IFGVSYDEYRYKsVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1631900066 1366 S-QVIRKTLKHAFANCTVILSEHRLEAMLECQRFLVIEDNKLRQYESIQKLLNEKSSFRQAISHADRLKLLPVHHRNS 1442
Cdd:cd03291 195 EkEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLMGYDTFDQFSAERRNS 272
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
422-616 |
2.92e-19 |
|
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: 87.95 E-value: 2.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG------------RISFSPQVSWIMPG-TIKEN 488
Cdd:cd03263 16 PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdrkaarqSLGYCPQFDALFDElTVREH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 489 IIF-----GVSYDEYRYKS--VIKACQLEEDISKFPEKdytvlgeggiiLSGGQRARISLARAVYKDADLYLLDSPFGHL 561
Cdd:cd03263 96 LRFyarlkGLPKSEIKEEVelLLRVLGLTDKANKRART-----------LSGGMKRKLSLAIALIGGPSVLLLDEPTSGL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1631900066 562 DIFTEKEIFEsCVCKLMANKTRILVTSKLEHLKI-ADKILILHEGSCYFYGTFSEL 616
Cdd:cd03263 165 DPASRRAIWD-LILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1197-1409 |
3.41e-19 |
|
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: 87.72 E-value: 3.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKYGEggAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSvqqwRKAFGVIP 1275
Cdd:cd03269 3 VENVTKRFGR--VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILpDSGEVLFDGKPLDIAA----RNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1276 -----------QKVFIFSGTFR-MNLDPYGQWNDEEIWKVAEEVGLKSVIEQfpgqldfvlvdggcvLSHGHKQLMCLAR 1343
Cdd:cd03269 77 eerglypkmkvIDQLVYLAQLKgLKKEEARRRIDEWLERLELSEYANKRVEE---------------LSKGNQQKVQFIA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1631900066 1344 SVLSRAKILLLDEPSAHLDPVTSQVIRKTLKH-AFANCTVILSEHRLEAMLE-CQRFLVIEDNKLRQY 1409
Cdd:cd03269 142 AVIHDPELLILDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLY 209
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
398-1403 |
4.05e-19 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 94.33 E-value: 4.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 398 ENNNSKAPSTD-NNLFFSNFPLHASP-----VLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKI----KH 467
Cdd:PTZ00265 369 ENNDDGKKLKDiKKIQFKNVRFHYDTrkdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiindSH 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 468 S----------GRISFSPQVSWIMPGTIKENIIFGV-------------------SYDEYRYK----------------- 501
Cdd:PTZ00265 449 NlkdinlkwwrSKIGVVSQDPLLFSNSIKNNIKYSLyslkdlealsnyynedgndSQENKNKRnscrakcagdlndmsnt 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 502 ----------------------SVIKACQLEEDISKFPEKDYTVLGEGGIILSGGQRARISLARAVYKDADLYLLDSPFG 559
Cdd:PTZ00265 529 tdsneliemrknyqtikdsevvDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATS 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 560 HLDIFTEKeIFESCVCKLMANKTRI--LVTSKLEHLKIADKILILHegscyfygtfSELQGQRPDFssELMGFDSFDQFS 637
Cdd:PTZ00265 609 SLDNKSEY-LVQKTINNLKGNENRItiIIAHRLSTIRYANTIFVLS----------NRERGSTVDV--DIIGEDPTKDNK 675
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 638 AERRNSILTETLRRFSIEGEGMGSRNE-IKKQSfkqTSDFNDKRKSSIIINPLNaNRKFSVVQKNgmqvgvEDGHNDPPE 716
Cdd:PTZ00265 676 ENNNKNNKDDNNNNNNNNNNKINNAGSyIIEQG---THDALMKNKNGIYYTMIN-NQKVSSKKSS------NNDNDKDSD 745
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 717 RRLSLIPDLEQG-DVGLLRSNMLSTDHMLQSRRRQSVLNLMTGtssvsygpNVSKKGSTTFRKmsmvpqtnlaseiDIYT 795
Cdd:PTZ00265 746 MKSSAYKDSERGyDPDEMNGNSKHENESASNKKSCKMSDENAS--------ENNAGGKLPFLR-------------NLFK 804
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 796 RRLSRDSVLDItdeINEEDLkvce**********ttwnTYFRYVTIHKNLIFVLILCVTVFLIEVAASLAGLWFLKKtaL 875
Cdd:PTZ00265 805 RKPKAPNNLRI---VYREIF------------------SYKKDVTIIALSILVAGGLYPVFALLYAKYVSTLFDFAN--L 861
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 876 KANATQsenstsdkppvivtdtsayYIIYIYVgvadTLLAMGIFRGLPLVHTLI---TVSKTLHQKMVHAVLHAPMSTFN 952
Cdd:PTZ00265 862 EANSNK-------------------YSLYILV----IAIAMFISETLKNYYNNVigeKVEKTMKRRLFENILYQEISFFD 918
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 953 SWK-AGGMLN-RFAKDTAVLDDLLPLTVFDFVQLILIVIgaitvVSILQPYIFlasVPVIAA------FIVLRAYF---- 1020
Cdd:PTZ00265 919 QDKhAPGLLSaHINRDVHLLKTGLVNNIVIFTHFIVLFL-----VSMVMSFYF---CPIVAAvltgtyFIFMRVFAirar 990
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1021 LHTSQQLKQLESEARSPIFTH-------------LVTSLKGLWTLRAFGRQPYFETLFHKALNLhtanwflylstlrwfq 1087
Cdd:PTZ00265 991 LTANKDVEKKEINQPGTVFAYnsddeifkdpsflIQEAFYNMNTVIIYGLEDYFCNLIEKAIDY---------------- 1054
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1088 mrieiifvvffvavafisiitTGDGPGRVGIILTLAMNIMGTLQWAVNS-------------SIDVDSLMRSVgRIFKFI 1154
Cdd:PTZ00265 1055 ---------------------SNKGQKRKTLVNSMLWGFSQSAQLFINSfaywfgsflirrgTILVDDFMKSL-FTFLFT 1112
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1155 DMPTEEMKNIKPQKKN-------------QLSDALVIENRHAKEEKNWPSGGKMTVKDLTAKY-GEGGAAVLENISFSID 1220
Cdd:PTZ00265 1113 GSYAGKLMSLKGDSENaklsfekyypliiRKSNIDVRDNGGIRIKNKNDIKGKIEIMDVNFRYiSRPNVPIYKDLTFSCD 1192
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1221 SGQRVGLLGRTGSGKSTLLFAFLR-------------------------------------------------------L 1245
Cdd:PTZ00265 1193 SKKTTAIVGETGSGKSTVMSLLMRfydlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstV 1272
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1246 LNTEGDIQIDGVSWNTVSVQQWRKAFGVIPQKVFIFSGTFRMNLDpYGQWND--EEIWKVAEEVGLKSVIEQFPGQLDFV 1323
Cdd:PTZ00265 1273 FKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK-FGKEDAtrEDVKRACKFAAIDEFIESLPNKYDTN 1351
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1324 LVDGGCVLSHGHKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHA--FANCTVILSEHRLEAMLECQRFLVI 1401
Cdd:PTZ00265 1352 VGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASIKRSDKIVVF 1431
|
..
gi 1631900066 1402 ED 1403
Cdd:PTZ00265 1432 NN 1433
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
421-616 |
5.71e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 92.72 E-value: 5.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 421 SPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG-------------RISFSPQVSWIMPGTIKE 487
Cdd:PRK13657 348 RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdirtvtraslrrNIAVVFQDAGLFNRSIED 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 488 NIIFG---VSYDEYRYKSviKACQLEEDISKFPEKDYTVLGEGGIILSGGQRARISLARAVYKDADLYLLDSPFGHLDIF 564
Cdd:PRK13657 428 NIRVGrpdATDEEMRAAA--ERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVE 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1631900066 565 TEKEIFESCVCkLMANKTRILVTSKLEHLKIADKILILHEGSCYFYGTFSEL 616
Cdd:PRK13657 506 TEAKVKAALDE-LMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDEL 556
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1196-1402 |
6.00e-19 |
|
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: 87.73 E-value: 6.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1196 TVKDLTAKYGEggAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSVQQ-WRKAFGV 1273
Cdd:COG0410 5 EVENLHAGYGG--IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPpRSGSIRFDGEDITGLPPHRiARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1274 IPQKVFIFSG-TFRMNLD--PYGQWNDEEIWKVAEEVglksvIEQFP------GQLdfvlvdGGcVLSHGHKQLMCLARS 1344
Cdd:COG0410 83 VPEGRRIFPSlTVEENLLlgAYARRDRAEVRADLERV-----YELFPrlkerrRQR------AG-TLSGGEQQMLAIGRA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1345 VLSRAKILLLDEPSAHLDPVTSQVIRKTLKH-AFANCTVILSEHRLEAMLE-CQRFLVIE 1402
Cdd:COG0410 151 LMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRlNREGVTILLVEQNARFALEiADRAYVLE 210
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1198-1406 |
6.94e-19 |
|
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: 86.69 E-value: 6.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1198 KDLTAKYGEGGAAvLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRL-LNTEGDIQIDGVSWNTV---SVQQWRKAFGV 1273
Cdd:cd03292 4 INVTKTYPNGTAA-LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEeLPTSGTIRVNGQDVSDLrgrAIPYLRRKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1274 IPQKvfifsgtFRMNLD----------------PYGQWNdEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQ 1337
Cdd:cd03292 83 VFQD-------FRLLPDrnvyenvafalevtgvPPREIR-KRVPAALELVGLSHKHRALPAEL-----------SGGEQQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 1338 LMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHA-FANCTVILSEHRLEAMLECQ-RFLVIEDNKL 1406
Cdd:cd03292 144 RVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATHAKELVDTTRhRVIALERGKL 214
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
422-602 |
9.23e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 85.75 E-value: 9.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG--RISFSPQ---VSWIMPGTIKENIIFGV--- 493
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQrseVPDSLPLTVRDLVAMGRwar 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 494 -----SYDEYRYKSVIKAcqLE----EDISKFPekdytvLGEggiiLSGGQRARISLARAVYKDADLYLLDSPFGHLDIF 564
Cdd:NF040873 86 rglwrRLTRDDRAAVDDA--LErvglADLAGRQ------LGE----LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAE 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 1631900066 565 TEKEIFESCVCKLMANKTRILVTSKLEHLKIADKILIL 602
Cdd:NF040873 154 SRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
422-565 |
1.18e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 87.61 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGRISFSP--------QVSWIMPG-TIKENIIFG 492
Cdd:COG4525 21 PALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPgadrgvvfQKDALLPWlNVLDNVAFG 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1631900066 493 VsydeyRYKSVIKA---CQLEEDISKFPEKDYtvlgEGGII--LSGGQRARISLARAVYKDADLYLLDSPFGHLDIFT 565
Cdd:COG4525 101 L-----RLRGVPKAerrARAEELLALVGLADF----ARRRIwqLSGGMRQRVGIARALAADPRFLLMDEPFGALDALT 169
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1214-1409 |
1.95e-18 |
|
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: 85.42 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1214 NISFSIdSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNT------VSVQQwrKAFGVIPQKVFIFSG-TF 1285
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKpDGGTIVLNGTVLFDsrkkinLPPQQ--RKIGLVFQQYALFPHlNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1286 RMNLDpYG---QWNDEEIWKVAEEV---GLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSRAKILLLDEPSA 1359
Cdd:cd03297 93 RENLA-FGlkrKRNREDRISVDELLdllGLDHLLNRYPAQ-----------LSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1631900066 1360 HLDPVTSQVIRKTLK--HAFANCTVILSEHRL-EAMLECQRFLVIEDNKLRQY 1409
Cdd:cd03297 161 ALDRALRLQLLPELKqiKKNLNIPVIFVTHDLsEAEYLADRIVVMEDGRLQYI 213
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1197-1406 |
2.39e-18 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 86.20 E-value: 2.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKYGeGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVS---VQQWRKAFG 1272
Cdd:TIGR02315 4 VENLSKVYP-NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEpSSGSILLEGTDITKLRgkkLRKLRRRIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1273 VIPQK------------VFI----FSGTFRMNLdpyGQWNDEEIWK---VAEEVGLKSVIEQFPGQLdfvlvdggcvlSH 1333
Cdd:TIGR02315 83 MIFQHynlierltvlenVLHgrlgYKPTWRSLL---GRFSEEDKERalsALERVGLADKAYQRADQL-----------SG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1631900066 1334 GHKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFA--NCTVILSEHRLE-AMLECQRFLVIEDNKL 1406
Cdd:TIGR02315 149 GQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKedGITVIINLHQVDlAKKYADRIVGLKAGEI 224
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1211-1406 |
3.11e-18 |
|
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: 85.22 E-value: 3.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1211 VLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSVQQWRKAFGVIPQKVFIFSGTFRMNL 1289
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQpQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFARSLQDNI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1290 dPYG--QWNDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQ 1367
Cdd:cd03248 109 -AYGlqSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQ 187
|
170 180 190
....*....|....*....|....*....|....*....
gi 1631900066 1368 VIRKTLKHAFANCTVILSEHRLEAMLECQRFLVIEDNKL 1406
Cdd:cd03248 188 QVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
422-605 |
3.92e-18 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 87.85 E-value: 3.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGRisfspQVSWIMPG-----------------T 484
Cdd:COG3842 19 TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGR-----DVTGLPPEkrnvgmvfqdyalfphlT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 485 IKENIIFG-----VSYDEYRYK--SVIKACQLEEDISKFPEKdytvlgeggiiLSGGQRARISLARAVYKDADLYLLDSP 557
Cdd:COG3842 94 VAENVAFGlrmrgVPKAEIRARvaELLELVGLEGLADRYPHQ-----------LSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1631900066 558 FGHLDIFT------E-KEIFEScvcklmANKTRILVT-SKLEHLKIADKILILHEG 605
Cdd:COG3842 163 LSALDAKLreemreElRRLQRE------LGITFIYVThDQEEALALADRIAVMNDG 212
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
409-620 |
4.01e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 90.16 E-value: 4.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 409 NNLFFSNfpLHASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGR--ISFSPQV--------- 477
Cdd:PRK10790 344 DNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRplSSLSHSVlrqgvamvq 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 478 --SWIMPGTIKENIIFGVSYDEYRYKSVIKACQLEEDISKFPEKDYTVLGEGGIILSGGQRARISLARAVYKDADLYLLD 555
Cdd:PRK10790 422 qdPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILD 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1631900066 556 SPFGHLDIFTEKEIfESCVCKLMANKTRILVTSKLEHLKIADKILILHEGSCYFYGTFSELQGQR 620
Cdd:PRK10790 502 EATANIDSGTEQAI-QQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQ 565
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1196-1408 |
4.27e-18 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 87.51 E-value: 4.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1196 TVKDLTAKYGegGAAVLENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLN-----TEGDIQIDGVSWNT-VSVQQwRK 1269
Cdd:COG1118 4 EVRNISKRFG--SFTLLDDVSLEIASGELVALLGPSGSGKTTL----LRIIAgletpDSGRIVLNGRDLFTnLPPRE-RR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1270 --------------------AFG--VIPqkvfifsgtfrmnldpygqWNDEEIWKVAEE----VGLKSVIEQFPGQldfv 1323
Cdd:COG1118 77 vgfvfqhyalfphmtvaeniAFGlrVRP-------------------PSKAEIRARVEEllelVQLEGLADRYPSQ---- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1324 lvdggcvLSHGHKQLMCLARSVLSRAKILLLDEPSAHLDpvtSQViRKTLK------HAFANCTVILSEH-RLEAMLECQ 1396
Cdd:COG1118 134 -------LSGGQRQRVALARALAVEPEVLLLDEPFGALD---AKV-RKELRrwlrrlHDELGGTTVFVTHdQEEALELAD 202
|
250
....*....|..
gi 1631900066 1397 RFLVIEDNKLRQ 1408
Cdd:COG1118 203 RVVVMNQGRIEQ 214
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
419-612 |
4.56e-18 |
|
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: 84.39 E-value: 4.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 419 HASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG-------------RISFSPQVSWIMPGTI 485
Cdd:cd03369 19 DLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLTIIPQDPTLFSGTI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 486 KENIIfgvSYDEYRYKSVIKACQLEediskfpekdytvlgEGGIILSGGQRARISLARAVYKDADLYLLDSPFGHLDIFT 565
Cdd:cd03369 99 RSNLD---PFDEYSDEEIYGALRVS---------------EGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1631900066 566 EKEIFEScVCKLMANKTRILVTSKLEHLKIADKILILHEGSCYFYGT 612
Cdd:cd03369 161 DALIQKT-IREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
418-616 |
5.44e-18 |
|
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: 84.41 E-value: 5.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 418 LHA----SPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGR--------------ISFSPQVSW 479
Cdd:cd03224 6 LNAgygkSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPEGRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 480 IMPG-TIKENIIFGVSydeYRYKSVIKAcQLEEDISKFPekdytVLGE-----GGiILSGGQRARISLARAVYKDADLYL 553
Cdd:cd03224 86 IFPElTVEENLLLGAY---ARRRAKRKA-RLERVYELFP-----RLKErrkqlAG-TLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1631900066 554 LDSPfghldifTE-------KEIFEsCVCKLMANKTRILVTsklEH-----LKIADKILILHEGSCYFYGTFSEL 616
Cdd:cd03224 156 LDEP-------SEglapkivEEIFE-AIRELRDEGVTILLV---EQnarfaLEIADRAYVLERGRVVLEGTAAEL 219
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
422-617 |
6.22e-18 |
|
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: 84.65 E-value: 6.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG----------------RIS--------FSpqv 477
Cdd:COG1127 19 VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqditglsekelyelrrRIGmlfqggalFD--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 478 SwiMpgTIKENIIF------GVSYDEYRYK--SVIKACQLEEDISKFPekdytvlGEggiiLSGGQRARISLARAVYKDA 549
Cdd:COG1127 96 S--L--TVFENVAFplrehtDLSEAEIRELvlEKLELVGLPGAADKMP-------SE----LSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1631900066 550 DLYLLDSPFGHLDIFTEKEIFE---SCVCKLmaNKTRILVTskleH-----LKIADKILILHEGSCYFYGTFSELQ 617
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDElirELRDEL--GLTSVVVT----HdldsaFAIADRVAVLADGKIIAEGTPEELL 230
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
423-643 |
7.48e-18 |
|
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: 85.29 E-value: 7.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 423 VLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMgELEPSQGKIKHSG-----------RISFS--PQVSWIMPGTIKENI 489
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvswnsvplqkwRKAFGviPQKVFIFSGTFRKNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 490 -IFGVSYDEYRYKsVIKACQLEEDISKFPEKDYTVLGEGGIILSGGQRARISLARAVYKDADLYLLDSPFGHLDIFTEKe 568
Cdd:cd03289 98 dPYGKWSDEEIWK-VAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQ- 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1631900066 569 IFESCVCKLMANKTRILVTSKLEHLKIADKILILHEGSCYFYGTFSELQGQRPDFSSELMGFDSFDQFSAERRNS 643
Cdd:cd03289 176 VIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAISPSDRLKLFPRRNSSK 250
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
410-616 |
1.02e-17 |
|
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: 88.42 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 410 NLFFSnFPLHASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGeLEPSQGKIkhSGRISF-------------SPQ 476
Cdd:COG1123 9 DLSVR-YPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHGGRI--SGEVLLdgrdllelsealrGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 477 VSWIM--------PGTIKENIIF-----GVSYDEYRYK--SVIKACQLEEDISKFPEKdytvlgeggiiLSGGQRARISL 541
Cdd:COG1123 85 IGMVFqdpmtqlnPVTVGDQIAEalenlGLSRAEARARvlELLEAVGLERRLDRYPHQ-----------LSGGQRQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1631900066 542 ARAVYKDADLYLLDSPFGHLDIFTEKEIFEsCVCKLMA--NKTRILVTSKLEH-LKIADKILILHEGSCYFYGTFSEL 616
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILD-LLRELQRerGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
420-605 |
1.62e-17 |
|
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: 83.29 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 420 ASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGR-------------ISFSPQVSWIMPGTIK 486
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehkylhskVSLVGQEPVLFARSLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 487 ENIIFGVSYDEY-RYKSVIKACQLEEDISKFPEKDYTVLGEGGIILSGGQRARISLARAVYKDADLYLLDSPFGHLDIFT 565
Cdd:cd03248 106 DNIAYGLQSCSFeCVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAES 185
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1631900066 566 EKEIFESCVCKLmANKTRILVTSKLEHLKIADKILILHEG 605
Cdd:cd03248 186 EQQVQQALYDWP-ERRTVLVIAHRLSTVERADQILVLDGG 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
422-616 |
1.99e-17 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 82.98 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGR--------------ISFSPQVSWIMPG-TIK 486
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklpmhkrarlgIGYLPQEASIFRKlTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 487 ENI-----IFGVSYDEYRYKsvikacqLEEDISKFpeKDYTVLGEGGIILSGGQRARISLARAVYKDADLYLLDSPFGHL 561
Cdd:cd03218 94 ENIlavleIRGLSKKEREEK-------LEELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1631900066 562 DIFTEKEIfESCVCKLMANKTRILVTSK--LEHLKIADKILILHEGSCYFYGTFSEL 616
Cdd:cd03218 165 DPIAVQDI-QKIIKILKDRGIGVLITDHnvRETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
419-605 |
3.00e-17 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 79.80 E-value: 3.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 419 HASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGRISFS--PQvswimpgtikeniifgvsyd 496
Cdd:cd03221 11 GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGyfEQ-------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 497 eyryksvikacqleediskfpekdytvlgeggiiLSGGQRARISLARAVYKDADLYLLDSPFGHLDIFT----EKEI--F 570
Cdd:cd03221 71 ----------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESiealEEALkeY 116
|
170 180 190
....*....|....*....|....*....|....*.
gi 1631900066 571 ESCVcklmanktrILVTSKLEHL-KIADKILILHEG 605
Cdd:cd03221 117 PGTV---------ILVSHDRYFLdQVATKIIELEDG 143
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1190-1365 |
3.17e-17 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 83.22 E-value: 3.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1190 PSGGKMTVKDLTAKYGEGGAA--VLENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLL-----NTEGDIQIDGVSWNTV 1262
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGGvtALDDVSLTVAAGEFVALVGPSGCGKSTL----LRLIaglekPTSGEVLVDGKPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1263 S-----VQQ------WRK-----AFGVIPQKVfifsgtfrmnldpygqwNDEEIWKVAEE----VGLKSVIEQFPGQldf 1322
Cdd:COG1116 79 GpdrgvVFQepallpWLTvldnvALGLELRGV-----------------PKAERRERAREllelVGLAGFEDAYPHQ--- 138
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1631900066 1323 vlvdggcvLSHGHKQLMCLARSVLSRAKILLLDEPSAHLDPVT 1365
Cdd:COG1116 139 --------LSGGMRQRVAIARALANDPEVLLMDEPFGALDALT 173
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
422-615 |
3.49e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 86.66 E-value: 3.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIK--HSGRISFSPQ--------------VSWIMPGTI 485
Cdd:COG0488 329 TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKlgETVKIGYFDQhqeeldpdktvldeLRDGAPGGT 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 486 KENII-----FGVSYDeyryksvikacQLEEDISKfpekdytvlgeggiiLSGGQRARISLARAVYKDADLYLLDSPFGH 560
Cdd:COG0488 409 EQEVRgylgrFLFSGD-----------DAFKPVGV---------------LSGGEKARLALAKLLLSPPNVLLLDEPTNH 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1631900066 561 LDIFTeKEI-------FESCVcklmanktriLVTSKLEHL--KIADKILILHEGSCYFY-GTFSE 615
Cdd:COG0488 463 LDIET-LEAleealddFPGTV----------LLVSHDRYFldRVATRILEFEDGGVREYpGGYDD 516
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1197-1400 |
4.74e-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: 82.10 E-value: 4.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKYGegGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLfaflRLLN-----TEGDIQIDGVSWNTVSVQQwRKAF 1271
Cdd:cd03219 3 VRGLTKRFG--GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLF----NLISgflrpTSGSVLFDGEDITGLPPHE-IARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1272 GVIP--QKVFIFSG-TFRMNL---------DPYGQWND--------EEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvl 1331
Cdd:cd03219 76 GIGRtfQIPRLFPElTVLENVmvaaqartgSGLLLARArreerearERAEELLERVGLADLADRPAGEL----------- 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 1332 SHGHKQLMCLARSVLSRAKILLLDEPSAHLDPV-TSQVIRKTLKHAFANCTVILSEHRLEAMLE-CQRFLV 1400
Cdd:cd03219 145 SYGQQRRLEIARALATDPKLLLLDEPAAGLNPEeTEELAELIRELRERGITVLLVEHDMDVVMSlADRVTV 215
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1197-1363 |
5.33e-17 |
|
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: 81.42 E-value: 5.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKYGegGAAVLENISFSIDSGQRVGLLGRTGSGKSTllfaFLRLLN-----TEGDIQIDGvswntVSVQQWRKAF 1271
Cdd:cd03262 3 IKNLHKSFG--DFHVLKGIDLTVKKGEVVVIIGPSGSGKST----LLRCINlleepDSGTIIIDG-----LKLTDDKKNI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1272 GVIPQKV-FIFSgtfRMNLDP---------YGQ-----WNDEEIWKVAEE----VGLKSVIEQFPGQldfvlvdggcvLS 1332
Cdd:cd03262 72 NELRQKVgMVFQ---QFNLFPhltvlenitLAPikvkgMSKAEAEERALEllekVGLADKADAYPAQ-----------LS 137
|
170 180 190
....*....|....*....|....*....|.
gi 1631900066 1333 HGHKQLMCLARSVLSRAKILLLDEPSAHLDP 1363
Cdd:cd03262 138 GGQQQRVAIARALAMNPKVMLFDEPTSALDP 168
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1190-1410 |
5.85e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.89 E-value: 5.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1190 PSGGKM-TVKDLTAKYGegGAAVLENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLNteGDIQIDG--VSWN-TVSVq 1265
Cdd:COG0488 310 RLGKKVlELEGLSKSYG--DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTL----LKLLA--GELEPDSgtVKLGeTVKI- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1266 qwrkafGVIPQKvfifSGTFRMNLDPYgqwndEEIWKVAE---EVGLKSVIEQ--FPGQLDFVLVDggcVLSHGHKQLMC 1340
Cdd:COG0488 381 ------GYFDQH----QEELDPDKTVL-----DELRDGAPggtEQEVRGYLGRflFSGDDAFKPVG---VLSGGEKARLA 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1631900066 1341 LARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHaFANCTVILSEHR--LEAMleCQRFLVIEDNKLRQYE 1410
Cdd:COG0488 443 LAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDD-FPGTVLLVSHDRyfLDRV--ATRILEFEDGGVREYP 511
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
1206-1387 |
6.16e-17 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 80.54 E-value: 6.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1206 EGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDG--VSWNTVSVQQWRKAFGVIPQKV--FI 1280
Cdd:TIGR01166 2 PGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRpQSGAVLIDGepLDYSRKGLLERRQRVGLVFQDPddQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1281 FSGTFRMNLdPYGQWN----DEEIWKVAEE----VGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSRAKIL 1352
Cdd:TIGR01166 82 FAADVDQDV-AFGPLNlglsEAEVERRVREaltaVGASGLRERPTHCL-----------SGGEKKRVAIAGAVAMRPDVL 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 1631900066 1353 LLDEPSAHLDPV-TSQVIRKTLKHAFANCTVILSEH 1387
Cdd:TIGR01166 150 LLDEPTAGLDPAgREQMLAILRRLRAEGMTVVISTH 185
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
82-286 |
6.17e-17 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 83.03 E-value: 6.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 82 PLLLGRIIASYDPDNSDERSIAYYLgIGLCLLFLVRTLLIHPAIFGLHHIGMQMRIAMFSLIYKKILKLSSRVLDKISTG 161
Cdd:cd18559 17 PSNLWLLLWFDDPVNGPQEHGQVYL-SVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 162 QLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLLWDMLEASAFSGLAFLIVLAFFQAWLGQMMMKYRNKRAGKINER 241
Cdd:cd18559 96 ELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQLKRLESVSKDPR 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1631900066 242 LVITSEIIENIQSVKAYCWEDAMEKMIESIRETELKLTRKAAYVR 286
Cdd:cd18559 176 YKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLR 220
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
422-605 |
6.85e-17 |
|
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: 81.40 E-value: 6.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGRI----------SFSPQVSWIM--PG------ 483
Cdd:cd03257 19 KALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDllklsrrlrkIRRKEIQMVFqdPMsslnpr 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 484 -TIKENII------FGVSYDEYRYKSVI-KACQL---EEDISKFPEKdytvlgeggiiLSGGQRARISLARAVYKDADLY 552
Cdd:cd03257 99 mTIGEQIAeplrihGKLSKKEARKEAVLlLLVGVglpEEVLNRYPHE-----------LSGGQRQRVAIARALALNPKLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 553 LLDSPFGHLDIFTEKEIFEscvckLMA------NKTRILVTSKLE-HLKIADKILILHEG 605
Cdd:cd03257 168 IADEPTSALDVSVQAQILD-----LLKklqeelGLTLLFITHDLGvVAKIADRVAVMYAG 222
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
424-616 |
7.40e-17 |
|
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: 82.31 E-value: 7.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 424 LQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG-----------------RISFSPQVSWIMPG-TI 485
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaamsrkelrelrrkKISMVFQSFALLPHrTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 486 KENIIF-----GVSYDEYRYKS--VIKACQLEEDISKFPEKdytvlgeggiiLSGGQRARISLARAVYKDADLYLLDSPF 558
Cdd:cd03294 120 LENVAFglevqGVPRAEREERAaeALELVGLEGWEHKYPDE-----------LSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 559 GHLDIFTEKEIFESCVcKLMAN--KTRILVTSKL-EHLKIADKILILHEGSCYFYGTFSEL 616
Cdd:cd03294 189 SALDPLIRREMQDELL-RLQAElqKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1197-1419 |
7.45e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 82.35 E-value: 7.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKYGEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSVQQWRKAFGVI- 1274
Cdd:PRK13632 10 VENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKpQSGEIKIDGITISKENLKEIRKKIGIIf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1275 --PQKVFIFS--------GTFRMNLDPygqwndEEIWK----VAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMC 1340
Cdd:PRK13632 90 qnPDNQFIGAtveddiafGLENKKVPP------KKMKDiiddLAKKVGMEDYLDKEPQN-----------LSGGQKQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1341 LArSVLS-RAKILLLDEPSAHLDPVTSQVIRKTLK--HAFANCTVILSEHRLEAMLECQRFLVIEDNKLRQYESIQKLLN 1417
Cdd:PRK13632 153 IA-SVLAlNPEIIIFDESTSMLDPKGKREIKKIMVdlRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILN 231
|
..
gi 1631900066 1418 EK 1419
Cdd:PRK13632 232 NK 233
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
419-571 |
8.85e-17 |
|
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: 80.91 E-value: 8.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 419 HASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG----------------RISFSPQVSWIMP 482
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgraipylrrKIGVVFQDFRLLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 483 G-TIKENIIF-----GVSYDEY--RYKSVIKACQLEEDISKFPEKdytvlgeggiiLSGGQRARISLARAVYKDADLYLL 554
Cdd:cd03292 92 DrNVYENVAFalevtGVPPREIrkRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTILIA 160
|
170
....*....|....*..
gi 1631900066 555 DSPFGHLDIFTEKEIFE 571
Cdd:cd03292 161 DEPTGNLDPDTTWEIMN 177
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1197-1408 |
9.00e-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: 80.70 E-value: 9.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKYGEGGAavLENISFSIDSGQrVGLLGRTGSGKSTLLfaflRLLNT-----EGDIQIDGVSwNTVSVQQWRKAF 1271
Cdd:cd03264 3 LENLTKRYGKKRA--LDGVSLTLGPGM-YGLLGPNGAGKTTLM----RILATltppsSGTIRIDGQD-VLKQPQKLRRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1272 GVIPQKVFIFSG-TFRMNLDpYGQW--------NDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLA 1342
Cdd:cd03264 75 GYLPQEFGVYPNfTVREFLD-YIAWlkgipskeVKARVDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVGIA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1631900066 1343 RSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFANCTVILSEHRLEAMLE-CQRFLVIEDNKLRQ 1408
Cdd:cd03264 143 QALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVF 209
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1195-1407 |
1.11e-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: 80.49 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTAKYG--EGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLfaflRLLNT-----EGDIQIDGVSWNTvSVQQW 1267
Cdd:cd03266 2 ITADALTKRFRdvKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTL----RMLAGllepdAGFATVDGFDVVK-EPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1268 RKAFGVIPQKVFIFSG-TFRMNL----DPYGQWNDE---EIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLM 1339
Cdd:cd03266 77 RRRLGFVSDSTGLYDRlTARENLeyfaGLYGLKGDEltaRLEELADRLGMEELLDRRVGGF-----------STGMRQKV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1340 CLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKH-AFANCTVILSEHRL-EAMLECQRFLVIEDNKLR 1407
Cdd:cd03266 146 AIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQlRALGKCILFSTHIMqEVERLCDRVVVLHRGRVV 215
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1197-1405 |
1.29e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 82.02 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKYGEGG---AAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGV--SWNTVSVQQWRKA 1270
Cdd:PRK13637 5 IENLTHIYMEGTpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKpTSGKIIIDGVdiTDKKVKLSDIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1271 FGVIPQ----KVF-------IFSGTFRMNLdpygqwNDEEIWKVAEE----VGLKsvIEQFPGQLDFvlvdggcVLSHGH 1335
Cdd:PRK13637 85 VGLVFQypeyQLFeetiekdIAFGPINLGL------SEEEIENRVKRamniVGLD--YEDYKDKSPF-------ELSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1631900066 1336 KQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLK--HAFANCTVILSEHRLEAMLE-CQRFLVIEDNK 1405
Cdd:PRK13637 150 KRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKelHKEYNMTIILVSHSMEDVAKlADRIIVMNKGK 222
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1197-1400 |
1.55e-16 |
|
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: 82.41 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKY--GEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLL----NTEGDIQIDGVSWNTVSVQQWRKA 1270
Cdd:COG0444 4 VRNLKVYFptRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppgITSGEILFDGEDLLKLSEKELRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1271 ----FGVIPQkvfifsgtfrmnlDPY--------------------GQWNDEEIWKVAEE----VGL---KSVIEQFPGQ 1319
Cdd:COG0444 84 rgreIQMIFQ-------------DPMtslnpvmtvgdqiaeplrihGGLSKAEARERAIEllerVGLpdpERRLDRYPHE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1320 ldfvlvdggcvLSHGHKQLMCLARSVLSRAKILLLDEPSAHLDpVT--SQVIR--KTLKHAFaNCTVILSEHRLEAMLE- 1394
Cdd:COG0444 151 -----------LSGGMRQRVMIARALALEPKLLIADEPTTALD-VTiqAQILNllKDLQREL-GLAILFITHDLGVVAEi 217
|
....*.
gi 1631900066 1395 CQRFLV 1400
Cdd:COG0444 218 ADRVAV 223
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1198-1405 |
1.66e-16 |
|
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: 80.90 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1198 KDLTAKYGegGAAVLENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLNTE------GDIQIDGVSWNTVSVQQWRKAF 1271
Cdd:COG1119 7 RNVTVRRG--GKTILDDISWTVKPGEHWAILGPNGAGKSTL----LSLITGDlpptygNDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1272 GVI----------PQKVF--IFSGTFRMnLDPYGQWNDEEI---WKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHK 1336
Cdd:COG1119 81 GLVspalqlrfprDETVLdvVLSGFFDS-IGLYREPTDEQReraRELLELLGLAHLADRPFGT-----------LSQGEQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1631900066 1337 QLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFAN--CTVILSEHRLEAMLEC-QRFLVIEDNK 1405
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVEEIPPGiTHVLLLKDGR 220
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1208-1414 |
1.73e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 84.86 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1208 GAAVLENISFSIDSGQRVGLLGRTGSGKSTLLfaflRLLN-----TEGDIQIDgvswntvsvQQWRKAFgvIPQKVFIFS 1282
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLL----RAIAglwpyGSGRIARP---------AGARVLF--LPQRPYLPL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1283 GTFRMNL---DPYGQWNDEEIWKVAEEVGLksviEQFPGQLDFVlVDGGCVLSHGHKQLMCLARSVLSRAKILLLDEPSA 1359
Cdd:COG4178 440 GTLREALlypATAEAFSDAELREALEAVGL----GHLAERLDEE-ADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATS 514
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1631900066 1360 HLDPVTSQVIRKTLKHAFANCTVILSEHRLEAMLECQRFLVIEDNKLRQYESIQK 1414
Cdd:COG4178 515 ALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGDGSWQLLPAEA 569
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1195-1406 |
2.76e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 80.50 E-value: 2.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTAKYGEGG-------AAVLENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLL-----NTEGDIQIDGVSWNTV 1262
Cdd:PRK10419 4 LNVSGLSHHYAHGGlsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTL----ARLLvglesPSQGNVSWRGEPLAKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1263 SVQQWRkAFGVIPQKVF---------------IFSGTFR--MNLDPYGQwnDEEIWKVAEEVGLK-SVIEQFPGQldfvl 1324
Cdd:PRK10419 80 NRAQRK-AFRRDIQMVFqdsisavnprktvreIIREPLRhlLSLDKAER--LARASEMLRAVDLDdSVLDKRPPQ----- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1325 vdggcvLSHGHKQLMCLARSVLSRAKILLLDEPSAHLDPV-TSQVIR--KTLKHAFAN-CTVILSEHRLEAMLeCQRFLV 1400
Cdd:PRK10419 152 ------LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVlQAGVIRllKKLQQQFGTaCLFITHDLRLVERF-CQRVMV 224
|
....*.
gi 1631900066 1401 IEDNKL 1406
Cdd:PRK10419 225 MDNGQI 230
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
422-605 |
2.86e-16 |
|
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: 79.68 E-value: 2.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQG------------KIKHSGRISF----SPQVSWIMP--- 482
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGevrvaglvpwkrRKKFLRRIGVvfgqKTQLWWDLPvid 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 483 --GTIKEniIFGVSYDEYRyKSVIKACQLE--EDISKFPEKDytvlgeggiiLSGGQRARISLARAVYKDADLYLLDSPF 558
Cdd:cd03267 115 sfYLLAA--IYDLPPARFK-KRLDELSELLdlEELLDTPVRQ----------LSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 559 GHLDIFTEKEI--FESCVCKLmaNKTRILVTSKLEH--LKIADKILILHEG 605
Cdd:cd03267 182 IGLDVVAQENIrnFLKEYNRE--RGTTVLLTSHYMKdiEALARRVLVIDKG 230
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
423-611 |
3.03e-16 |
|
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: 79.50 E-value: 3.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 423 VLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGRIS--------FSPQVswimpgTIKENIIF--- 491
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSsllglgggFNPEL------TGRENIYLngr 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 492 --GVSYDEY--RYKSVIKACQLEEDISKfPEKDYtvlgeggiilSGGQRARISLARAVYKDADLYLLDSPFGHLDI-FTE 566
Cdd:cd03220 111 llGLSRKEIdeKIDEIIEFSELGDFIDL-PVKTY----------SSGMKARLAFAIATALEPDILLIDEVLAVGDAaFQE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1631900066 567 K--EIFEscvCKLMANKTRILVTSKLEHLK-IADKILILHEGSCYFYG 611
Cdd:cd03220 180 KcqRRLR---ELLKQGKTVILVSHDPSSIKrLCDRALVLEKGKIRFDG 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1196-1369 |
3.89e-16 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 81.66 E-value: 3.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1196 TVKDLTAKYGEGGAAV--LENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLN-----TEGDIQIDGVSWNTVSVQQWR 1268
Cdd:COG1135 3 ELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTL----IRCINllerpTSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1269 KA---FGVIPQK--------VF-------IFSGtfrmnldpygqWNDEEIWKVAEE----VGLKSVIEQFPGQldfvlvd 1326
Cdd:COG1135 79 AArrkIGMIFQHfnllssrtVAenvalplEIAG-----------VPKAEIRKRVAEllelVGLSDKADAYPSQ------- 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1631900066 1327 ggcvLSHGHKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVI 1369
Cdd:COG1135 141 ----LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSI 179
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
426-611 |
4.61e-16 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 78.49 E-value: 4.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 426 DINFRIEK--------------GQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGRISFSPQVSWIMPG-------- 483
Cdd:cd03297 1 MLCVDIEKrlpdftlkidfdlnEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPqqrkiglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 484 ----------TIKENIIFGV-----SYDEYRYKSVIKACQLEEDISKFPEKdytvlgeggiiLSGGQRARISLARAVYKD 548
Cdd:cd03297 81 fqqyalfphlNVRENLAFGLkrkrnREDRISVDELLDLLGLDHLLNRYPAQ-----------LSGGEKQRVALARALAAQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1631900066 549 ADLYLLDSPFGHLDIFTeKEIFESCVCKLMA--NKTRILVTSKLEHL-KIADKILILHEGSCYFYG 611
Cdd:cd03297 150 PELLLLDEPFSALDRAL-RLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1200-1388 |
6.09e-16 |
|
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: 77.59 E-value: 6.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1200 LTAKYGEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAF---LRLLNTEGDIQIDGVSwntVSVQQWRKAFGVIPQ 1276
Cdd:cd03213 13 VKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagrRTGLGVSGEVLINGRP---LDKRSFRKIIGYVPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1277 KvFIFSGTFRMnldpygqwnDEEIWKVAEevgLKSvieqfpgqldfvlvdggcvLSHGHKQLMCLARSVLSRAKILLLDE 1356
Cdd:cd03213 90 D-DILHPTLTV---------RETLMFAAK---LRG-------------------LSGGERKRVSIALELVSNPSLLFLDE 137
|
170 180 190
....*....|....*....|....*....|...
gi 1631900066 1357 PSAHLDPVTSQVIRKTLKH-AFANCTVILSEHR 1388
Cdd:cd03213 138 PTSGLDSSSALQVMSLLRRlADTGRTIICSIHQ 170
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
422-617 |
6.50e-16 |
|
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: 78.70 E-value: 6.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG--RISFSP--------QVSWIMPG-------T 484
Cdd:cd03261 14 TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedISGLSEaelyrlrrRMGMLFQSgalfdslT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 485 IKENIIFGVS----YDEYRYKSVIKAC----QLEEDISKFPekdytvlGEggiiLSGGQRARISLARAVYKDADLYLLDS 556
Cdd:cd03261 94 VFENVAFPLRehtrLSEEEIREIVLEKleavGLRGAEDLYP-------AE----LSGGMKKRVALARALALDPELLLYDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1631900066 557 PFGHLDIFTeKEIFESCVCKL--MANKTRILVTSKL-EHLKIADKILILHEGSCYFYGTFSELQ 617
Cdd:cd03261 163 PTAGLDPIA-SGVIDDLIRSLkkELGLTSIMVTHDLdTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
423-612 |
6.72e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 78.97 E-value: 6.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 423 VLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGRIS--------FSPQvswiMPGtiKENIIF--- 491
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSallelgagFHPE----LTG--RENIYLngr 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 492 --GVSYDEYRYKsvikacqlEEDISKF---------PEKDYtvlgeggiilSGGQRARISLARAVYKDADLYLLD----- 555
Cdd:COG1134 115 llGLSRKEIDEK--------FDEIVEFaelgdfidqPVKTY----------SSGMRARLAFAVATAVDPDILLVDevlav 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1631900066 556 --SPFGH--LDIFteKEIFEScvcklmaNKTRILVTSKLEHLK-IADKILILHEGSCYFYGT 612
Cdd:COG1134 177 gdAAFQKkcLARI--RELRES-------GRTVIFVSHSMGAVRrLCDRAIWLEKGRLVMDGD 229
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1196-1417 |
8.94e-16 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 78.26 E-value: 8.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1196 TVKDLTAKYGEggaaVLENISFSIDSGQRVGLLGRTGSGKSTLLFA---FLRLlnTEGDIQIDGVSWNTVSVQQwRKaFG 1272
Cdd:COG3840 3 RLDDLTYRYGD----FPLRFDLTIAAGERVAILGPSGAGKSTLLNLiagFLPP--DSGRILWNGQDLTALPPAE-RP-VS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1273 VIPQKVFIFSG-TFRMN----LDPYGQWNDEEIWKV---AEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARS 1344
Cdd:COG3840 75 MLFQENNLFPHlTVAQNiglgLRPGLKLTAEQRAQVeqaLERVGLAGLLDRLPGQ-----------LSGGQRQRVALARC 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1345 VLSRAKILLLDEPSAHLDPV--------TSQVIRKTlkhafaNCTVILSEHRLE-AMLECQRFLVIEDNKLRQYESIQKL 1415
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPAlrqemldlVDELCRER------GLTVLMVTHDPEdAARIADRVLLVADGRIAADGPTAAL 217
|
..
gi 1631900066 1416 LN 1417
Cdd:COG3840 218 LD 219
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
431-620 |
1.41e-15 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 78.22 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 431 IEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG-RISFSPQ-VSWIMPGTIKE---NIIFGVSYDEYRYKSVIK 505
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQyIKADYEGTVRDllsSITKDFYTHPYFKTEIAK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 506 ACQLEEDI-SKFPEkdytvlgeggiiLSGGQRARISLARAVYKDADLYLLDSPFGHLDIftEKEIFESCVCK---LMANK 581
Cdd:cd03237 102 PLQIEQILdREVPE------------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDV--EQRLMASKVIRrfaENNEK 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1631900066 582 TRILVtsklEH-----LKIADKiLILHEGSCYFYGTFSELQGQR 620
Cdd:cd03237 168 TAFVV----EHdiimiDYLADR-LIVFEGEPSVNGVANPPQSLR 206
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
422-563 |
1.54e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 81.65 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG--RISFSPQVSWIMPG-TIKENIIFGvsyDEY 498
Cdd:COG0488 12 PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLDDDlTVLDTVLDG---DAE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 499 RYKSVIKACQLEEDISkFPEKDYTVLGE--------GG---------II----------------LSGGQRARISLARAV 545
Cdd:COG0488 89 LRALEAELEELEAKLA-EPDEDLERLAElqeefealGGweaearaeeILsglgfpeedldrpvseLSGGWRRRVALARAL 167
|
170
....*....|....*...
gi 1631900066 546 YKDADLYLLDSPFGHLDI 563
Cdd:COG0488 168 LSEPDLLLLDEPTNHLDL 185
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1197-1425 |
1.77e-15 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 77.38 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKYGEggaAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLNTE-GDIQIDGVSWNTVSVQqwRKAFGVIP 1275
Cdd:cd03299 3 VENLSKDWKE---FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDsGKILLNGKDITNLPPE--KRDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1276 QKVFIFSG-TFRMNLDpYGQWN--------DEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVL 1346
Cdd:cd03299 78 QNYALFPHmTVYKNIA-YGLKKrkvdkkeiERKVLEIAEMLGIDHLLNRKPETL-----------SGGEQQRVAIARALV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1347 SRAKILLLDEPSAHLDPVTSQVIRKTLK--HAFANCTVILSEHRL-EAMLECQRFLVIEDNKLRQYESIQKLLNEKSSFR 1423
Cdd:cd03299 146 VNPKILLLDEPFSALDVRTKEKLREELKkiRKEFGVTVLHVTHDFeEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEF 225
|
..
gi 1631900066 1424 QA 1425
Cdd:cd03299 226 VA 227
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
424-615 |
2.04e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 78.55 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 424 LQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKI------------------KHSGRISFSPQVSwIMPGTI 485
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIiidgvditdkkvklsdirKKVGLVFQYPEYQ-LFEETI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 486 KENIIFGVS----YDEYRYKSVIKACQL-----EE--DISKFPekdytvlgeggiiLSGGQRARISLARAVYKDADLYLL 554
Cdd:PRK13637 102 EKDIAFGPInlglSEEEIENRVKRAMNIvgldyEDykDKSPFE-------------LSGGQKRRVAIAGVVAMEPKILIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1631900066 555 DSPFGHLDIFTEKEIFEScVCKLMA--NKTRILVTSKLEHL-KIADKILILHEGSCYFYGTFSE 615
Cdd:PRK13637 169 DEPTAGLDPKGRDEILNK-IKELHKeyNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPRE 231
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
415-605 |
2.10e-15 |
|
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: 75.16 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 415 NFPlhASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGRisfspqvswimpgtikeniifgvs 494
Cdd:cd03216 9 RFG--GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK------------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 495 ydEYRYKSVIKACQLeediskfpekdytvlgegGII----LSGGQRARISLARAVYKDADLYLLDSPFGHLDIfTEKEIF 570
Cdd:cd03216 63 --EVSFASPRDARRA------------------GIAmvyqLSVGERQMVEIARALARNARLLILDEPTAALTP-AEVERL 121
|
170 180 190
....*....|....*....|....*....|....*..
gi 1631900066 571 ESCVCKLMAN-KTRILVTSKLEH-LKIADKILILHEG 605
Cdd:cd03216 122 FKVIRRLRAQgVAVIFISHRLDEvFEIADRVTVLRDG 158
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
423-605 |
2.16e-15 |
|
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: 77.22 E-value: 2.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 423 VLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGeLEPSQGKIKHSGRISFSPQ--------VSWI-----M-------- 481
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNR-LNDLIPGAPDEGEVLLDGKdiydldvdVLELrrrvgMvfqkpnpf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 482 PGTIKENIIFGVSYDEYRYKSVIKAcQLEEDISK---FPE-KDYTVLGEggiiLSGGQRARISLARAVYKDADLYLLDSP 557
Cdd:cd03260 94 PGSIYDNVAYGLRLHGIKLKEELDE-RVEEALRKaalWDEvKDRLHALG----LSGGQQQRLCLARALANEPEVLLLDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1631900066 558 FGHLD-IFTEKeiFESCVCKLMANKTRILVTSKLEH-LKIADKILILHEG 605
Cdd:cd03260 169 TSALDpISTAK--IEELIAELKKEYTIVIVTHNMQQaARVADRTAFLLNG 216
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1190-1406 |
2.79e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 77.41 E-value: 2.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1190 PSGGKMTVKDLTAKYGEggAAVLENISFSIDSGQRVGLLGRTGSGKSTLLfaflRLL-----NTEGDIQIDGVSWNTVS- 1263
Cdd:PRK11247 8 NQGTPLLLNAVSKRYGE--RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLL----RLLagletPSAGELLAGTAPLAEARe 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1264 -----VQQWRkafgVIPQKVFIFSgtfrMNLDPYGQWNDEEIwKVAEEVGLKSVIEQFPGqldfvlvdggcVLSHGHKQL 1338
Cdd:PRK11247 82 dtrlmFQDAR----LLPWKKVIDN----VGLGLKGQWRDAAL-QALAAVGLADRANEWPA-----------ALSGGQKQR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1631900066 1339 MCLARSVLSRAKILLLDEPSAHLDPVT----SQVIRKT-LKHAFancTVILSEHRL-EAMLECQRFLVIEDNKL 1406
Cdd:PRK11247 142 VALARALIHRPGLLLLDEPLGALDALTriemQDLIESLwQQHGF---TVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
422-606 |
3.50e-15 |
|
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: 76.51 E-value: 3.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGR-ISFSP----------QVSWIMPG-TIKENI 489
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKdITNLPphkrpvntvfQNYALFPHlTVFENI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 490 IFG-----VSYDEY--RYKSVIKACQLEEDISKFPEKdytvlgeggiiLSGGQRARISLARAVYKDADLYLLDSPFGHLD 562
Cdd:cd03300 94 AFGlrlkkLPKAEIkeRVAEALDLVQLEGYANRKPSQ-----------LSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1631900066 563 IFTEKEI-FESCVCKLMANKTRILVT-SKLEHLKIADKILILHEGS 606
Cdd:cd03300 163 LKLRKDMqLELKRLQKELGITFVFVThDQEEALTMSDRIAVMNKGK 208
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
423-617 |
3.77e-15 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 76.71 E-value: 3.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 423 VLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGR--------------ISFSPQVSWIMPG-TIKE 487
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEditglppheiarlgIGRTFQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 488 NIIFGVSYDEYRYKSVIKACQLEEDIskfPEKDYTVLGEGGI---------ILSGGQRARISLARAVYKDADLYLLDSPF 558
Cdd:cd03219 95 NVMVAAQARTGSGLLLARARREEREA---RERAEELLERVGLadladrpagELSYGQQRRLEIARALATDPKLLLLDEPA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1631900066 559 GHLDIfTEKEIFESCVCKLMANKTRILVTsklEH-----LKIADKILILHEGSCYFYGTFSELQ 617
Cdd:cd03219 172 AGLNP-EETEELAELIRELRERGITVLLV---EHdmdvvMSLADRVTVLDQGRVIAEGTPDEVR 231
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1173-1402 |
4.11e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 78.33 E-value: 4.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1173 SDALVIENRHAK--EEKNWPSGGKMTVK----DLTAKYGegGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLL 1246
Cdd:PRK13536 14 LELSPIERKHQGisEAKASIPGSMSTVAidlaGVSKSYG--DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1247 N-TEGDIQIDGVSWNTvSVQQWRKAFGVIPQkvfiFSG-----TFRMNLDPYGQW---NDEEIwkvaEEVglksvieqFP 1317
Cdd:PRK13536 92 SpDAGKITVLGVPVPA-RARLARARIGVVPQ----FDNldlefTVRENLLVFGRYfgmSTREI----EAV--------IP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1318 GQLDFVLVDGGC-----VLSHGHKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFANC-TVILSEHRL-E 1390
Cdd:PRK13536 155 SLLEFARLESKAdarvsDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGkTILLTTHFMeE 234
|
250
....*....|..
gi 1631900066 1391 AMLECQRFLVIE 1402
Cdd:PRK13536 235 AERLCDRLCVLE 246
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1197-1408 |
5.35e-15 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 75.93 E-value: 5.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKYGEGGAAV--LENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLL-----NTEGDIQIDGVSWNTVSVQQwRK 1269
Cdd:COG4181 11 LRGLTKTVGTGAGELtiLKGISLEVEAGESVAIVGASGSGKSTL----LGLLagldrPTSGTVRLAGQDLFALDEDA-RA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1270 AFgvIPQKV-FIF-------SGTFRMN----LDPYGQWNDEEIWKVA-EEVGLKSVIEQFPGQldfvlvdggcvLSHGHK 1336
Cdd:COG4181 86 RL--RARHVgFVFqsfqllpTLTALENvmlpLELAGRRDARARARALlERVGLGHRLDHYPAQ-----------LSGGEQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1631900066 1337 QLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTL--KHAFANCTVILSEHRLEAMLECQRFLVIEDNKLRQ 1408
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLfeLNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
415-588 |
5.40e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 75.37 E-value: 5.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 415 NFPLHASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG------RISFSPQV------SWIMP 482
Cdd:PRK13540 8 DFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqsikkdLCTYQKQLcfvghrSGINP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 483 G-TIKENIIFGVSYDEyryksviKACQLEEDISKFPEKDYTVLGEGgiILSGGQRARISLARAVYKDADLYLLDSPFGHL 561
Cdd:PRK13540 88 YlTLRENCLYDIHFSP-------GAVGITELCRLFSLEHLIDYPCG--LLSSGQKRQVALLRLWMSKAKLWLLDEPLVAL 158
|
170 180 190
....*....|....*....|....*....|
gi 1631900066 562 DiftEKEIfESCVCKLMANKTR---ILVTS 588
Cdd:PRK13540 159 D---ELSL-LTIITKIQEHRAKggaVLLTS 184
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
423-606 |
5.53e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 78.20 E-value: 5.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 423 VLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGeLEpSQgkikHSGRISFSPQ-VSWI-------------------Mp 482
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAG-LE-HQ----TSGHIRFHGTdVSRLhardrkvgfvfqhyalfrhM- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 483 gTIKENIIFGV---------SYDEYRYK--SVIKACQLEEDISKFPEKdytvlgeggiiLSGGQRARISLARAVYKDADL 551
Cdd:PRK10851 90 -TVFDNIAFGLtvlprrerpNAAAIKAKvtQLLEMVQLAHLADRYPAQ-----------LSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1631900066 552 YLLDSPFGHLDIFTEKEIfESCVCKLMANK--TRILVT-SKLEHLKIADKILILHEGS 606
Cdd:PRK10851 158 LLLDEPFGALDAQVRKEL-RRWLRQLHEELkfTSVFVThDQEEAMEVADRVVVMSQGN 214
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
423-611 |
5.65e-15 |
|
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: 75.39 E-value: 5.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 423 VLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG---------RISFSPQVSWIMPG-TIKENIIF- 491
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpldiaarnRIGYLPEERGLYPKmKVIDQLVYl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 492 ----GVSYDEYRYksvikacQLEEDISKF--PEKDYTVLGEggiiLSGGQRARISLARAVYKDADLYLLDSPFGHLDIfT 565
Cdd:cd03269 95 aqlkGLKKEEARR-------RIDEWLERLelSEYANKRVEE----LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-V 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1631900066 566 EKEIFESCVCKLMAN-KTRILVTSKLEHL-KIADKILILHEGSCYFYG 611
Cdd:cd03269 163 NVELLKDVIRELARAgKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
424-639 |
5.69e-15 |
|
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: 75.97 E-value: 5.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 424 LQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGRISFSP--------QVSWIMPG-TIKENIIFGV- 493
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgpdrmvvfQNYSLLPWlTVRENIALAVd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 494 ------SYDEYR--YKSVIKACQLEEDISKFPEKdytvlgeggiiLSGGQRARISLARAVYKDADLYLLDSPFGHLDIFT 565
Cdd:TIGR01184 81 rvlpdlSKSERRaiVEEHIALVGLTEAADKRPGQ-----------LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 566 EKEIFEscvcKLM-----ANKTRILVTSKL-EHLKIADKILILHEGSCYFYGTFSELQGQRPDFSSELMGFDSFDQFSAE 639
Cdd:TIGR01184 150 RGNLQE----ELMqiweeHRVTVLMVTHDVdEALLLSDRVVMLTNGPAANIGQILEVPFPRPRDRLEVVEDPSYYDLRNE 225
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1196-1406 |
5.83e-15 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 77.92 E-value: 5.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1196 TVKDLTAKYGEGGAAV--LENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLN-----TEGDIQIDGVSWNTVSVQQWR 1268
Cdd:PRK11153 3 ELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTL----IRCINllerpTSGRVLVDGQDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1269 KA---FGVIPQKVFIFSG-------TFRMNLDpygQWNDEEIWKVAEE----VGLKSVIEQFPGQldfvlvdggcvLSHG 1334
Cdd:PRK11153 79 KArrqIGMIFQHFNLLSSrtvfdnvALPLELA---GTPKAEIKARVTEllelVGLSDKADRYPAQ-----------LSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1631900066 1335 HKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLK--HAFANCTVILSEHRLEAMLE-CQRFLVIEDNKL 1406
Cdd:PRK11153 145 QKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKdiNRELGLTIVLITHEMDVVKRiCDRVAVIDAGRL 219
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1197-1406 |
5.95e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 76.98 E-value: 5.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKYGEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLN-----TEGDIQIDGVSWNTVSVQQWRKAF 1271
Cdd:PRK13635 8 VEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTL----AKLLNglllpEAGTITVGGMVLSEETVWDVRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1272 GVI---PQKVFIFSgTFR----MNLDPYGQWNDEEIWKVAE---EVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCL 1341
Cdd:PRK13635 84 GMVfqnPDNQFVGA-TVQddvaFGLENIGVPREEMVERVDQalrQVGMEDFLNREPHR-----------LSGGQKQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1631900066 1342 ARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKH--AFANCTVILSEHRLEAMLECQRFLVIEDNKL 1406
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEI 218
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1211-1387 |
6.20e-15 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 75.77 E-value: 6.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1211 VLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLL----NTEGDIQIDGVSwntVSVQQWRKAFGVIPQKVFI------ 1280
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVegggTTSGQILFNGQP---RKPDQFQKCVAYVRQDDILlpgltv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1281 -----FSGTFRMnldPYGQwNDEEIWKVAEEVGLKSVIEQfpgQLDFVLVDGgcvLSHGHKQLMCLARSVLSRAKILLLD 1355
Cdd:cd03234 99 retltYTAILRL---PRKS-SDAIRKKRVEDVLLRDLALT---RIGGNLVKG---ISGGERRRVSIAVQLLWDPKVLILD 168
|
170 180 190
....*....|....*....|....*....|...
gi 1631900066 1356 EPSAHLDPVTSQVIRKTLKH-AFANCTVILSEH 1387
Cdd:cd03234 169 EPTSGLDSFTALNLVSTLSQlARRNRIVILTIH 201
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1196-1392 |
6.96e-15 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 77.83 E-value: 6.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1196 TVKDLTAKYGegGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFA---FLRLlnTEGDIQIDGVSWNTVSVQQwRKaFG 1272
Cdd:COG3842 7 ELENVSKRYG--DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMiagFETP--DSGRILLDGRDVTGLPPEK-RN-VG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1273 VIPQKVFIFsgtfrmnldP---------YG----QWNDEEIWKVAEE----VGLKSVIEQFPGQldfvlvdggcvLSHGH 1335
Cdd:COG3842 81 MVFQDYALF---------PhltvaenvaFGlrmrGVPKAEIRARVAEllelVGLEGLADRYPHQ-----------LSGGQ 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1336 KQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFA--NCTVILSEH-RLEAM 1392
Cdd:COG3842 141 QQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRelGITFIYVTHdQEEAL 200
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1195-1390 |
9.33e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 75.97 E-value: 9.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTAKYGEGGAavLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRL--LNTE----GDIQIDG---VSWNTVSVQ 1265
Cdd:PRK14239 6 LQVSDLSVYYNKKKA--LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtitGSIVYNGhniYSPRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1266 qWRKAFGVIPQKVFIFSGTFRMNLdPYG----QWNDEEIWKVAEEVGLK--SVIEQFPGQLDfvlvDGGCVLSHGHKQLM 1339
Cdd:PRK14239 84 -LRKEIGMVFQQPNPFPMSIYENV-VYGlrlkGIKDKQVLDEAVEKSLKgaSIWDEVKDRLH----DSALGLSGGQQQRV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 1340 CLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFANCTVILSEHRLE 1390
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQ 208
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
423-611 |
1.33e-14 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 74.71 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 423 VLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG------------RISFSPQVSWIMPG-TIKENI 489
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkepaearrRLGFVSDSTGLYDRlTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 490 IF-----GVSYDEyryksvIKAcQLEEDISKFPEKDYTVLGEGGiiLSGGQRARISLARAVYKDADLYLLDSPFGHLDIF 564
Cdd:cd03266 100 EYfaglyGLKGDE------LTA-RLEELADRLGMEELLDRRVGG--FSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVM 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1631900066 565 TEKEIFEScVCKLMANKTRILVTSKL--EHLKIADKILILHEGSCYFYG 611
Cdd:cd03266 171 ATRALREF-IRQLRALGKCILFSTHImqEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
418-605 |
1.33e-14 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 73.62 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 418 LHASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGRIsfspqvswIMPGTIKENIIFGVSYde 497
Cdd:cd03215 10 LSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKP--------VTRRSPRDAIRAGIAY-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 498 yryksvikacqLEED------ISKFPEKDYTVLGeggIILSGGQRARISLARAVYKDADLYLLDSPFGHLDIFTEKEIFE 571
Cdd:cd03215 80 -----------VPEDrkreglVLDLSVAENIALS---SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYR 145
|
170 180 190
....*....|....*....|....*....|....*
gi 1631900066 572 SCVCKLMANKTRILVTSKL-EHLKIADKILILHEG 605
Cdd:cd03215 146 LIRELADAGKAVLLISSELdELLGLCDRILVMYEG 180
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
422-645 |
1.49e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 77.18 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGR-ISFSP----------QVSWIMPG-TIKENI 489
Cdd:PRK11607 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdLSHVPpyqrpinmmfQSYALFPHmTVEQNI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 490 IFGVSYDEY-------RYKSVIKACQLEEDISKFPEKdytvlgeggiiLSGGQRARISLARAVYKDADLYLLDSPFGHLD 562
Cdd:PRK11607 113 AFGLKQDKLpkaeiasRVNEMLGLVHMQEFAKRKPHQ-----------LSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 563 ifteKEIFESCVCKLMANKTRILVTSKL------EHLKIADKILILHEGSCYFYGTFSELQgQRPD--FSSELMG-FDSF 633
Cdd:PRK11607 182 ----KKLRDRMQLEVVDILERVGVTCVMvthdqeEAMTMAGRIAIMNRGKFVQIGEPEEIY-EHPTtrYSAEFIGsVNVF 256
|
250
....*....|..
gi 1631900066 634 DQFSAERRNSIL 645
Cdd:PRK11607 257 EGVLKERQEDGL 268
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
431-563 |
1.67e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 78.31 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 431 IEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGRISFSPQ-VSWIMPGTIKENI-----IFGVSYdeyrYKS-V 503
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQyIKPDYDGTVEDLLrsitdDLGSSY----YKSeI 437
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 504 IKACQLEeDISKFPEKDytvlgeggiiLSGGQRARISLARAVYKDADLYLLDSPFGHLDI 563
Cdd:PRK13409 438 IKPLQLE-RLLDKNVKD----------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 486
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1216-1421 |
1.89e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 74.23 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1216 SFSIDSGQRVGLLGRTGSGKSTLL-----FaflrLLNTEGDIQIDGVSWNTVSVQQwrKAFGVIPQKVFIFSG-TFRMN- 1288
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLnliagF----LTPASGSLTLNGQDHTTTPPSR--RPVSMLFQENNLFSHlTVAQNi 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1289 ---LDPYGQWNDEE---IWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSRAKILLLDEPSAHLD 1362
Cdd:PRK10771 93 glgLNPGLKLNAAQrekLHAIARQMGIEDLLARLPGQL-----------SGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1631900066 1363 PVTSQVIRKTLKHAFA--NCTVILSEHRLE-AMLECQRFLVIEDNKLRQYESIQKLLNEKSS 1421
Cdd:PRK10771 162 PALRQEMLTLVSQVCQerQLTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLSGKAS 223
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1198-1363 |
1.91e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 74.74 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1198 KDLTAKYGEggAAVLENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLN-----TEGDIQIDGVSWN--TVSVQQWRKA 1270
Cdd:PRK09493 5 KNVSKHFGP--TQVLHNIDLNIDQGEVVVIIGPSGSGKSTL----LRCINkleeiTSGDLIVDGLKVNdpKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1271 FGVIPQKVFIFS----------GTFRMNldpyGQwNDEEIWKVAEE----VGLKSVIEQFPGQldfvlvdggcvLSHGHK 1336
Cdd:PRK09493 79 AGMVFQQFYLFPhltalenvmfGPLRVR----GA-SKEEAEKQAREllakVGLAERAHHYPSE-----------LSGGQQ 142
|
170 180
....*....|....*....|....*..
gi 1631900066 1337 QLMCLARSVLSRAKILLLDEPSAHLDP 1363
Cdd:PRK09493 143 QRVAIARALAVKPKLMLFDEPTSALDP 169
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
415-622 |
1.97e-14 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 74.41 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 415 NFPLHASpvlqdinFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGR-ISFSPqvswimPG---------- 483
Cdd:COG3840 13 DFPLRFD-------LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdLTALP------PAerpvsmlfqe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 484 -------TIKENIIFGVS----YDEYRYKSVIKACQ---LEEDISKFPEkdytvlgeggiILSGGQRARISLARAVYKDA 549
Cdd:COG3840 80 nnlfphlTVAQNIGLGLRpglkLTAEQRAQVEQALErvgLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1631900066 550 DLYLLDSPFGHLDIFTEKEIFEsCVCKLMANK--TRILVTSKLEH-LKIADKILILHEGSCYFYGTFSELQGQRPD 622
Cdd:COG3840 149 PILLLDEPFSALDPALRQEMLD-LVDELCRERglTVLMVTHDPEDaARIADRVLLVADGRIAADGPTAALLDGEPP 223
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1194-1369 |
2.00e-14 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 75.07 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1194 KMTVKDLTAKYGEggAAVLENISFSIDSGQRVGLLGRTGSGKSTllfaFLRLLN----------TEGDIQIDG--VSWNT 1261
Cdd:COG1117 11 KIEVRNLNVYYGD--KQALKDINLDIPENKVTALIGPSGCGKST----LLRCLNrmndlipgarVEGEILLDGedIYDPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1262 VSVQQWRKAFGVIPQKVFIFSGT--------FRMNldpyGQWNDEEIWKVAEEVgLKSVieqfpGQLDFV---LVDGGCV 1330
Cdd:COG1117 85 VDVVELRRRVGMVFQKPNPFPKSiydnvaygLRLH----GIKSKSELDEIVEES-LRKA-----ALWDEVkdrLKKSALG 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 1631900066 1331 LSHGHKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVI 1369
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKI 193
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1197-1406 |
2.23e-14 |
|
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: 72.46 E-value: 2.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKYGegGAAVLENISFSIDSGQRVGLLGRTGSGKSTL---LFAFLRLlnTEGDIQIDGVSWNTVSVQQ-WRKAFG 1272
Cdd:cd03216 3 LRGITKRFG--GVKALDGVSLSVRRGEVHALLGENGAGKSTLmkiLSGLYKP--DSGEILVDGKEVSFASPRDaRRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1273 VIPQkvfifsgtfrmnldpygqwndeeiwkvaeevglksvieqfpgqldfvlvdggcvLSHGHKQLMCLARSVLSRAKIL 1352
Cdd:cd03216 79 MVYQ------------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1631900066 1353 LLDEPSAHLDPVTSQ----VIRKTLKhafANCTVILSEHRLEAMLE-CQRFLVIEDNKL 1406
Cdd:cd03216 105 ILDEPTAALTPAEVErlfkVIRRLRA---QGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1197-1419 |
2.39e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 75.16 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKYGEGGAAvLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRL-LNTEGDIQIDGVSWNTVSVQQWRKAFGVIP 1275
Cdd:PRK13647 7 VEDLHFRYKDGTKA-LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIyLPQRGRVKVMGREVNAENEKWVRSKVGLVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1276 QKV--FIFSGTF---------RMNLDPygqwndEEIWKVAEE----VGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMC 1340
Cdd:PRK13647 86 QDPddQVFSSTVwddvafgpvNMGLDK------DEVERRVEEalkaVRMWDFRDKPPYH-----------LSYGQKKRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1341 LARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFAN-CTVILSEHRLEAMLE-CQRFLVIEDNKLRQYESIQKLLNE 1418
Cdd:PRK13647 149 IAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQgKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDE 228
|
.
gi 1631900066 1419 K 1419
Cdd:PRK13647 229 D 229
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1212-1432 |
2.47e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 78.86 E-value: 2.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1212 LENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLNTEGDIQIDgvswntvsvqqWRKAFGVIPQKVFIFSGTFRMNLDP 1291
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV-----------IRGSVAYVPQVSWIFNATVRENILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1292 YGQWNDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSRAKILLLDEPSAHLDP-VTSQVIR 1370
Cdd:PLN03232 702 GSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAhVAHQVFD 781
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1631900066 1371 KTLKHAFANCTVILSEHRLEAMLECQRFLVIEDNKLRQYESIQKLLNEKSSFRQAISHADRL 1432
Cdd:PLN03232 782 SCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAGKM 843
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1197-1408 |
2.68e-14 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 74.30 E-value: 2.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKYGegGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLfaflRLLN-----TEGDIQIDGVSWNTVSVQQwrKAF 1271
Cdd:cd03296 5 VRNVSKRFG--DFVALDDVSLDIPSGELVALLGPSGSGKTTLL----RLIAglerpDSGTILFGGEDATDVPVQE--RNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1272 GVIPQKVFIFSG-------TFRMNLDPYGQWNDE-EIWKVAEE----VGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLM 1339
Cdd:cd03296 77 GFVFQHYALFRHmtvfdnvAFGLRVKPRSERPPEaEIRAKVHEllklVQLDWLADRYPAQL-----------SGGQRQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1631900066 1340 CLARSVLSRAKILLLDEPSAHLDpvtSQViRKTLK------HAFANCTVILSEHRLEAMLE-CQRFLVIEDNKLRQ 1408
Cdd:cd03296 146 ALARALAVEPKVLLLDEPFGALD---AKV-RKELRrwlrrlHDELHVTTVFVTHDQEEALEvADRVVVMNKGRIEQ 217
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
420-616 |
2.71e-14 |
|
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: 73.86 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 420 ASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGR--------------ISFSPQVSWIMPG-T 484
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEditglpphriarlgIGYVPEGRRIFPSlT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 485 IKENIIFGVsydeY--RYKSVIKAcQLEEDISKFPekdytVLGE-----GGiILSGGQRARISLARAVYKDADLYLLDSP 557
Cdd:COG0410 95 VEENLLLGA----YarRDRAEVRA-DLERVYELFP-----RLKErrrqrAG-TLSGGEQQMLAIGRALMSRPKLLLLDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 558 fghldifTE-------KEIFEsCVCKLMANKTRILVTsklEH-----LKIADKILILHEGSCYFYGTFSEL 616
Cdd:COG0410 164 -------SLglaplivEEIFE-IIRRLNREGVTILLV---EQnarfaLEIADRAYVLERGRIVLEGTAAEL 223
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1196-1405 |
2.74e-14 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 71.33 E-value: 2.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1196 TVKDLTAKYGEGgaAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFL-RLLNTEGDIQIDGvswntvsvqqwRKAFGVI 1274
Cdd:cd03221 2 ELENLSKTYGGK--LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAgELEPDEGIVTWGS-----------TVKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1275 PQkvfiFSGtfrmnldpyGQWNdeeiwKVAeevglksvieqfpgqldfvlvdggcvlshghkqlmcLARSVLSRAKILLL 1354
Cdd:cd03221 69 EQ----LSG---------GEKM-----RLA------------------------------------LAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1631900066 1355 DEPSAHLDPVTSQVIRKTLKhAFaNCTVILSEH-RleAMLE--CQRFLVIEDNK 1405
Cdd:cd03221 95 DEPTNHLDLESIEALEEALK-EY-PGTVILVSHdR--YFLDqvATKIIELEDGK 144
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
413-625 |
3.16e-14 |
|
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: 78.45 E-value: 3.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 413 FSNFPLHASP----VLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG-------------RISFSP 475
Cdd:TIGR00957 1287 FRNYCLRYREdldlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGlniakiglhdlrfKITIIP 1366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 476 QVSWIMPGTIKENIIFGVSYDEYRYKSVIKACQLEEDISKFPEKDYTVLGEGGIILSGGQRARISLARAVYKDADLYLLD 555
Cdd:TIGR00957 1367 QDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLD 1446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1631900066 556 SPFGHLDIFTEKEI-------FESCvcklmankTRILVTSKLEHLKIADKILILHEGSCYFYGTFSELQGQRPDFSS 625
Cdd:TIGR00957 1447 EATAAVDLETDNLIqstirtqFEDC--------TVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYS 1515
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1210-1368 |
3.49e-14 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 77.03 E-value: 3.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1210 AVlENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLNTEGDIQIDGVSWNTVS---VQQWRKAFGVIPQkvfifsgtfr 1286
Cdd:COG4172 301 AV-DGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQ---------- 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1287 mnlDPYGQWN-------------------------DEEIWKVAEEVGLK-SVIEQFPGQldfvlvdggcvLSHGHKQLMC 1340
Cdd:COG4172 370 ---DPFGSLSprmtvgqiiaeglrvhgpglsaaerRARVAEALEEVGLDpAARHRYPHE-----------FSGGQRQRIA 435
|
170 180
....*....|....*....|....*....
gi 1631900066 1341 LARSVLSRAKILLLDEP-SAhLDpVTSQV 1368
Cdd:COG4172 436 IARALILEPKLLVLDEPtSA-LD-VSVQA 462
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1195-1375 |
5.54e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 73.37 E-value: 5.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTAKYGEggAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFL-RLLNTEGDIQIDG---VSWNTVSVQqwRKA 1270
Cdd:PRK11614 6 LSFDKVSAHYGK--IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCgDPRATSGRIVFDGkdiTDWQTAKIM--REA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1271 FGVIPQKVFIFSG-TFRMNLDPYGQWNDEEIWKVAeevgLKSVIEQFPGQLDFVLVDGGcVLSHGHKQLMCLARSVLSRA 1349
Cdd:PRK11614 82 VAIVPEGRRVFSRmTVEENLAMGGFFAERDQFQER----IKWVYELFPRLHERRIQRAG-TMSGGEQQMLAIGRALMSQP 156
|
170 180
....*....|....*....|....*.
gi 1631900066 1350 KILLLDEPSAHLDPVTSQVIRKTLKH 1375
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQ 182
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1195-1432 |
6.59e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 73.00 E-value: 6.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTAKYGegGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLL-NTEGDIQIDGVSWNTVSV-QQWRKAFG 1272
Cdd:PRK10895 4 LTAKNLAKAYK--GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVpRDAGNIIIDDEDISLLPLhARARRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1273 VIPQKVFIFSGTFRMN-----LDPYGQWNDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdgGCVLSHGHKQLMCLARSVLS 1347
Cdd:PRK10895 82 YLPQEASIFRRLSVYDnlmavLQIRDDLSAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIARALAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1348 RAKILLLDEPSAHLDPVTSQVIRKTLKHAF-ANCTVILSEHRLEAMLE-CQRFLVIEDNKLRQYESIQKLLNEKSSFRQA 1425
Cdd:PRK10895 155 NPKFILLDEPFAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEILQDEHVKRVY 234
|
....*..
gi 1631900066 1426 ISHADRL 1432
Cdd:PRK10895 235 LGEDFRL 241
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
424-605 |
8.32e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 73.71 E-value: 8.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 424 LQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGRiSFSPQVS--------------------WIMPG 483
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGY-HITPETGnknlkklrkkvslvfqfpeaQLFEN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 484 TIKENII-----FGVSYDEYRYKSV--IKACQLEED-ISKFPEKdytvlgeggiiLSGGQRARISLARAVYKDADLYLLD 555
Cdd:PRK13641 102 TVLKDVEfgpknFGFSEDEAKEKALkwLKKVGLSEDlISKSPFE-----------LSGGQMRRVAIAGVMAYEPEILCLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 556 SPFGHLDIFTEKEIFESCVCKLMANKTRILVTSKLEHL-KIADKILILHEG 605
Cdd:PRK13641 171 EPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHG 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1196-1375 |
9.03e-14 |
|
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: 72.58 E-value: 9.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1196 TVKDLTAKYGegGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSV-QQWRKAFGV 1273
Cdd:cd03218 2 RAENLSKRYG--KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKpDSGKILLDGQDITKLPMhKRARLGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1274 IPQKVFIFSG-TFRMNL--------DPYGQWNDEeiwkvaeevgLKSVIEQFpgQLDFVLVDGGCVLSHGHKQLMCLARS 1344
Cdd:cd03218 80 LPQEASIFRKlTVEENIlavleirgLSKKEREEK----------LEELLEEF--HITHLRKSKASSLSGGERRRVEIARA 147
|
170 180 190
....*....|....*....|....*....|.
gi 1631900066 1345 VLSRAKILLLDEPSAHLDPVTSQVIRKTLKH 1375
Cdd:cd03218 148 LATNPKFLLLDEPFAGVDPIAVQDIQKIIKI 178
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
422-617 |
9.31e-14 |
|
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: 72.60 E-value: 9.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG----------------RISF-SPQVSWIMPGT 484
Cdd:cd03256 15 KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdinklkgkalrqlrrQIGMiFQQFNLIERLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 485 IKENIIFGvsydeyR--YKSVIKACqleedISKFPEKDYTV----LGEGGII---------LSGGQRARISLARAVYKDA 549
Cdd:cd03256 95 VLENVLSG------RlgRRSTWRSL-----FGLFPKEEKQRalaaLERVGLLdkayqradqLSGGQQQRVAIARALMQQP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1631900066 550 DLYLLDSPFGHLDIFTEKEIFEscVCKLMANKTRILVTSKLEHL----KIADKILILHEGSCYFYGTFSELQ 617
Cdd:cd03256 164 KLILADEPVASLDPASSRQVMD--LLKRINREEGITVIVSLHQVdlarEYADRIVGLKDGRIVFDGPPAELT 233
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1205-1389 |
1.01e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 73.21 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1205 GEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTllfaFLRLLNT----------EGDIQIDGVS-WNTVSVQQWRKAFGV 1273
Cdd:PRK14271 30 GFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTT----FLRTLNRmndkvsgyrySGDVLLGGRSiFNYRDVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1274 IPQKVFIFSGTFRMNL----DPYGQWNDEEIWKVAE----EVGLKSVIEQfpgqldfVLVDGGCVLSHGHKQLMCLARSV 1345
Cdd:PRK14271 106 LFQRPNPFPMSIMDNVlagvRAHKLVPRKEFRGVAQarltEVGLWDAVKD-------RLSDSPFRLSGGQQQLLCLARTL 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1631900066 1346 LSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFANCTVILSEHRL 1389
Cdd:PRK14271 179 AVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNL 222
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1194-1362 |
2.16e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 71.97 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1194 KMTVKDLTAKYGEggAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLNTE-GDIQIDGVSWNTVSVQQWRKAFG 1272
Cdd:PRK11231 2 TLRTENLTVGYGT--KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQsGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1273 VIPQKVFIFSGTFRMNLDPYGQ------W-----NDEEIWKVAEEvglKSVIEQFPGQLdfvLVDggcvLSHGHKQLMCL 1341
Cdd:PRK11231 80 LLPQHHLTPEGITVRELVAYGRspwlslWgrlsaEDNARVNQAME---QTRINHLADRR---LTD----LSGGQRQRAFL 149
|
170 180
....*....|....*....|.
gi 1631900066 1342 ARSVLSRAKILLLDEPSAHLD 1362
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLD 170
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
423-611 |
2.21e-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: 71.15 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 423 VLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEpsQGKIKhSGRI----------------SFSPQVSWIMPG-TI 485
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVE--GGGTT-SGQIlfngqprkpdqfqkcvAYVRQDDILLPGlTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 486 KENIIFGV-------SYDEYRYKSVikACQLEEDISKFPEKDYTVLGeggiiLSGGQRARISLARAVYKDADLYLLDSPF 558
Cdd:cd03234 99 RETLTYTAilrlprkSSDAIRKKRV--EDVLLRDLALTRIGGNLVKG-----ISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1631900066 559 GHLDIFTEKEIFEscVCKLMANKTRILVTS----KLEHLKIADKILILHEGSCYFYG 611
Cdd:cd03234 172 SGLDSFTALNLVS--TLSQLARRNRIVILTihqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
431-563 |
2.31e-13 |
|
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: 74.82 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 431 IEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGRISFSPQ-VSWIMPGTIKENI------IFGVSYdeyrYKS- 502
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQyISPDYDGTVEEFLrsantdDFGSSY----YKTe 438
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 503 VIKACQLEedisKFPEKDytvLGEggiiLSGGQRARISLARAVYKDADLYLLDSPFGHLDI 563
Cdd:COG1245 439 IIKPLGLE----KLLDKN---VKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1158-1392 |
3.79e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 74.68 E-value: 3.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1158 TEEMKNIkpQKKNQLSDAL----VIENRhaKEEKNWPSGGKMTVKDLTAKYG-EGGAAVLENISFSIDSGQRVGLLGRTG 1232
Cdd:PTZ00265 346 TEYMKSL--EATNSLYEIInrkpLVENN--DDGKKLKDIKKIQFKNVRFHYDtRKDVEIYKDLNFTLTEGKTYAFVGESG 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1233 SGKSTLLFAFLRLLN-TEGDIQI-DGVSWNTVSVQQWRKAFGVIPQKVFIFSGTFRMNL--------------------- 1289
Cdd:PTZ00265 422 CGKSTILKLIERLYDpTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIkyslyslkdlealsnyynedg 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1290 -------------------------------------DPYGQWNDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLS 1332
Cdd:PTZ00265 502 ndsqenknkrnscrakcagdlndmsnttdsneliemrKNYQTIKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLS 581
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1631900066 1333 HGHKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFAN---CTVILSeHRLEAM 1392
Cdd:PTZ00265 582 GGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNenrITIIIA-HRLSTI 643
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
418-562 |
5.03e-13 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 69.82 E-value: 5.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 418 LHASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEP---SQGKIK-----------HSGRISFSPQVSWIMPG 483
Cdd:COG4136 11 LGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLlngrrltalpaEQRRIGILFQDDLLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 484 -TIKENIIFGVSYD---EYRYKSVIKAcqLEE-DISKFPEKDYTVLgeggiilSGGQRARISLARAVYKDADLYLLDSPF 558
Cdd:COG4136 91 lSVGENLAFALPPTigrAQRRARVEQA--LEEaGLAGFADRDPATL-------SGGQRARVALLRALLAEPRALLLDEPF 161
|
....
gi 1631900066 559 GHLD 562
Cdd:COG4136 162 SKLD 165
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1196-1401 |
5.16e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 71.29 E-value: 5.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1196 TVKDLTAKYGEggAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGvswNTVSVQQwRKAFGVI 1274
Cdd:COG4152 3 ELKGLTKRFGD--KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILApDSGEVLWDG---EPLDPED-RRRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1275 PqkvfifsgtfrmnldpygqwndeeiwkvaEEVGL---KSVIEQ--FPGQL------------DFVL------------V 1325
Cdd:COG4152 77 P-----------------------------EERGLypkMKVGEQlvYLARLkglskaeakrraDEWLerlglgdrankkV 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1631900066 1326 DGgcvLSHGHKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLK-HAFANCTVILSEHRLEAMLE-CQRFLVI 1401
Cdd:COG4152 128 EE---LSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIReLAAKGTTVIFSSHQMELVEElCDRIVII 202
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
413-612 |
5.56e-13 |
|
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: 73.40 E-value: 5.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 413 FSNFPLHASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKI----------KHSGRISFSPQVSWIM- 481
Cdd:COG1123 270 YPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIlfdgkdltklSRRSLRELRRRVQMVFq 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 482 -PG-------TIKENI-----IFGVSYDEYRYKSV---IKACQLEED-ISKFPekdytvlGEggiiLSGGQRARISLARA 544
Cdd:COG1123 350 dPYsslnprmTVGDIIaeplrLHGLLSRAERRERVaelLERVGLPPDlADRYP-------HE----LSGGQRQRVAIARA 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1631900066 545 VYKDADLYLLDSPFGHLDIFTEKEIFEscvckLMA------NKTRILVTskleH-----LKIADKILILHEGSCYFYGT 612
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILN-----LLRdlqrelGLTYLFIS----HdlavvRYIADRVAVMYDGRIVEDGP 488
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
423-605 |
6.20e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 70.48 E-value: 6.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 423 VLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQG----------KIKHSGRISFspQVSWIMP-GTIKENIIF 491
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGellagtaplaEAREDTRLMF--QDARLLPwKKVIDNVGL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 492 GVSYDeYRYKS--VIKACQLEEDISKFPEKdytvlgeggiiLSGGQRARISLARAVYKDADLYLLDSPFGHLDIFTEKEI 569
Cdd:PRK11247 105 GLKGQ-WRDAAlqALAAVGLADRANEWPAA-----------LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEM 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 1631900066 570 fESCVCKLMANK--TRILVTSKL-EHLKIADKILILHEG 605
Cdd:PRK11247 173 -QDLIESLWQQHgfTVLLVTHDVsEAVAMADRVLLIEEG 210
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
1197-1389 |
6.24e-13 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 69.74 E-value: 6.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKYGEggAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNtvsvqqwRKAFGVIp 1275
Cdd:TIGR03740 3 TKNLSKRFGK--QTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRpTSGEIIFDGHPWT-------RKDLHKI- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1276 qKVFIFSGTFRMNLDPYGQWN---------DEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVL 1346
Cdd:TIGR03740 73 -GSLIESPPLYENLTARENLKvhttllglpDSRIDEVLNIVDLTNTGKKKAKQF-----------SLGMKQRLGIAIALL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1631900066 1347 SRAKILLLDEPSAHLDPVTSQVIRKTLKhAFAN--CTVILSEHRL 1389
Cdd:TIGR03740 141 NHPKLLILDEPTNGLDPIGIQELRELIR-SFPEqgITVILSSHIL 184
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1211-1414 |
6.43e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.20 E-value: 6.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1211 VLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLNTEGDIQIDGVSWNTVSVQQ---WRKAFGVIPQkvfifsgtfrm 1287
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFDGQPLHNLNRRQllpVRHRIQVVFQ----------- 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1288 nlDPYGQWN-------------------------DEEIWKVAEEVGLKSVIEQ-FPGQldfvlvdggcvLSHGHKQLMCL 1341
Cdd:PRK15134 370 --DPNSSLNprlnvlqiieeglrvhqptlsaaqrEQQVIAVMEEVGLDPETRHrYPAE-----------FSGGQRQRIAI 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1631900066 1342 ARSVLSRAKILLLDEPSAHLD-PVTSQVIR--KTL--KHAFAnctVILSEHRLEAMLE-CQRFLViednkLRQYESIQK 1414
Cdd:PRK15134 437 ARALILKPSLIILDEPTSSLDkTVQAQILAllKSLqqKHQLA---YLFISHDLHVVRAlCHQVIV-----LRQGEVVEQ 507
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
423-605 |
7.07e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 71.37 E-value: 7.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 423 VLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG------------RISFSPQVSWIMPG-TIKENI 489
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepvpsrarharqRVGVVPQFDNLDPDfTVRENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 490 -IFGvsydeyRYKSvIKACQLEE------DISKFPEKDYTVLGEggiiLSGGQRARISLARAVYKDADLYLLDSPFGHLD 562
Cdd:PRK13537 102 lVFG------RYFG-LSAAAARAlvppllEFAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1631900066 563 IFTEKEIFESCVCKLMANKTRILVTSKLEHL-KIADKILILHEG 605
Cdd:PRK13537 171 PQARHLMWERLRSLLARGKTILLTTHFMEEAeRLCDRLCVIEEG 214
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1207-1406 |
1.02e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 69.80 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1207 GGAAVLENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLN-----TEGDIQIDG---VSWntvSVQQWRKAFGVIPQKV 1278
Cdd:PRK13548 13 GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTL----LRALSgelspDSGEVRLNGrplADW---SPAELARRRAVLPQHS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1279 fifSGTF--------RMNLDPYGQWNDEEiwkvaeevglKSVIEQfpgqldfVLVDGGCV---------LSHGHKQLMCL 1341
Cdd:PRK13548 86 ---SLSFpftveevvAMGRAPHGLSRAED----------DALVAA-------ALAQVDLAhlagrdypqLSGGEQQRVQL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1631900066 1342 ARsVL-------SRAKILLLDEPSAHLDPVTSQVIRKTLKhAFA---NCTVILSEHRLE-AMLECQRFLVIEDNKL 1406
Cdd:PRK13548 146 AR-VLaqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLAR-QLAherGLAVIVVLHDLNlAARYADRIVLLHQGRL 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1197-1362 |
1.19e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.40 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKYGegGAAVLENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLNteGDIQIDGvswNTVSVQQ-WRkaFGVIP 1275
Cdd:COG0488 1 LENLSKSFG--GRPLLDDVSLSINPGDRIGLVGRNGAGKSTL----LKILA--GELEPDS---GEVSIPKgLR--IGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1276 QKVFIFSG-----TFRMNLDPYGQW-------------NDEEIWKVA------EEVG---LKSVIEQFPGQLDFVLVDGG 1328
Cdd:COG0488 68 QEPPLDDDltvldTVLDGDAELRALeaeleeleaklaePDEDLERLAelqeefEALGgweAEARAEEILSGLGFPEEDLD 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 1631900066 1329 C---VLSHGHKQLMCLARSVLSRAKILLLDEPSAHLD 1362
Cdd:COG0488 148 RpvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
423-571 |
1.22e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 69.07 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 423 VLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG-----------------RISFSPQVSWIMPG-T 484
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmsklssaakaelrnqKLGFIYQFHHLLPDfT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 485 IKENI-----IFGVSYDEYRYKS--VIKACQLEEDISKFPEKdytvlgeggiiLSGGQRARISLARAVYKDADLYLLDSP 557
Cdd:PRK11629 104 ALENVampllIGKKKPAEINSRAleMLAAVGLEHRANHRPSE-----------LSGGERQRVAIARALVNNPRLVLADEP 172
|
170
....*....|....
gi 1631900066 558 FGHLDIFTEKEIFE 571
Cdd:PRK11629 173 TGNLDARNADSIFQ 186
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
422-605 |
1.25e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 71.02 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG------------RISFSPQVSWIMPG-TIKEN 488
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvpvpararlaraRIGVVPQFDNLDLEfTVREN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 489 -IIFGvsydeyRYKSvIKACQLEEDISKFPE------KDYTVLGEggiiLSGGQRARISLARAVYKDADLYLLDSPFGHL 561
Cdd:PRK13536 135 lLVFG------RYFG-MSTREIEAVIPSLLEfarlesKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1631900066 562 DIFTEKEIFESCVCKLMANKTRILVTSKLEHL-KIADKILILHEG 605
Cdd:PRK13536 204 DPHARHLIWERLRSLLARGKTILLTTHFMEEAeRLCDRLCVLEAG 248
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
422-620 |
1.28e-12 |
|
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: 69.55 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG-------------RISFSPQVSWIMPGTIKEN 488
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklplhtlrsRLSIILQDPILFSGSIRFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 489 IIFGVSYDEYRYKSVIKACQLEEDISKFPEKDYTVLGEGGIILSGGQRARISLARAVYKDADLYLLDSPFGHLDIFTEKe 568
Cdd:cd03288 115 LDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATEN- 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1631900066 569 IFESCVCKLMANKTRILVTSKLEHLKIADKILILHEGSCYFYGTFSELQGQR 620
Cdd:cd03288 194 ILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQE 245
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1214-1418 |
1.34e-12 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 69.59 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1214 NISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLN-----TEGDIQIDGVSWNTVSVQQWRK-----------AFGVIPQK 1277
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTL----LRCINrliepTSGKVLIDGQDIAAMSRKELRElrrkkismvfqSFALLPHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1278 VFIFSGTFRMNLDpyGQWNDEEIWKVAE---EVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSRAKILLL 1354
Cdd:cd03294 118 TVLENVAFGLEVQ--GVPRAEREERAAEaleLVGLEGWEHKYPDE-----------LSGGMQQRVGLARALAVDPDILLM 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 1355 DEPSAHLDPvtsqVIRKTLK------HAFANCTVILSEHRL-EAMLECQRFLVIEDNKLRQYESIQKLLNE 1418
Cdd:cd03294 185 DEAFSALDP----LIRREMQdellrlQAELQKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1195-1373 |
1.46e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 71.41 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTAKYGEggAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSVQQWRKAFGV 1273
Cdd:PRK09536 4 IDVSDLSVEFGD--TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTpTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1274 IPQKV---FIFSG--TFRMNLDP----YGQWNDEEIWKVAEEVGLKSViEQFPGQlDFVlvdggcVLSHGHKQLMCLARS 1344
Cdd:PRK09536 82 VPQDTslsFEFDVrqVVEMGRTPhrsrFDTWTETDRAAVERAMERTGV-AQFADR-PVT------SLSGGERQRVLLARA 153
|
170 180
....*....|....*....|....*....
gi 1631900066 1345 VLSRAKILLLDEPSAHLDpVTSQVirKTL 1373
Cdd:PRK09536 154 LAQATPVLLLDEPTASLD-INHQV--RTL 179
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
413-602 |
1.51e-12 |
|
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: 67.18 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 413 FSNFPLHAS---PVLQDINFRIEKGQLLAVSGSTGAGKTSLLmMIMGELEPS-QGKIKH--SGRISFSPQVSWIMPGTIK 486
Cdd:cd03223 3 LENLSLATPdgrVLLKDLSFEIKPGDRLLITGPSGTGKSSLF-RALAGLWPWgSGRIGMpeGEDLLFLPQRPYLPLGTLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 487 ENIIfgvsydeyryksvikacqleediskFPEKDytvlgeggiILSGGQRARISLARAVYKDADLYLLDSPFGHLDIFTE 566
Cdd:cd03223 82 EQLI-------------------------YPWDD---------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE 127
|
170 180 190
....*....|....*....|....*....|....*.
gi 1631900066 567 KEIFESCVCKLMankTRILVTSKLEHLKIADKILIL 602
Cdd:cd03223 128 DRLYQLLKELGI---TVISVGHRPSLWKFHDRVLDL 160
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1197-1407 |
1.67e-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: 68.55 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKYGEGGAavLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDG--VSWNTVSVqqwRKAFGV 1273
Cdd:cd03265 3 VENLVKKYGDFEA--VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKpTSGRATVAGhdVVREPREV---RRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1274 IPQKVFIFSG-TFRMNLDPYGQwndeeIWKVAEEVgLKSVIEQFpgqLDFV-LVDGG----CVLSHGHKQLMCLARSVLS 1347
Cdd:cd03265 78 VFQDLSVDDElTGWENLYIHAR-----LYGVPGAE-RRERIDEL---LDFVgLLEAAdrlvKTYSGGMRRRLEIARSLVH 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1631900066 1348 RAKILLLDEPSAHLDPVT-SQVIR--KTLKHAFaNCTVILSEHRL-EAMLECQRFLVIEDNKLR 1407
Cdd:cd03265 149 RPEVLFLDEPTIGLDPQTrAHVWEyiEKLKEEF-GMTILLTTHYMeEAEQLCDRVAIIDHGRII 211
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1212-1419 |
1.72e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 69.86 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1212 LENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDG--VSWNTVS--VQQWRKAFGVIPQ--KVFIFSGT 1284
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKpSSGTITIAGyhITPETGNknLKKLRKKVSLVFQfpEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1285 FRMNLDpYGQWN--------DEEIWKVAEEVGLK-SVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSRAKILLLD 1355
Cdd:PRK13641 103 VLKDVE-FGPKNfgfsedeaKEKALKWLKKVGLSeDLISKSPFE-----------LSGGQMRRVAIAGVMAYEPEILCLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1631900066 1356 EPSAHLDPVTSQVIRKTLK-HAFANCTVILSEHRLEAMLE-CQRFLVIEDNKLRQYESIQKLLNEK 1419
Cdd:PRK13641 171 EPAAGLDPEGRKEMMQLFKdYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1195-1405 |
2.04e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 69.83 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTAKYGEggAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLNTE-GDIQIDGVSWNTVSvQQWRKAFGV 1273
Cdd:PRK13537 8 IDFRNVEKRYGD--KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDaGSISLCGEPVPSRA-RHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1274 IPQkvfiFSgtfrmNLDPygqwnD----EEIWKVAEEVGLKS--VIEQFPGQLDFVLVDGGC-----VLSHGHKQLMCLA 1342
Cdd:PRK13537 85 VPQ----FD-----NLDP-----DftvrENLLVFGRYFGLSAaaARALVPPLLEFAKLENKAdakvgELSGGMKRRLTLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1631900066 1343 RSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFANC-TVILSEHRL-EAMLECQRFLVIEDNK 1405
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGkTILLTTHFMeEAERLCDRLCVIEEGR 215
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
423-619 |
2.27e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 69.37 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 423 VLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKI---------KHSGRISFspqvswiMP---G-----TI 485
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVlwdgepldpEDRRRIGY-------LPeerGlypkmKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 486 KENIIF-----GVSydeyryKSVIKAcQLEEDISKF--PEKDYTVLGEggiiLSGGQRARISLARAVYKDADLYLLDSPF 558
Cdd:COG4152 89 GEQLVYlarlkGLS------KAEAKR-RADEWLERLglGDRANKKVEE----LSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1631900066 559 GHLD-----IFtEKEIFEscvckLMAN-KTRILVTSKLEHL-KIADKILILHEGSCYFYGTFSELQGQ 619
Cdd:COG4152 158 SGLDpvnveLL-KDVIRE-----LAAKgTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
419-606 |
2.62e-12 |
|
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: 68.29 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 419 HASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGRI-------SFSPQVSWIM--------PG 483
Cdd:COG1124 16 RRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPvtrrrrkAFRRRVQMVFqdpyaslhPR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 484 -TIKENI-----IFGVSYDEYRYKSVIKACQLEEDI-SKFPEKdytvlgeggiiLSGGQRARISLARAVYKDADLYLLDS 556
Cdd:COG1124 96 hTVDRILaeplrIHGLPDREERIAELLEQVGLPPSFlDRYPHQ-----------LSGGQRQRVAIARALILEPELLLLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1631900066 557 PFGHLDIFTEKEIFEsCVCKLMA--NKTRILVT---SKLEHLkiADKILILHEGS 606
Cdd:COG1124 165 PTSALDVSVQAEILN-LLKDLREerGLTYLFVShdlAVVAHL--CDRVAVMQNGR 216
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1196-1409 |
2.81e-12 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 70.10 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1196 TVKDLTAKYGegGAAVLENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLN-----TEGDIQIDGVSWNTVSVQQwRK- 1269
Cdd:COG3839 5 ELENVSKSYG--GVEALKDIDLDIEDGEFLVLLGPSGCGKSTL----LRMIAgledpTSGEILIGGRDVTDLPPKD-RNi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1270 -------------------AFGVIPQKVfifsgtfrmnldpygqwNDEEIWK----VAEEVGLKSVIEQFPGQldfvlvd 1326
Cdd:COG3839 78 amvfqsyalyphmtvyeniAFPLKLRKV-----------------PKAEIDRrvreAAELLGLEDLLDRKPKQ------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1327 ggcvLSHGHKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLK--HAFANCTVILSEH-RLEAMLECQRFLVIED 1403
Cdd:COG3839 134 ----LSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKrlHRRLGTTTIYVTHdQVEAMTLADRIAVMND 209
|
....*.
gi 1631900066 1404 NKLRQY 1409
Cdd:COG3839 210 GRIQQV 215
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
428-632 |
3.04e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 68.07 E-value: 3.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 428 NFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGR-----------ISFSPQVSWIMPG-TIKENIIFGV-- 493
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtttppsrrpVSMLFQENNLFSHlTVAQNIGLGLnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 494 -----SYDEYRYKSVIKACQLEEDISKFPEKdytvlgeggiiLSGGQRARISLARAVYKDADLYLLDSPFGHLDIFTEKE 568
Cdd:PRK10771 99 glklnAAQREKLHAIARQMGIEDLLARLPGQ-----------LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1631900066 569 IFE--SCVCKlMANKTRILVTSKLEH-LKIADKILILHEGSCYFYGTFSELQGQRPDfSSELMGFDS 632
Cdd:PRK10771 168 MLTlvSQVCQ-ERQLTLLMVSHSLEDaARIAPRSLVVADGRIAWDGPTDELLSGKAS-ASALLGIKS 232
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1195-1363 |
3.59e-12 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 67.00 E-value: 3.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTakYGEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLN-----TEGDIQIDGVSWNTVSVQqwrk 1269
Cdd:TIGR01189 1 LAARNLA--CSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTL----LRILAgllrpDSGEVRWNGTPLAEQRDE---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1270 afgviPQKVFIFSG---------TFRMNLD---PYGQWNDEEIWKVAEEVGLKSvIEQFP-GQldfvlvdggcvLSHGHK 1336
Cdd:TIGR01189 71 -----PHENILYLGhlpglkpelSALENLHfwaAIHGGAQRTIEDALAAVGLTG-FEDLPaAQ-----------LSAGQQ 133
|
170 180
....*....|....*....|....*..
gi 1631900066 1337 QLMCLARSVLSRAKILLLDEPSAHLDP 1363
Cdd:TIGR01189 134 RRLALARLWLSRRPLWILDEPTTALDK 160
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
422-616 |
4.17e-12 |
|
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: 67.61 E-value: 4.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGeLE-PSQGKIKHSGRI----------SFSPQVSWIMPG------- 483
Cdd:cd03258 19 TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCING-LErPTSGSVLVDGTDltllsgkelrKARRRIGMIFQHfnllssr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 484 TIKENI-----IFGVSyDEYRYKSV---IKACQLEEDISKFPEKdytvlgeggiiLSGGQRARISLARAVYKDADLYLLD 555
Cdd:cd03258 98 TVFENValpleIAGVP-KAEIEERVlelLELVGLEDKADAYPAQ-----------LSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1631900066 556 SPFGHLDIFTEKEIFE---SCVCKLmaNKTRILVTSKLEHLK-IADKILILHEGSCYFYGTFSEL 616
Cdd:cd03258 166 EATSALDPETTQSILAllrDINREL--GLTIVLITHEMEVVKrICDRVAVMEKGEVVEEGTVEEV 228
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1195-1425 |
4.26e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 70.60 E-value: 4.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTAKYGegGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFaFLRLL----NTEGDI-----------QID---- 1255
Cdd:TIGR03269 1 IEVKNLTKKFD--GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMH-VLRGMdqyePTSGRIiyhvalcekcgYVErpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1256 --------GVSWNTVSVQQW---RKAFGVIPQKVFI-FSGTFRMnldpYGqwND---EEIWKVAEEVGLKS--------- 1311
Cdd:TIGR03269 78 vgepcpvcGGTLEPEEVDFWnlsDKLRRRIRKRIAImLQRTFAL----YG--DDtvlDNVLEALEEIGYEGkeavgravd 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1312 VIEQFpgQLDFVLVDGGCVLSHGHKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAF--ANCTVILSEHRL 1389
Cdd:TIGR03269 152 LIEMV--QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHWP 229
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1631900066 1390 EAMLE-CQRFLVIEDNKLRQY----ESIQKLLNEKSSFRQA 1425
Cdd:TIGR03269 230 EVIEDlSDKAIWLENGEIKEEgtpdEVVAVFMEGVSEVEKE 270
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
416-605 |
4.33e-12 |
|
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: 67.13 E-value: 4.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 416 FPLHASPVLQDINFriEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGR-ISFSP----QVSWIMPG------- 483
Cdd:cd03298 8 FSYGEQPMHFDLTF--AQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVdVTAAPpadrPVSMLFQEnnlfahl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 484 TIKENIIFGVS-------YDEYRYKSVIKACQLEEDISKFPEKdytvlgeggiiLSGGQRARISLARAVYKDADLYLLDS 556
Cdd:cd03298 86 TVEQNVGLGLSpglkltaEDRQAIEVALARVGLAGLEKRLPGE-----------LSGGERQRVALARVLVRDKPVLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1631900066 557 PFGHLDIFTEKEIFEsCVCKLMANK--TRILVTSKLEH-LKIADKILILHEG 605
Cdd:cd03298 155 PFAALDPALRAEMLD-LVLDLHAETkmTVLMVTHQPEDaKRLAQRVVFLDNG 205
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1194-1387 |
5.31e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 67.63 E-value: 5.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1194 KMTVKDLTAKYGEggAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN------TEGDIQIDGVSWNTVSVQQW 1267
Cdd:PRK14247 3 KIEIRDLKVSFGQ--VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypearVSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1268 RKAFGVIPQ------KVFIFSG-TFRMNLDPYGQWNDEEIWKVAEEVGLKSVIEQFPGQLDfvlvDGGCVLSHGHKQLMC 1340
Cdd:PRK14247 81 RRRVQMVFQipnpipNLSIFENvALGLKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLD----APAGKLSGGQQQRLC 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1631900066 1341 LARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFANCTVILSEH 1387
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTH 203
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
423-611 |
5.48e-12 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 66.83 E-value: 5.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 423 VLQDINFRIEKGqLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG------------RISFSPQVswimpgtikenii 490
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqpqklrrRIGYLPQE------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 491 FGV-----SYDEYRYKSVIK----------ACQLEEDISKFPEKDYTVLGeggiiLSGGQRARISLARAVYKDADLYLLD 555
Cdd:cd03264 81 FGVypnftVREFLDYIAWLKgipskevkarVDEVLELVNLGDRAKKKIGS-----LSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1631900066 556 SPFGHLDIfTEKEIFESCVCKLMANKTRILVTSKLEHLK-IADKILILHEGSCYFYG 611
Cdd:cd03264 156 EPTAGLDP-EERIRFRNLLSELGEDRIVILSTHIVEDVEsLCNQVAVLNKGKLVFEG 211
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1207-1421 |
5.89e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 68.96 E-value: 5.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1207 GGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSVQQWRKAFgvipqkVFIFSGTF 1285
Cdd:PRK10851 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHqTSGHIRFHGTDVSRLHARDRKVGF------VFQHYALF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1286 R-MNL---------------DPYGQWNDEEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSRA 1349
Cdd:PRK10851 87 RhMTVfdniafgltvlprreRPNAAAIKAKVTQLLEMVQLAHLADRYPAQ-----------LSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1631900066 1350 KILLLDEPSAHLDpvtSQViRKTLK------HAFANCTVILSEH-RLEAMLECQRFLVIEDNKLRQYESIQKLLNEKSS 1421
Cdd:PRK10851 156 QILLLDEPFGALD---AQV-RKELRrwlrqlHEELKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPAT 230
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1197-1387 |
5.91e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 67.80 E-value: 5.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKYGEGGAAvLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDG--VSWNTVSVQQWRKAFGV 1273
Cdd:PRK13639 4 TRDLKYSYPDGTEA-LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKpTSGEVLIKGepIKYDKKSLLEVRKTVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1274 IPQKV--FIFSGTFR-------MNLdpygQWNDEEIWKVAEE----VGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMC 1340
Cdd:PRK13639 83 VFQNPddQLFAPTVEedvafgpLNL----GLSKEEVEKRVKEalkaVGMEGFENKPPHH-----------LSGGQKKRVA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1631900066 1341 LARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFAN-CTVILSEH 1387
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEgITIIISTH 195
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
424-569 |
6.16e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.99 E-value: 6.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 424 LQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGR----------ISFSPQ---VSWIMPGTIKENII 490
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVPQseeVDWSFPVLVEDVVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 491 FG-------VSYDEYRYKSVIKACQLEEDISKFPEKDytvLGEggiiLSGGQRARISLARAVYKDADLYLLDSPFGHLDI 563
Cdd:PRK15056 103 MGryghmgwLRRAKKRDRQIVTAALARVDMVEFRHRQ---IGE----LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
....*.
gi 1631900066 564 FTEKEI 569
Cdd:PRK15056 176 KTEARI 181
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
424-616 |
6.46e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 69.29 E-value: 6.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 424 LQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG-----------------RISFSPQVSWIMPG-TI 485
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelrevrrkKIAMVFQSFALMPHmTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 486 KENIIFG-----VSYDEYRYKSV--IKACQLEEDISKFPEKdytvlgeggiiLSGGQRARISLARAVYKDADLYLLDSPF 558
Cdd:PRK10070 124 LDNTAFGmelagINAEERREKALdaLRQVGLENYAHSYPDE-----------LSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 559 GHLDIFTEKEIFESCVcKLMA--NKTRILVTSKL-EHLKIADKILILHEGSCYFYGTFSEL 616
Cdd:PRK10070 193 SALDPLIRTEMQDELV-KLQAkhQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
424-616 |
6.84e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 68.12 E-value: 6.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 424 LQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKI--------------------KHSGrISFSPQVSWIMPG 483
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVtigervitagkknkklkplrKKVG-IVFQFPEHQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 484 TIKENIIFG-----VSYDE--YRYKSVIKACQLEEDI---SKFPekdytvlgeggiiLSGGQRARISLARAVYKDADLYL 553
Cdd:PRK13634 102 TVEKDICFGpmnfgVSEEDakQKAREMIELVGLPEELlarSPFE-------------LSGGQMRRVAIAGVLAMEPEVLV 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 554 LDSPFGHLDIFTEKEIFEscvcklM-------ANKTRILVTSKLEHL-KIADKILILHEGSCYFYGTFSEL 616
Cdd:PRK13634 169 LDEPTAGLDPKGRKEMME------MfyklhkeKGLTTVLVTHSMEDAaRYADQIVVMHKGTVFLQGTPREI 233
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
422-563 |
6.87e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.44 E-value: 6.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGRISFSPQVSWIM-----------PGTIKENII 490
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAChylghrnamkpALTVAENLE 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1631900066 491 FGVSY---DEYRYKSVIKACQLeEDISKFPEKDytvlgeggiiLSGGQRARISLARAVYKDADLYLLDSPFGHLDI 563
Cdd:PRK13539 96 FWAAFlggEELDIAAALEAVGL-APLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
422-611 |
7.38e-12 |
|
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: 66.04 E-value: 7.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSqgkikhsgrisfspqvswIMPGTIKENiifGVSYDEYRYK 501
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGL------------------GVSGEVLIN---GRPLDKRSFR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 502 SVIKACQlEEDISkFPEK------DYTVLGEGgiiLSGGQRARISLARAVYKDADLYLLDSPFGHLDIFTEKEIFEScvc 575
Cdd:cd03213 82 KIIGYVP-QDDIL-HPTLtvretlMFAAKLRG---LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSL--- 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1631900066 576 kLMA----NKTRILVT----SKLEHLkiADKILILHEGSCYFYG 611
Cdd:cd03213 154 -LRRladtGRTIICSIhqpsSEIFEL--FDKLLLLSQGRVIYFG 194
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
416-563 |
1.17e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 65.64 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 416 FPLHASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKI----KHSGRISFSPQVSWI--MPG-----T 484
Cdd:PRK13543 19 FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqidgKTATRGDRSRFMAYLghLPGlkadlS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 485 IKENIIFGVSYDEYRYKsvikacqleedisKFPEKDYTVLGEGGII------LSGGQRARISLARAVYKDADLYLLDSPF 558
Cdd:PRK13543 99 TLENLHFLCGLHGRRAK-------------QMPGSALAIVGLAGYEdtlvrqLSAGQKKRLALARLWLSPAPLWLLDEPY 165
|
....*
gi 1631900066 559 GHLDI 563
Cdd:PRK13543 166 ANLDL 170
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1195-1408 |
1.26e-11 |
|
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: 65.74 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTAKYGEggAAVLENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLN-----TEGDIQIDGVSWNTVS------ 1263
Cdd:cd03301 1 VELENVTKRFGN--VTALDDLNLDIADGEFVVLLGPSGCGKTTT----LRMIAgleepTSGRIYIGGRDVTDLPpkdrdi 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1264 --VQQwrkAFGVIPQKVFIFSGTFRMNLDPYGQWN-DEEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMC 1340
Cdd:cd03301 75 amVFQ---NYALYPHMTVYDNIAFGLKLRKVPKDEiDERVREVAELLQIEHLLDRKPKQ-----------LSGGQRQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 1341 LARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLK--HAFANCTVILSEH-RLEAMLECQRFLVIEDNKLRQ 1408
Cdd:cd03301 141 LGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKrlQQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQ 211
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
422-615 |
1.31e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 66.58 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG-------------RISFSPQVSWIMPG-TIKE 487
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlarRLALLPQHHLTPEGiTVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 488 NIIFGVS-----------YDEYRYKSVIKACQLEEdiskFPEKDYTVLgeggiilSGGQRARISLARAVYKDADLYLLDS 556
Cdd:PRK11231 96 LVAYGRSpwlslwgrlsaEDNARVNQAMEQTRINH----LADRRLTDL-------SGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1631900066 557 PFGHLDIFTEKEIFescvcKLM-----ANKTRILVTSKLEHL-KIADKILILHEGSCYFYGTFSE 615
Cdd:PRK11231 165 PTTYLDINHQVELM-----RLMrelntQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEE 224
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1212-1432 |
1.79e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 69.38 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1212 LENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLNTegdiqidgVSWNTVSVqqwRKAFGVIPQKVFIFSGTFRMNLDP 1291
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPP--------RSDASVVI---RGTVAYVPQVSWIFNATVRDNILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1292 YGQWNDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSRAKILLLDEPSAHLDP-VTSQVIR 1370
Cdd:PLN03130 702 GSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAhVGRQVFD 781
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1631900066 1371 KTLKHAFANCTVILSEHRLEAMLECQRFLVIEDNKLRQYESIQKLLNEKSSFRQAISHADRL 1432
Cdd:PLN03130 782 KCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMENAGKM 843
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
399-605 |
2.00e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 66.17 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 399 NNNSKAPSTDNNLFFSnFPLHASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKI------------- 465
Cdd:PRK13632 1 IKNKSVMIKVENVSFS-YPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIkidgitiskenlk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 466 ---KHSGRISFSPQVSWImPGTIKENIIFGVS---YDEYRYKSVI----KACQLEEDISKFPEKdytvlgeggiiLSGGQ 535
Cdd:PRK13632 80 eirKKIGIIFQNPDNQFI-GATVEDDIAFGLEnkkVPPKKMKDIIddlaKKVGMEDYLDKEPQN-----------LSGGQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1631900066 536 RARISLARAVYKDADLYLLDSPFGHLDIFTEKEIFescvcKLM------ANKTRILVTSKLEHLKIADKILILHEG 605
Cdd:PRK13632 148 KQRVAIASVLALNPEIIIFDESTSMLDPKGKREIK-----KIMvdlrktRKKTLISITHDMDEAILADKVIVFSEG 218
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1198-1406 |
2.02e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 66.26 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1198 KDLTAKYGEGGAA----VLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLL-NTEGDIQIDGVSW-NTVSVQQWRKAF 1271
Cdd:PRK13633 8 KNVSYKYESNEESteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLiPSEGKVYVDGLDTsDEENLWDIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1272 GVIPQK--------------VFifsGTFRMNLDPygqwndEEIWKVAEEvGLKSV----IEQFPGQLdfvlvdggcvLSH 1333
Cdd:PRK13633 88 GMVFQNpdnqivativeedvAF---GPENLGIPP------EEIRERVDE-SLKKVgmyeYRRHAPHL----------LSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1631900066 1334 GHKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLK--HAFANCTVILSEHRLEAMLECQRFLVIEDNKL 1406
Cdd:PRK13633 148 GQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKelNKKYGITIILITHYMEEAVEADRIIVMDSGKV 222
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1211-1401 |
2.37e-11 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 65.43 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1211 VLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDG-VSWNTVSvqQWRKAFGVI-PQKVFIF-----S 1282
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQpTSGEVRVAGlVPWKRRK--KFLRRIGVVfGQKTQLWwdlpvI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1283 GTFRMNLDPYGQWNDE---EIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSRAKILLLDEPSA 1359
Cdd:cd03267 114 DSFYLLAAIYDLPPARfkkRLDELSELLDLEELLDTPVRQL-----------SLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1631900066 1360 HLDPVTSQVIRKTLKHAFAN--CTVILSEHRL---EAMleCQRFLVI 1401
Cdd:cd03267 183 GLDVVAQENIRNFLKEYNRErgTTVLLTSHYMkdiEAL--ARRVLVI 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
422-616 |
2.63e-11 |
|
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: 65.49 E-value: 2.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGK----------------IKHsgRISF-SPQVSWIMPGT 484
Cdd:COG1119 17 TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrlfgerrggedvweLRK--RIGLvSPALQLRFPRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 485 IK-ENII----FGVS--YDEYRYKSVIKACQ-LEE-DISKFPEKDYTVlgeggiiLSGGQRARISLARAVYKDADLYLLD 555
Cdd:COG1119 95 ETvLDVVlsgfFDSIglYREPTDEQRERARElLELlGLAHLADRPFGT-------LSQGEQRRVLIARALVKDPELLILD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1631900066 556 SPFGHLDIFtEKEIFESCVCKLMAN--KTRILVTSKLEhlKIADKI---LILHEGSCYFYGTFSEL 616
Cdd:COG1119 168 EPTAGLDLG-ARELLLALLDKLAAEgaPTLVLVTHHVE--EIPPGIthvLLLKDGRVVAAGPKEEV 230
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
422-605 |
3.58e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 66.89 E-value: 3.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGR-ISFSP----------QVSWIMPG-TIKENI 489
Cdd:PRK09452 28 EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQdITHVPaenrhvntvfQSYALFPHmTVFENV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 490 IFG-----VSYDEY--RYKSVIKACQLEEDISKFPEKdytvlgeggiiLSGGQRARISLARAVYKDADLYLLDSPFGHLD 562
Cdd:PRK09452 108 AFGlrmqkTPAAEItpRVMEALRMVQLEEFAQRKPHQ-----------LSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1631900066 563 IFTEKEifescvcklMANK----------TRILVT-SKLEHLKIADKILILHEG 605
Cdd:PRK09452 177 YKLRKQ---------MQNElkalqrklgiTFVFVThDQEEALTMSDRIVVMRDG 221
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
415-612 |
3.66e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 65.39 E-value: 3.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 415 NFPlHASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGRISFSPQVswiMPGTIKeniIFGVS 494
Cdd:PRK13644 10 SYP-DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSK---LQGIRK---LVGIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 495 YDEYRYKSVIKAcqLEEDISKFPE-----------KDYTVLGEGGI---------ILSGGQRARISLARAVYKDADLYLL 554
Cdd:PRK13644 83 FQNPETQFVGRT--VEEDLAFGPEnlclppieirkRVDRALAEIGLekyrhrspkTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1631900066 555 DSPFGHLDIFTEKEIFESCVCKLMANKTRILVTSKLEHLKIADKILILHEGSCYFYGT 612
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
422-611 |
3.90e-11 |
|
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: 63.82 E-value: 3.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEpsqGKIKHSGRISFSpqvswimpgtikeniifGVSYDEY--R 499
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTE---GNVSVEGDIHYN-----------------GIPYKEFaeK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 500 YKSVIKACQlEEDIsKFPEK------DYTVLGEGGIIL---SGGQRARISLARAVYKDADLYLLDSPFGHLDIFTEKEIF 570
Cdd:cd03233 81 YPGEIIYVS-EEDV-HFPTLtvretlDFALRCKGNEFVrgiSGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEIL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1631900066 571 eSCVcKLMANKTRILVTSKL-----EHLKIADKILILHEGSCYFYG 611
Cdd:cd03233 159 -KCI-RTMADVLKTTTFVSLyqasdEIYDLFDKVLVLYEGRQIYYG 202
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1210-1387 |
5.37e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 64.68 E-value: 5.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1210 AVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLNT-EGDIQIDGVSWN------TVSVQQWRKAFGVIPQKVFIFS 1282
Cdd:PRK14246 24 AILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIyDSKIKVDGKVLYfgkdifQIDAIKLRKEVGMVFQQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1283 -----GTFRMNLDPYGQWNDEEIWKVAEE----VGL-KSVIEQfpgqldfvLVDGGCVLSHGHKQLMCLARSVLSRAKIL 1352
Cdd:PRK14246 104 hlsiyDNIAYPLKSHGIKEKREIKKIVEEclrkVGLwKEVYDR--------LNSPASQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190
....*....|....*....|....*....|....*
gi 1631900066 1353 LLDEPSAHLDPVTSQVIRKTLKHAFANCTVILSEH 1387
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSH 210
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
425-562 |
5.43e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 63.67 E-value: 5.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 425 QDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIK------HSGRISFSPQVSWI--MPGtIK------ENII 490
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLwqgepiRRQRDEYHQDLLYLghQPG-IKteltalENLR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 491 FgvsydeyryksvikACQLEEDISkfPEKDYTVLGEGGII---------LSGGQRARISLARAVYKDADLYLLDSPFGHL 561
Cdd:PRK13538 97 F--------------YQRLHGPGD--DEALWEALAQVGLAgfedvpvrqLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
.
gi 1631900066 562 D 562
Cdd:PRK13538 161 D 161
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1195-1425 |
5.50e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 65.25 E-value: 5.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTAKYGEGGAAvLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDG--VSWNTVSVQQWRKAF 1271
Cdd:PRK13636 6 LKVEELNYNYSDGTHA-LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKpSSGRILFDGkpIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1272 GVIPQKV--FIFSGTFRMNLDpYGQWN----DEEIWKVAEEVGLKSVIEQFPGQLDFVLvdggcvlSHGHKQLMCLARSV 1345
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYQDVS-FGAVNlklpEDEVRKRVDNALKRTGIEHLKDKPTHCL-------SFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1346 LSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFA--NCTVILSEHRLEAM-LECQRFLVIEDNKLRQYESIQKLLNEKSSF 1422
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEVFAEKEML 236
|
...
gi 1631900066 1423 RQA 1425
Cdd:PRK13636 237 RKV 239
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
422-563 |
7.09e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 66.02 E-value: 7.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG-------------RISFSPQ-VSWIMPGTIKE 487
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraasrRVASVPQdTSLSFEFDVRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 488 NIIFGVSYDEYRY-------KSVIKACQLEEDISKFPEKDYTVlgeggiiLSGGQRARISLARAVYKDADLYLLDSPFGH 560
Cdd:PRK09536 97 VVEMGRTPHRSRFdtwtetdRAAVERAMERTGVAQFADRPVTS-------LSGGERQRVLLARALAQATPVLLLDEPTAS 169
|
...
gi 1631900066 561 LDI 563
Cdd:PRK09536 170 LDI 172
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
845-1154 |
7.32e-11 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 64.93 E-value: 7.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 845 LIFVLILCVTVFlievaASLAGLWFLKKTALKANATQSEnstsdkppvivtdTSAYYIIYIYVGVADTLLAMGIFRGLPL 924
Cdd:cd18559 3 LLIKLVLCNHVF-----SGPSNLWLLLWFDDPVNGPQEH-------------GQVYLSVLGALAILQGITVFQYSMAVSI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 925 VHtlITVSKTLHQKMVHAVLHAPMSTFNSWKAGGMLNRFAKDTAVLDDLLPLTVFDFVQLILIVIGAITVVSILQPyIFL 1004
Cdd:cd18559 65 GG--IFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGP-MAA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1005 ASVPVIAAFIVLRAYFLHTSQQLKQLESEARSPIFTHLVTSLKGLWTLRAFGrqpyFETLFHKALNLHTANWFLYLST-- 1082
Cdd:cd18559 142 VGIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFE----WEEAFIRQVDAKRDNELAYLPSiv 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1631900066 1083 -LRWFQMRIEIIFVVFFVAVAFISIITTGDGPGRVGIILTLAMNIMGTLQWAVNSSIDVDSLMRSVGRIFKFI 1154
Cdd:cd18559 218 yLRALAVRLWCVGPCIVLFASFFAYVSRHSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
424-605 |
8.48e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 64.64 E-value: 8.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 424 LQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQG--------------KIKHSGRISFSPQVSWIMP------G 483
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqtivgdyaipanlkKIKEVKRLRKEIGLVFQFPeyqlfqE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 484 TIKENIIFGVSY----DEYRYKSV---IKACQLEEDISKfpekdytvlgEGGIILSGGQRARISLARAVYKDADLYLLDS 556
Cdd:PRK13645 107 TIEKDIAFGPVNlgenKQEAYKKVpelLKLVQLPEDYVK----------RSPFELSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1631900066 557 PFGHLDIFTEKEiFESCVCKLMANKTR--ILVTSKLEH-LKIADKILILHEG 605
Cdd:PRK13645 177 PTGGLDPKGEED-FINLFERLNKEYKKriIMVTHNMDQvLRIADEVIVMHEG 227
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
484-625 |
8.49e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.98 E-value: 8.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 484 TIKENIIFGvsYDEYRYKSVIKACQ---LEEDISKFPEKDYTVLGEGGIILSGGQRARISLARAVYKDADLYLLDSPFGH 560
Cdd:PTZ00265 1311 SIYENIKFG--KEDATREDVKRACKfaaIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSS 1388
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1631900066 561 LDIFTEKEIFESCV-CKLMANKTRILVTSKLEHLKIADKILILHEGScyFYGTFSELQGQRPDFSS 625
Cdd:PTZ00265 1389 LDSNSEKLIEKTIVdIKDKADKTIITIAHRIASIKRSDKIVVFNNPD--RTGSFVQAHGTHEELLS 1452
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
424-617 |
8.94e-11 |
|
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: 63.16 E-value: 8.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 424 LQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG------------RISFSPQVSWIMPG-TIKENI- 489
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrrRIGIVFQDLSVDDElTGWENLy 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 490 ----IFGVSYDEYRYK--SVIKACQLEEDISKfPEKDYtvlgeggiilSGGQRARISLARAVYKDADLYLLDSPFGHLDI 563
Cdd:cd03265 96 iharLYGVPGAERRERidELLDFVGLLEAADR-LVKTY----------SGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1631900066 564 FTEKEIFEScVCKLMA--NKTRILVTSKLEHL-KIADKILILHEGSCYFYGTFSELQ 617
Cdd:cd03265 165 QTRAHVWEY-IEKLKEefGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1197-1402 |
9.05e-11 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 63.97 E-value: 9.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKYGEGGAAvLENISFSIDSGQRVGLLGRTGSGKSTllfaFLRLLN-----TEGDIQIDGVswnTVSVQqwrkaf 1271
Cdd:cd03237 1 YTYPTMKKTLGEFT-LEVEGGSISESEVIGILGPNGIGKTT----FIKMLAgvlkpDEGDIEIELD---TVSYK------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1272 gviPQKV----------FIFSGTFRMNLDPYgqWNDEeiwkVAEEVGLKSVIEQfpgQLDfvlvdggcVLSHGHKQLMCL 1341
Cdd:cd03237 67 ---PQYIkadyegtvrdLLSSITKDFYTHPY--FKTE----IAKPLQIEQILDR---EVP--------ELSGGELQRVAI 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1631900066 1342 ARSVLSRAKILLLDEPSAHLDP----VTSQVIRKTLKHafANCTVILSEHR-LEAMLECQRFLVIE 1402
Cdd:cd03237 127 AACLSKDADIYLLDEPSAYLDVeqrlMASKVIRRFAEN--NEKTAFVVEHDiIMIDYLADRLIVFE 190
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
409-616 |
9.14e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 64.27 E-value: 9.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 409 NNLFFsNFPLHASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGRIsFSPQVSW--------- 479
Cdd:PRK13635 9 EHISF-RYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV-LSEETVWdvrrqvgmv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 480 -------IMPGTIKENIIF-----GVSYDEY--RYKSVIKACQLEEDISKFPEKdytvlgeggiiLSGGQRARISLARAV 545
Cdd:PRK13635 87 fqnpdnqFVGATVQDDVAFgleniGVPREEMveRVDQALRQVGMEDFLNREPHR-----------LSGGQKQRVAIAGVL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1631900066 546 YKDADLYLLDSPFGHLDIFTEKEIFEscVCKLMANKTRILV---TSKLEHLKIADKILILHEGSCYFYGTFSEL 616
Cdd:PRK13635 156 ALQPDIIILDEATSMLDPRGRREVLE--TVRQLKEQKGITVlsiTHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
1203-1415 |
1.07e-10 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 64.33 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1203 KYGEGGAavLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGvsWNTVS-VQQWRKAFGVIPQKVFI 1280
Cdd:TIGR01188 2 VYGDFKA--VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRpTSGTARVAG--YDVVRePRKVRRSIGIVPQYASV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1281 FSG-TFRMNLDPYGQWNDEEiWKVAEEvGLKSVIEQFPgqldfvLVDGGCVL----SHGHKQLMCLARSVLSRAKILLLD 1355
Cdd:TIGR01188 78 DEDlTGRENLEMMGRLYGLP-KDEAEE-RAEELLELFE------LGEAADRPvgtySGGMRRRLDIAASLIHQPDVLFLD 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1631900066 1356 EPSAHLDPVTSQVIR---KTLKHafANCTVILSEHRL-EAMLECQRFLVIEDNKLRQYESIQKL 1415
Cdd:TIGR01188 150 EPTTGLDPRTRRAIWdyiRALKE--EGVTILLTTHYMeEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1199-1387 |
1.08e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 63.71 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1199 DLTAKYGEGgaAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN------TEGDIQIDGVSWNTVSVQ--QWRKA 1270
Cdd:PRK14267 9 NLRVYYGSN--HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneearVEGEVRLFGRNIYSPDVDpiEVRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1271 FGVipqkVFIFSGTF---------------------RMNLDPYGQW--NDEEIWkvaEEVglKSVIEQFPGQLdfvlvdg 1327
Cdd:PRK14267 87 VGM----VFQYPNPFphltiydnvaigvklnglvksKKELDERVEWalKKAALW---DEV--KDRLNDYPSNL------- 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1328 gcvlSHGHKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFANCTVILSEH 1387
Cdd:PRK14267 151 ----SGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1195-1425 |
1.50e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 63.67 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTAKYGEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLL----NTEGDIQIDGVSWNTVSVQQWRKA 1270
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpddNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1271 FGVI---PQKVFI---FSGTFRMNLDPYGQWNDEEI---WKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCL 1341
Cdd:PRK13640 86 VGIVfqnPDNQFVgatVGDDVAFGLENRAVPRPEMIkivRDVLADVGMLDYIDSEPAN-----------LSGGQKQRVAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1342 ARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFA--NCTVILSEHRLEAMLECQRFLVIEDNKLRQYESIQKLLNEK 1419
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
....*.
gi 1631900066 1420 SSFRQA 1425
Cdd:PRK13640 235 EMLKEI 240
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
409-623 |
1.54e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 63.98 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 409 NNLFFSNFPLhASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG-RISFSPQVSWIMPGTIKE 487
Cdd:PRK13643 8 NYTYQPNSPF-ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDiVVSSTSKQKEIKPVRKKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 488 NIIFGVSYDEYRYKSVIKACQL--------EEDISKFPEKDYTVLG-------EGGIILSGGQRARISLARAVYKDADLY 552
Cdd:PRK13643 87 GVVFQFPESQLFEETVLKDVAFgpqnfgipKEKAEKIAAEKLEMVGladefweKSPFELSGGQMRRVAIAGILAMEPEVL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1631900066 553 LLDSPFGHLDIFTEKEIFESCVCKLMANKTRILVTSKLEHL-KIADKILILHEGSCYFYGTFSELqGQRPDF 623
Cdd:PRK13643 167 VLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVaDYADYVYLLEKGHIISCGTPSDV-FQEVDF 237
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1211-1259 |
1.78e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 62.79 E-value: 1.78e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1631900066 1211 VLENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLN-----TEGDIQIDG-VSW 1259
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTL----LKLIAgilepTSGRVEVNGrVSA 91
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
418-612 |
1.79e-10 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 63.25 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 418 LHASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGRisfsPQVSW----------IMPG---- 483
Cdd:PRK13548 12 LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGR----PLADWspaelarrraVLPQhssl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 484 ----TIKENIIFGVS---YDEYRYKSVIKACQLEEDISKFPEKDYTVlgeggiiLSGGQRARISLARA---VYKDAD--- 550
Cdd:PRK13548 88 sfpfTVEEVVAMGRAphgLSRAEDDALVAAALAQVDLAHLAGRDYPQ-------LSGGEQQRVQLARVlaqLWEPDGppr 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1631900066 551 LYLLDSPFGHLDIFTEKEIFEscVCKLMANKTRILVTSKLEHLKIA----DKILILHEGSCYFYGT 612
Cdd:PRK13548 161 WLLLDEPTSALDLAHQHHVLR--LARQLAHERGLAVIVVLHDLNLAaryaDRIVLLHQGRLVADGT 224
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
423-612 |
1.91e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 64.10 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 423 VLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQG-----KIKHSGRISFSPQVSWIMPGTIKE--------NI 489
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGtiqvgDIYIGDKKNNHELITNPYSKKIKNfkelrrrvSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 490 IFgvSYDEYR-YKSVIkacqlEEDISKFP------------------EK---DYTVLGEGGIILSGGQRARISLARAVYK 547
Cdd:PRK13631 121 VF--QFPEYQlFKDTI-----EKDIMFGPvalgvkkseakklakfylNKmglDDSYLERSPFGLSGGQKRRVAIAGILAI 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1631900066 548 DADLYLLDSPFGHLDIFTEKEIFESCVCKLMANKTRILVTSKLEH-LKIADKILILHEGSCYFYGT 612
Cdd:PRK13631 194 QPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHvLEVADEVIVMDKGKILKTGT 259
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1216-1404 |
1.93e-10 |
|
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: 62.13 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1216 SFSIDSGQRVGLLGRTGSGKSTLL---FAFLrlLNTEGDIQIDGVSWNTVSVQqwRKAFGVIPQKVFIFSG-TFRMNLD- 1290
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLnliAGFE--TPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAHlTVEQNVGl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1291 ---PYGQWNDEE---IWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSRAKILLLDEPSAHLDPV 1364
Cdd:cd03298 94 glsPGLKLTAEDrqaIEVALARVGLAGLEKRLPGEL-----------SGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1631900066 1365 TSQVIRKTLK--HAFANCTVILSEHRLEAMLECQRFLVIEDN 1404
Cdd:cd03298 163 LRAEMLDLVLdlHAETKMTVLMVTHQPEDAKRLAQRVVFLDN 204
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1208-1403 |
1.97e-10 |
|
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: 62.35 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1208 GAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLrllnteGDIQ-IDG-VSWNTV---------SVQQWRKAFGVIPQ 1276
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAIL------GEMQtLEGkVHWSNKnesepsfeaTRSRNRYSVAYAAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1277 KVFIFSGTFRMNLDPYGQWNDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSRAKILLLDE 1356
Cdd:cd03290 87 KPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1631900066 1357 P-SA---HL-DPVTSQVIRKTLKHafANCTVILSEHRLEAMLECQRFLVIED 1403
Cdd:cd03290 167 PfSAldiHLsDHLMQEGILKFLQD--DKRTLVLVTHKLQYLPHADWIIAMKD 216
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
845-1086 |
2.06e-10 |
|
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: 63.34 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 845 LIFVLILcvtvFLIEVAASLAGLWFLKKTAlkanatqsenstsdkpPVIVTDTSAYYIIYIYVGVADTLLAMGIFRGLPL 924
Cdd:cd07346 1 LLLALLL----LLLATALGLALPLLTKLLI----------------DDVIPAGDLSLLLWIALLLLLLALLRALLSYLRR 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 925 VHTLITVSKTLH---QKMVHAVLHAPMSTFNSWKAGGMLNRFAKDTAVLDDLLPLTVFDFVQLILIVIGAITVVSILQPY 1001
Cdd:cd07346 61 YLAARLGQRVVFdlrRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1002 IFLASVPVIAAFIVLRAYFLHTSQQLKQLESEARSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKAL------NLHTAN 1075
Cdd:cd07346 141 LTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANrdlrdaNLRAAR 220
|
250
....*....|.
gi 1631900066 1076 WFLYLSTLRWF 1086
Cdd:cd07346 221 LSALFSPLIGL 231
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
393-571 |
2.48e-10 |
|
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: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 393 VQANQENNNSKAPSTDNNLFFSNFPLHA---SPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGeLEPS-QGKIKH- 467
Cdd:COG4178 345 ADALPEAASRIETSEDGALALEDLTLRTpdgRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPYgSGRIARp 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 468 -SGRISFSPQVSWIMPGTIKENIIF---GVSYDEYRYKSVIKACQLEEDISKFPEKDytvlgEGGIILSGGQRARISLAR 543
Cdd:COG4178 424 aGARVLFLPQRPYLPLGTLREALLYpatAEAFSDAELREALEAVGLGHLAERLDEEA-----DWDQVLSLGEQQRLAFAR 498
|
170 180
....*....|....*....|....*...
gi 1631900066 544 AVYKDADLYLLDSPFGHLDIFTEKEIFE 571
Cdd:COG4178 499 LLLHKPDWLFLDEATSALDEENEAALYQ 526
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
424-598 |
2.62e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 62.49 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 424 LQDINFRIEKGQLLAVSGSTGAGKTSLLMMI--MGELEPS---QGKIKHSGRISFSPQVSWI---------------MPG 483
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIYSPRTDTVdlrkeigmvfqqpnpFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 484 TIKENIIFGVS---------YDEYRYKSVIKACQLEEdiskfpEKDYtvLGEGGIILSGGQRARISLARAVYKDADLYLL 554
Cdd:PRK14239 101 SIYENVVYGLRlkgikdkqvLDEAVEKSLKGASIWDE------VKDR--LHDSALGLSGGQQQRVCIARVLATSPKIILL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1631900066 555 DSPFGHLDIFTEKEIfESCVCKLMANKTRILVTSKLEHL-KIADK 598
Cdd:PRK14239 173 DEPTSALDPISAGKI-EETLLGLKDDYTMLLVTRSMQQAsRISDR 216
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1208-1407 |
2.88e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 62.70 E-value: 2.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1208 GAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLNTE-GDIQIDGVSWNTVS-VQQWRKAFGVI---PQKVFIfS 1282
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQkGKVLVSGIDTGDFSkLQGIRKLVGIVfqnPETQFV-G 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1283 GTFRMNLdPYGQWN----DEEIWKVAE----EVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSRAKILLL 1354
Cdd:PRK13644 93 RTVEEDL-AFGPENlclpPIEIRKRVDralaEIGLEKYRHRSPKT-----------LSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1631900066 1355 DEPSAHLDPVTSQ-VIRKTLKHAFANCTVILSEHRLEAMLECQRFLVIEDNKLR 1407
Cdd:PRK13644 161 DEVTSMLDPDSGIaVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIV 214
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
424-562 |
3.45e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 61.81 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 424 LQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGR-IS---------FSPQVSWI-------MPGTIK 486
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHdITrlknrevpfLRRQIGMIfqdhhllMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 487 EN-----IIFGVSYDEYRYK--SVIKACQLEEDISKFPekdytvlgeggIILSGGQRARISLARAVYKDADLYLLDSPFG 559
Cdd:PRK10908 98 DNvaiplIIAGASGDDIRRRvsAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
...
gi 1631900066 560 HLD 562
Cdd:PRK10908 167 NLD 169
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
418-605 |
3.54e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 64.27 E-value: 3.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 418 LHASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGR-ISF-SPQVSW---------------- 479
Cdd:COG1129 262 LSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpVRIrSPRDAIragiayvpedrkgegl 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 480 IMPGTIKENIIFgVSYDEYRYKSVIKAcQLEEDIS---------KFPEKDYTVLGeggiiLSGGQRARISLARAVYKDAD 550
Cdd:COG1129 342 VLDLSIRENITL-ASLDRLSRGGLLDR-RRERALAeeyikrlriKTPSPEQPVGN-----LSGGNQQKVVLAKWLATDPK 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 551 LYLLDSPFGHLDIFTEKEIFescvcKLMANKTR-----ILVTSKL-EHLKIADKILILHEG 605
Cdd:COG1129 415 VLILDEPTRGIDVGAKAEIY-----RLIRELAAegkavIVISSELpELLGLSDRILVMREG 470
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
423-616 |
3.77e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 64.44 E-value: 3.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 423 VLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMG--ELEPSQGKIKHsgRISFSPQVSWIMP------------------ 482
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIY--HVALCEKCGYVERpskvgepcpvcggtlepe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 483 --------------------------------GTIKENII-----FGVSYDEYRYKSV--IKACQLEEDISKFPEKdytv 523
Cdd:TIGR03269 93 evdfwnlsdklrrrirkriaimlqrtfalygdDTVLDNVLealeeIGYEGKEAVGRAVdlIEMVQLSHRITHIARD---- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 524 lgeggiiLSGGQRARISLARAVYKDADLYLLDSPFGHLDIFTEKEIFESCVCKLMANKTRILVTSKLEHL--KIADKILI 601
Cdd:TIGR03269 169 -------LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVieDLSDKAIW 241
|
250
....*....|....*
gi 1631900066 602 LHEGSCYFYGTFSEL 616
Cdd:TIGR03269 242 LENGEIKEEGTPDEV 256
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1195-1362 |
3.86e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 63.70 E-value: 3.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTAKYgEGGAAVlENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLN-----TEGDIQIDGVswNTVSVQQWRK 1269
Cdd:PRK11607 20 LEIRNLTKSF-DGQHAV-DDVSLTIYKGEIFALLGASGCGKSTL----LRMLAgfeqpTAGQIMLDGV--DLSHVPPYQR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1270 AFGVIPQKVFIFSG-TFRMNLdPYGQWNDE----EI-WKVAEEVGLKSVIE---QFPGQldfvlvdggcvLSHGHKQLMC 1340
Cdd:PRK11607 92 PINMMFQSYALFPHmTVEQNI-AFGLKQDKlpkaEIaSRVNEMLGLVHMQEfakRKPHQ-----------LSGGQRQRVA 159
|
170 180
....*....|....*....|..
gi 1631900066 1341 LARSVLSRAKILLLDEPSAHLD 1362
Cdd:PRK11607 160 LARSLAKRPKLLLLDEPMGALD 181
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1194-1406 |
4.11e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 62.80 E-value: 4.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1194 KMTVKDLTAKYGEGGAA---VLENISFSIDSGQRVGLLGRTGSGKSTL---LFAFLrlLNTEGDIQI-----------DG 1256
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPTelkALDNVSVEINQGEFIAIIGQTGSGKTTFiehLNALL--LPDTGTIEWifkdeknkkktKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1257 VSWNTVS-------------VQQWRKAFGVIPQ------------KVFIFsGTFRMNLDPygqwndEEIWKVAEE----V 1307
Cdd:PRK13651 80 KEKVLEKlviqktrfkkikkIKEIRRRVGVVFQfaeyqlfeqtieKDIIF-GPVSMGVSK------EEAKKRAAKyielV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1308 GL-KSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFANC-TVILS 1385
Cdd:PRK13651 153 GLdESYLQRSPFEL-----------SGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGkTIILV 221
|
250 260
....*....|....*....|..
gi 1631900066 1386 EHRLEAMLE-CQRFLVIEDNKL 1406
Cdd:PRK13651 222 THDLDNVLEwTKRTIFFKDGKI 243
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1197-1389 |
4.49e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 61.98 E-value: 4.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKYGEggAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLNTEGDIQIDG--------VSWNTVSVQQWR 1268
Cdd:PRK14258 10 VNNLSFYYDT--QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGrveffnqnIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1269 KAFGVIPQKVFIFSGTFRMNLdPYG----QWN--------------DEEIWKVAEEVGLKSVIEqfpgqldfvlvdggcv 1330
Cdd:PRK14258 88 RQVSMVHPKPNLFPMSVYDNV-AYGvkivGWRpkleiddivesalkDADLWDEIKHKIHKSALD---------------- 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 1331 LSHGHKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAF--ANCTVILSEHRL 1389
Cdd:PRK14258 151 LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNL 211
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1212-1424 |
4.61e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 62.80 E-value: 4.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1212 LENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVswntVSVQQwRKAF----GVipqkVFifsG--- 1283
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVpTSGEVRVLGY----VPFKR-RKEFarriGV----VF---Gqrs 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1284 ----------TFRMNLDPYGQwnDEEIWK-----VAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSR 1348
Cdd:COG4586 106 qlwwdlpaidSFRLLKAIYRI--PDAEYKkrldeLVELLDLGELLDTPVRQ-----------LSLGQRMRCELAAALLHR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1349 AKILLLDEPSAHLDPVTSQVIRKTLK--HAFANCTVILSEHRL---EAMleCQRFLVIEDNKLRQYESIQKLLNEKSSFR 1423
Cdd:COG4586 173 PKILFLDEPTIGLDVVSKEAIREFLKeyNRERGTTILLTSHDMddiEAL--CDRVIVIDHGRIIYDGSLEELKERFGPYK 250
|
.
gi 1631900066 1424 Q 1424
Cdd:COG4586 251 T 251
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
423-563 |
4.66e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 61.67 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 423 VLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG--RISFSPQ-----------VSWIM---PGTIK 486
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGklRIGYVPQklyldttlpltVNRFLrlrPGTKK 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1631900066 487 ENIIFGVsydeyryKSVIKACQLEEDISKfpekdytvlgeggiiLSGGQRARISLARAVYKDADLYLLDSPFGHLDI 563
Cdd:PRK09544 99 EDILPAL-------KRVQAGHLIDAPMQK---------------LSGGETQRVLLARALLNRPQLLVLDEPTQGVDV 153
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
423-605 |
4.87e-10 |
|
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: 61.01 E-value: 4.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 423 VLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGRISFSPQVSWI------------------MpgT 484
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINelrqkvgmvfqqfnlfphL--T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 485 IKENIIF------GVSYDEYRYKS--VIKACQLEEDISKFPEKdytvlgeggiiLSGGQRARISLARAVYKDADLYLLDS 556
Cdd:cd03262 93 VLENITLapikvkGMSKAEAEERAleLLEKVGLADKADAYPAQ-----------LSGGQQQRVAIARALAMNPKVMLFDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1631900066 557 PFGHLDIFTEKEIFEscVCKLMA--NKTRILVTskleH-----LKIADKILILHEG 605
Cdd:cd03262 162 PTSALDPELVGEVLD--VMKDLAeeGMTMVVVT----HemgfaREVADRVIFMDDG 211
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1190-1408 |
4.93e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 61.33 E-value: 4.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1190 PSGGKMTVKDLTAKYGEGGA--AVLENISFSIDSGQRVGLLGRTGSGKSTLLfAFLRLLN--TEGDIQIDGVSWNTVSVQ 1265
Cdd:PRK10584 2 PAENIVEVHHLKKSVGQGEHelSILTGVELVVKRGETIALIGESGSGKSTLL-AILAGLDdgSSGEVSLVGQPLHQMDEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1266 QWRK-----------AFGVIP----QKVFIFSGTFRMNLDpyGQWNDEEIwKVAEEVGLKSVIEQFPGQLdfvlvdggcv 1330
Cdd:PRK10584 81 ARAKlrakhvgfvfqSFMLIPtlnaLENVELPALLRGESS--RQSRNGAK-ALLEQLGLGKRLDHLPAQL---------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1331 lSHGHKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRK---TLKHAFANcTVILSEHRLEAMLECQRFLVIEDNKLR 1407
Cdd:PRK10584 148 -SGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADllfSLNREHGT-TLILVTHDLQLAARCDRRLRLVNGQLQ 225
|
.
gi 1631900066 1408 Q 1408
Cdd:PRK10584 226 E 226
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
431-631 |
5.25e-10 |
|
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: 60.28 E-value: 5.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 431 IEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG-RISFSPQVswimpgtikeniifgvsydeyryksvikacql 509
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGiTPVYKPQY-------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 510 eediskfpekdytvlgeggIILSGGQRARISLARAVYKDADLYLLDSPFGHLDIftEKEIFESCVCKLM---ANKTRILV 586
Cdd:cd03222 70 -------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDI--EQRLNAARAIRRLseeGKKTALVV 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1631900066 587 TSKLEHLKIADKILILHEGSCYFYGTFSELQGQRPDFSSELMGFD 631
Cdd:cd03222 129 EHDLAVLDYLSDRIHVFEGEPGVYGIASQPKGTREGINRFLRGYL 173
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
422-605 |
6.17e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.48 E-value: 6.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGR--ISFSPQ------VSWIMPGTIKENIIFGV 493
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHevVTRSPQdglangIVYISEDRKRDGLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 494 SYDE------YRYKSViKACQL---EEDIS----------KFPEKDYTVlGEggiiLSGGQRARISLARAVYKDADLYLL 554
Cdd:PRK10762 346 SVKEnmsltaLRYFSR-AGGSLkhaDEQQAvsdfirlfniKTPSMEQAI-GL----LSGGNQQKVAIARGLMTRPKVLIL 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1631900066 555 DSPFGHLDIFTEKEIFEscvcklMANKTR------ILVTSKL-EHLKIADKILILHEG 605
Cdd:PRK10762 420 DEPTRGVDVGAKKEIYQ------LINQFKaeglsiILVSSEMpEVLGMSDRILVMHEG 471
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
416-612 |
6.35e-10 |
|
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: 64.26 E-value: 6.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 416 FPLHASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGR------------ISFSPQVSWIMPG 483
Cdd:TIGR01257 938 FEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdietnldavrqsLGMCPQHNILFHH 1017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 484 -TIKENIIFgvsYDEYRYKSVIKAcQLE-----EDISKFPEKDytvlgEGGIILSGGQRARISLARAVYKDADLYLLDSP 557
Cdd:TIGR01257 1018 lTVAEHILF---YAQLKGRSWEEA-QLEmeamlEDTGLHHKRN-----EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1631900066 558 FGHLDIFTEKEIFEsCVCKLMANKTRILVTSKLEHLKI-ADKILILHEGSCYFYGT 612
Cdd:TIGR01257 1089 TSGVDPYSRRSIWD-LLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGT 1143
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1207-1387 |
7.70e-10 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 60.20 E-value: 7.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1207 GGAAVLENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLN-----TEGDiqidgVSWNTVSVQQWRKAFgvipQKVFIF 1281
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTL----LRILAglsppLAGR-----VLLNGGPLDFQRDSI----ARGLLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1282 SG---------TFRMNLDPYGQWN-DEEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSRAKI 1351
Cdd:cd03231 78 LGhapgikttlSVLENLRFWHADHsDEQVEEALARVGLNGFEDRPVAQ-----------LSAGQQRRVALARLLLSGRPL 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 1631900066 1352 LLLDEPSAHLDPVTSQVIRKTLK-HAFANCTVILSEH 1387
Cdd:cd03231 147 WILDEPTTALDKAGVARFAEAMAgHCARGGMVVLTTH 183
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1207-1369 |
8.09e-10 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 60.80 E-value: 8.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1207 GGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLfaflRLLN-----TEGDIQIDGVSW------NTVSVQQWRKAFGVIP 1275
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKSSLL----RVLNlletpDSGQLNIAGHQFdfsqkpSEKAIRLLRQKVGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1276 QKvfifsgtfrMNLDPY---------------GQWNDEEIWKVAE---EVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQ 1337
Cdd:COG4161 89 QQ---------YNLWPHltvmenlieapckvlGLSKEQAREKAMKllaRLRLTDKADRFPLHL-----------SGGQQQ 148
|
170 180 190
....*....|....*....|....*....|...
gi 1631900066 1338 LMCLARSVLSRAKILLLDEPSAHLDP-VTSQVI 1369
Cdd:COG4161 149 RVAIARALMMEPQVLLFDEPTAALDPeITAQVV 181
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1212-1421 |
8.46e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 62.74 E-value: 8.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1212 LENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSVQQWR-----------KAFGVIPQKVF 1279
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEpTRGQVLIDGVDIAKISDAELRevrrkkiamvfQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1280 IFSGTFRMNLDPY-GQWNDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSRAKILLLDEPS 1358
Cdd:PRK10070 124 LDNTAFGMELAGInAEERREKALDALRQVGLENYAHSYPDEL-----------SGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1631900066 1359 AHLDPV-----TSQVIRKTLKHafaNCTVILSEHRL-EAMLECQRFLVIEDNKLRQYESIQKLLNEKSS 1421
Cdd:PRK10070 193 SALDPLirtemQDELVKLQAKH---QRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAN 258
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1198-1390 |
8.72e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 61.34 E-value: 8.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1198 KDLTAKYGEGGAavLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRL------LNTEGDIQIDGVSWNTVSVQ--QWRK 1269
Cdd:PRK14243 14 ENLNVYYGSFLA--VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndlipgFRVEGKVTFHGKNLYAPDVDpvEVRR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1270 AFGVIPQKVFIFSGTFRMNLdPYG------QWNDEEIWKVA-------EEVGLKsvieqfpgqldfvLVDGGCVLSHGHK 1336
Cdd:PRK14243 92 RIGMVFQKPNPFPKSIYDNI-AYGaringyKGDMDELVERSlrqaalwDEVKDK-------------LKQSGLSLSGGQQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1631900066 1337 QLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFANCTVILSEHRLE 1390
Cdd:PRK14243 158 QRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQ 211
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
423-616 |
8.93e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 61.25 E-value: 8.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 423 VLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGR-----------------ISFSPQVSWIMPGTI 485
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikydkksllevrktvgIVFQNPDDQLFAPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 486 KENIIFG-----VSYDEY--RYKSVIKACQLEEDISKFPEKdytvlgeggiiLSGGQRARISLARAVYKDADLYLLDSPF 558
Cdd:PRK13639 97 EEDVAFGplnlgLSKEEVekRVKEALKAVGMEGFENKPPHH-----------LSGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1631900066 559 GHLDiftekEIFESCVCKLMA--NK---TRILVTSKLEHLKI-ADKILILHEGSCYFYGTFSEL 616
Cdd:PRK13639 166 SGLD-----PMGASQIMKLLYdlNKegiTIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEV 224
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1190-1259 |
8.93e-10 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 60.62 E-value: 8.93e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1631900066 1190 PSGGKMTVKDLTAKYGEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLN-----TEGDIQIDG-VSW 1259
Cdd:cd03220 16 GSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTL----LRLLAgiyppDSGTVTVRGrVSS 87
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1212-1419 |
9.48e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 61.18 E-value: 9.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1212 LENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN----TEGDIQIDGvswNTVS--------VQQWRKAFGVIPQK-- 1277
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksAGSHIELLG---RTVQregrlardIRKSRANTGYIFQQfn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1278 ----------VFIFS-GT---FRMNLDPYGQWNDEEIWKVAEEVGLKSVIEQFPGqldfvlvdggcVLSHGHKQLMCLAR 1343
Cdd:PRK09984 97 lvnrlsvlenVLIGAlGStpfWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVS-----------TLSGGQQQRVAIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1631900066 1344 SVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFAN--CTVILSEHRLE-AMLECQRFLVIEDNKLRQYESIQKLLNEK 1419
Cdd:PRK09984 166 ALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFDNER 244
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1195-1363 |
1.14e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 60.53 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTAKYGegGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAfLRLLNTE-------GDIQIDGvswnTVSVQQW 1267
Cdd:PRK11264 4 IEVKNLVKKFH--GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRC-INLLEQPeagtirvGDITIDT----ARSLSQQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1268 RKAFGVIPQKV-FIFSGtfrMNLDPY---------------GQWNDEEIWKVAE---EVGLKSVIEQFPGQldfvlvdgg 1328
Cdd:PRK11264 77 KGLIRQLRQHVgFVFQN---FNLFPHrtvleniiegpvivkGEPKEEATARAREllaKVGLAGKETSYPRR--------- 144
|
170 180 190
....*....|....*....|....*....|....*
gi 1631900066 1329 cvLSHGHKQLMCLARSVLSRAKILLLDEPSAHLDP 1363
Cdd:PRK11264 145 --LSGGQQQRVAIARALAMRPEVILFDEPTSALDP 177
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
424-612 |
1.14e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 60.92 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 424 LQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKI----------------KHSGrISFSPQVSWIMPGTIKE 487
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitddnfeklrKHIG-IVFQNPDNQFVGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 488 NIIFG-----VSYDEyrYKSVIKacQLEEDISKFPEKDYTVLGeggiiLSGGQRARISLARAVYKDADLYLLDSPFGHLD 562
Cdd:PRK13648 104 DVAFGlenhaVPYDE--MHRRVS--EALKQVDMLERADYEPNA-----LSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1631900066 563 IFTEKEIFeSCVCKLMANK--TRILVTSKLEHLKIADKILILHEGSCYFYGT 612
Cdd:PRK13648 175 PDARQNLL-DLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGT 225
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1208-1388 |
1.19e-09 |
|
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: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1208 GAAVLENISFSIDSGQRVGLLGRTGSGKSTLLfaflRLLN-----TEGDIQIDGVSwntvsvqqwRKAFgvIPQKVFIFS 1282
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLF----RALAglwpwGSGRIGMPEGE---------DLLF--LPQRPYLPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1283 GTFRmnldpyGQ----WNDeeiwkvaeevglksvieqfpgqldfvlvdggcVLSHGHKQLMCLARSVLSRAKILLLDEPS 1358
Cdd:cd03223 78 GTLR------EQliypWDD--------------------------------VLSGGEQQRLAFARLLLHKPKFVFLDEAT 119
|
170 180 190
....*....|....*....|....*....|
gi 1631900066 1359 AHLDPVTSQVIRKTLKHAFAncTVILSEHR 1388
Cdd:cd03223 120 SALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1198-1404 |
1.39e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 60.97 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1198 KDLTAKYgEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSVQQWRKAFGVIPQ 1276
Cdd:PRK13652 7 RDLCYSY-SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKpTSGSVLIRGEPITKENIREVRKFVGLVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1277 KV--FIFSGTFRMNLdPYGQWN---DEE-----IWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVL 1346
Cdd:PRK13652 86 NPddQIFSPTVEQDI-AFGPINlglDEEtvahrVSSALHMLGLEELRDRVPHH-----------LSGGEKKRVAIAGVIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1631900066 1347 SRAKILLLDEPSAHLDPvtsQVIRKTLkhAFAN-------CTVILSEHRLEAMLECQRFLVIEDN 1404
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDP---QGVKELI--DFLNdlpetygMTVIFSTHQLDLVPEMADYIYVMDK 213
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
407-573 |
1.51e-09 |
|
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: 62.46 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 407 TDNNLFFSNFPLhASP----VLQDINFRIEKGQLLAVSGSTGAGKTSLLmMIMGELEPSQG---KIKHSGRISFSPQVSW 479
Cdd:TIGR00954 448 QDNGIKFENIPL-VTPngdvLIESLSFEVPSGNNLLICGPNGCGKSSLF-RILGELWPVYGgrlTKPAKGKLFYVPQRPY 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 480 IMPGTIKENIIFGVSYDEYRYKSVIKAcQLEEdISKFPEKDYTVLGEGGI--------ILSGGQRARISLARAVYKDADL 551
Cdd:TIGR00954 526 MTLGTLRDQIIYPDSSEDMKRRGLSDK-DLEQ-ILDNVQLTHILEREGGWsavqdwmdVLSGGEKQRIAMARLFYHKPQF 603
|
170 180
....*....|....*....|..
gi 1631900066 552 YLLDSPFGHLDIFTEKEIFESC 573
Cdd:TIGR00954 604 AILDECTSAVSVDVEGYMYRLC 625
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
80-285 |
1.69e-09 |
|
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: 60.64 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 80 VQPLLLGRIIASYDPDnsDERSIAYYLGIGLCLLFLVRTLLIHPAIFGLHHIGMQMRIAMFSLIYKKILKLSSRVLDKIS 159
Cdd:cd07346 17 ALPLLTKLLIDDVIPA--GDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 160 TGQLVSLLSNNLNKFDEGLALAHFVWIAplQVALLMGLLWDMLEAS---AFSGLAFLIVLAFFQAWLGQMMMKY---RNK 233
Cdd:cd07346 95 TGDLMSRLTSDVDAVQNLVSSGLLQLLS--DVLTLIGALVILFYLNwklTLVALLLLPLYVLILRYFRRRIRKAsreVRE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1631900066 234 RAGKINERLVitsEIIENIQSVKAYCWEDAMEKMIESIRETELKLTRKAAYV 285
Cdd:cd07346 173 SLAELSAFLQ---ESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARL 221
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
423-605 |
1.77e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 60.24 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 423 VLQDINFRIEKGQLLAVSGSTGAGKTSLL-----MMIMGELEPSQGKIKHSGRISFSPQVSWI-----------MPG--- 483
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLrtfnrLLELNEEARVEGEVRLFGRNIYSPDVDPIevrrevgmvfqYPNpfp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 484 --TIKENIIFGVSYD---------EYRYKSVIKACQLEEDIsKFPEKDYTVLgeggiiLSGGQRARISLARAVYKDADLY 552
Cdd:PRK14267 99 hlTIYDNVAIGVKLNglvkskkelDERVEWALKKAALWDEV-KDRLNDYPSN------LSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1631900066 553 LLDSPFGHLDIFTEKEIfESCVCKLMANKTRILVT-SKLEHLKIADKILILHEG 605
Cdd:PRK14267 172 LMDEPTANIDPVGTAKI-EELLFELKKEYTIVLVThSPAQAARVSDYVAFLYLG 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
409-603 |
1.91e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 60.05 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 409 NNLFFSnfpLHASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMI--MGELEpsqGKIKHSGRISF------------- 473
Cdd:PRK14258 11 NNLSFY---YDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrMNELE---SEVRVEGRVEFfnqniyerrvnln 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 474 --SPQVSWIMPG------TIKENIIFGVSYDEYRYK--------SVIKACQLEEDISKfpekdytVLGEGGIILSGGQRA 537
Cdd:PRK14258 85 rlRRQVSMVHPKpnlfpmSVYDNVAYGVKIVGWRPKleiddiveSALKDADLWDEIKH-------KIHKSALDLSGGQQQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1631900066 538 RISLARAVYKDADLYLLDSPFGHLDIFTEKEIfESCV--CKLMANKTRILVTSKLEHL-KIADKILILH 603
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKV-ESLIqsLRLRSELTMVIVSHNLHQVsRLSDFTAFFK 225
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
424-611 |
1.92e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 60.52 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 424 LQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGRISFSPQVSWI---------------MPGTIKEN 488
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVrskvglvfqdpddqvFSSTVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 489 IIFG-----VSYDEY--RYKSVIKACQLEEDISKFPEKdytvlgeggiiLSGGQRARISLARAVYKDADLYLLDSPFGHL 561
Cdd:PRK13647 101 VAFGpvnmgLDKDEVerRVEEALKAVRMWDFRDKPPYH-----------LSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 562 DIFTEKEIFESCVCKLMANKTRILVTSKLE-HLKIADKILILHEGSCYFYG 611
Cdd:PRK13647 170 DPRGQETLMEILDRLHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEG 220
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
424-619 |
2.82e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 60.18 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 424 LQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG-----------------RISFSPQV--SWIMPGT 484
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirpvrkRIGMVFQFpeSQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 485 IKENIIFGVSYDEYRYKSV-IKACQLEEDISkFPEKdytVLGEGGIILSGGQRARISLARAVYKDADLYLLDSPFGHLDI 563
Cdd:PRK13646 103 VEREIIFGPKNFKMNLDEVkNYAHRLLMDLG-FSRD---VMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1631900066 564 FTEKEIFESC-VCKLMANKTRILVTSKLEHL-KIADKILILHEGSCYFYGTFSELQGQ 619
Cdd:PRK13646 179 QSKRQVMRLLkSLQTDENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
422-606 |
2.96e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.82 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHS-GRISFSPQVSWImpgtikENIifGVSYDEYRY 500
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDvPDNQFGREASLI------DAI--GRKGDFKDA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 501 KSVIKACQLEEDIS---KFPEkdytvlgeggiiLSGGQRARISLARAVYKDADLYLLDSPFGHLDIFTEKEIfESCVCKL 577
Cdd:COG2401 116 VELLNAVGLSDAVLwlrRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRV-ARNLQKL 182
|
170 180 190
....*....|....*....|....*....|...
gi 1631900066 578 M--ANKTRILVTSKLEHLK--IADKILILHEGS 606
Cdd:COG2401 183 ArrAGITLVVATHHYDVIDdlQPDLLIFVGYGG 215
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
424-598 |
3.02e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 59.41 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 424 LQDINFRIEKGQLLAVSGSTGAGKTSLLMMI--MGELEPS---QGKIKHSGRISFSPQVSWI---------------MPG 483
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGfrvEGKVTFHGKNLYAPDVDPVevrrrigmvfqkpnpFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 484 TIKENIIFGV-------SYDEYRYKSVIKACQLEEDISKfpekdytvLGEGGIILSGGQRARISLARAVYKDADLYLLDS 556
Cdd:PRK14243 106 SIYDNIAYGAringykgDMDELVERSLRQAALWDEVKDK--------LKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1631900066 557 PFGHLDIFTEKEIfESCVCKLMANKTRILVTSKLEHL-KIADK 598
Cdd:PRK14243 178 PCSALDPISTLRI-EELMHELKEQYTIIIVTHNMQQAaRVSDM 219
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
422-615 |
3.26e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.41 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVL-QDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGRISFSpqvswimpgtikeniIFGVSYDEYRY 500
Cdd:PLN03073 522 PLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMA---------------VFSQHHVDGLD 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 501 KSVIKACQLEEDISKFPEKDYTV-LGEGGI----------ILSGGQRARISLARAVYKDADLYLLDSPFGHLDIftekEI 569
Cdd:PLN03073 587 LSSNPLLYMMRCFPGVPEQKLRAhLGSFGVtgnlalqpmyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDL----DA 662
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1631900066 570 FESCVCKLMANKTRILVTSKLEHL--KIADKILILHEGSCY-FYGTFSE 615
Cdd:PLN03073 663 VEALIQGLVLFQGGVLMVSHDEHLisGSVDELWVVSEGKVTpFHGTFHD 711
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
423-562 |
3.87e-09 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 58.27 E-value: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 423 VLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIK------HSGRISFSPQVSWI--MPG-----TIKENI 489
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLlnggplDFQRDSIARGLLYLghAPGikttlSVLENL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1631900066 490 IFgvsydeyrYKSVIKACQLEEDISkfpekDYTVLGEGGII---LSGGQRARISLARAVYKDADLYLLDSPFGHLD 562
Cdd:cd03231 95 RF--------WHADHSDEQVEEALA-----RVGLNGFEDRPvaqLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1195-1401 |
4.39e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 59.34 E-value: 4.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTAKY-GEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLNT-----EGDIQIDGVSWNTVSVQQWR 1268
Cdd:PRK13642 5 LEVENLVFKYeKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTT----ARLIDGlfeefEGKVKIDGELLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1269 KAFGVI---PQKVFIfsGTFRMNLDPYGQWND----EEIWKVAEEVGLKSvieqfpGQLDFVLVDGGcVLSHGHKQLMCL 1341
Cdd:PRK13642 81 RKIGMVfqnPDNQFV--GATVEDDVAFGMENQgiprEEMIKRVDEALLAV------NMLDFKTREPA-RLSGGQKQRVAV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1631900066 1342 ARSVLSRAKILLLDEPSAHLDPV-TSQVIR--KTLKHAFaNCTVILSEHRLEAMLECQRFLVI 1401
Cdd:PRK13642 152 AGIIALRPEIIILDESTSMLDPTgRQEIMRviHEIKEKY-QLTVLSITHDLDEAASSDRILVM 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1207-1422 |
5.36e-09 |
|
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: 58.40 E-value: 5.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1207 GGAAVLENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLN-----TEGDIQIDGVSWNTVSVQqwRKAFGVIPQKVFIF 1281
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTL----LRLIAgfetpTSGEILLDGKDITNLPPH--KRPVNTVFQNYALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1282 SgtfRMNLD---PYG----QWNDEEIWKVAEE----VGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSRAK 1350
Cdd:cd03300 85 P---HLTVFeniAFGlrlkKLPKAEIKERVAEaldlVQLEGYANRKPSQ-----------LSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1631900066 1351 ILLLDEPSAHLDPVTSQVIRKTLK--HAFANCTVILSEH-RLEAMLECQRFLVIEDNKLRQYESIQKLLNE-KSSF 1422
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKrlQKELGITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEpANRF 226
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1197-1369 |
5.63e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 58.49 E-value: 5.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKYGEGGAavLENISFSIDSGQRVGLLGRTGSGKSTLLfaflRLLN-----TEGDIQIDGVSWNtVSVQQWRKAF 1271
Cdd:PRK11124 5 LNGINCFYGAHQA--LFDITLDCPQGETLVLLGPSGAGKSSLL----RVLNllempRSGTLNIAGNHFD-FSKTPSDKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1272 GVIPQKVfifsgtfRMNLDPYGQW-------------------NDEEIWKVAEEV----GLKSVIEQFPGQLdfvlvdgg 1328
Cdd:PRK11124 78 RELRRNV-------GMVFQQYNLWphltvqqnlieapcrvlglSKDQALARAEKLlerlRLKPYADRFPLHL-------- 142
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1631900066 1329 cvlSHGHKQLMCLARSVLSRAKILLLDEPSAHLDP-VTSQVI 1369
Cdd:PRK11124 143 ---SGGQQQRVAIARALMMEPQVLLFDEPTAALDPeITAQIV 181
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1195-1365 |
5.74e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 58.56 E-value: 5.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTAKYGegGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLNTE-GDIQIDGVSWN------TVSVQQw 1267
Cdd:PRK11248 2 LQISHLYADYG--GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQhGSITLDGKPVEgpgaerGVVFQN- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1268 rkaFGVIPQKVFIFSGTFRMNLDPYGQWNDEEiwkVAEE----VGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLAR 1343
Cdd:PRK11248 79 ---EGLLPWRNVQDNVAFGLQLAGVEKMQRLE---IAHQmlkkVGLEGAEKRYIWQ-----------LSGGQRQRVGIAR 141
|
170 180
....*....|....*....|..
gi 1631900066 1344 SVLSRAKILLLDEPSAHLDPVT 1365
Cdd:PRK11248 142 ALAANPQLLLLDEPFGALDAFT 163
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
427-605 |
5.88e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 60.59 E-value: 5.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 427 INFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKI----------------KHSGR----ISFSPQVSWIMP-GTI 485
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmtkpgpDGRGRakryIGILHQEYDLYPhRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 486 KENIIFGVSY---DEY-RYKSVI--KACQLEED-----ISKFPEKdytvlgeggiiLSGGQRARISLARAVYKDADLYLL 554
Cdd:TIGR03269 383 LDNLTEAIGLelpDELaRMKAVItlKMVGFDEEkaeeiLDKYPDE-----------LSEGERHRVALAQVLIKEPRIVIL 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1631900066 555 DSPFGHLDIFTEKEIFESCV-CKLMANKTRILVTSKLEH-LKIADKILILHEG 605
Cdd:TIGR03269 452 DEPTGTMDPITKVDVTHSILkAREEMEQTFIIVSHDMDFvLDVCDRAALMRDG 504
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1196-1396 |
6.05e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 57.58 E-value: 6.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1196 TVKDLTAKygEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSvqqwrkafgVI 1274
Cdd:PRK13539 4 EGEDLACV--RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPpAAGTIKLDGGDIDDPD---------VA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1275 PQKVFIfsG---------TFRMNL----DPYGQwNDEEIWKVAEEVGLkSVIEQFPGQldfvlvdggcVLSHGHKQLMCL 1341
Cdd:PRK13539 73 EACHYL--GhrnamkpalTVAENLefwaAFLGG-EELDIAAALEAVGL-APLAHLPFG----------YLSAGQKRRVAL 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1342 ARSVLSRAKILLLDEPSAHLDpVTSQ-----VIRktlKHAFANCTVILSEHRLEAMLECQ 1396
Cdd:PRK13539 139 ARLLVSNRPIWILDEPTAALD-AAAValfaeLIR---AHLAQGGIVIAATHIPLGLPGAR 194
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1204-1362 |
6.21e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 58.19 E-value: 6.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1204 YGEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSVQQWRKAFGVIPQKVFIFS 1282
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISpTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1283 GTFRMNLD-PYgqwndeEIWKVA-EEVGLKSVIEQFpGQLDFVLVDGGCVLSHGHKQLMCLARSVLSRAKILLLDEPSAH 1360
Cdd:PRK10247 95 DTVYDNLIfPW------QIRNQQpDPAIFLDDLERF-ALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSA 167
|
..
gi 1631900066 1361 LD 1362
Cdd:PRK10247 168 LD 169
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
418-606 |
6.32e-09 |
|
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: 57.54 E-value: 6.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 418 LHAS----PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMG--ELEPSQGKIKHSGR--ISFSPQ--------VSWIM 481
Cdd:cd03217 6 LHVSvggkEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEdiTDLPPEerarlgifLAFQY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 482 PGTIKeniifGVSYDEY-RYksvikacqleediskfpekdytvLGEGgiiLSGGQRARISLARAVYKDADLYLLDSPFGH 560
Cdd:cd03217 86 PPEIP-----GVKNADFlRY-----------------------VNEG---FSGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1631900066 561 LDIFTEKEIFEScVCKLMANKTRILVTSKLEHL---KIADKILILHEGS 606
Cdd:cd03217 135 LDIDALRLVAEV-INKLREEGKSVLIITHYQRLldyIKPDRVHVLYDGR 182
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
424-627 |
6.35e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 60.45 E-value: 6.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 424 LQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPS---QGKIKHSG---------RIS-FSPQVSWIMPG-TIKENI 489
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGmpidakemrAISaYVQQDDLFIPTlTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 490 IFG--VSYDEYRYKSVIKAC--QLEEDISKFPEKDyTVLGEGGII--LSGGQRARISLARAVYKDADLYLLDSPFGHLDI 563
Cdd:TIGR00955 121 MFQahLRMPRRVTKKEKRERvdEVLQALGLRKCAN-TRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 564 FTEKEIFEscVCKLMANKTRILV------TSKLEHLkiADKILILHEGSCYFYGTFSELqgqrPDFSSEL 627
Cdd:TIGR00955 200 FMAYSVVQ--VLKGLAQKGKTIIctihqpSSELFEL--FDKIILMAEGRVAYLGSPDQA----VPFFSDL 261
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
410-605 |
7.67e-09 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 58.12 E-value: 7.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 410 NLFFSNFPlhaspVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMI--MGELEPSQgkiKHSGRISF------SPQVSWI- 480
Cdd:COG1117 18 NVYYGDKQ-----ALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLIPGA---RVEGEILLdgediyDPDVDVVe 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 481 ------M--------PGTIKENIIFGVSYDEYRYKSVI--------KACQLEEDIskfpeKDytVLGEGGIILSGGQRAR 538
Cdd:COG1117 90 lrrrvgMvfqkpnpfPKSIYDNVAYGLRLHGIKSKSELdeiveeslRKAALWDEV-----KD--RLKKSALGLSGGQQQR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1631900066 539 ISLARAVYKDADLYLLDSPFGHLD-IFTEKeifescVCKLMA----NKTRILVTskleH-----LKIADKILILHEG 605
Cdd:COG1117 163 LCIARALAVEPEVLLMDEPTSALDpISTAK------IEELILelkkDYTIVIVT----HnmqqaARVSDYTAFFYLG 229
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1213-1387 |
7.94e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 57.12 E-value: 7.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1213 ENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLN-----TEGDiqidgVSWNTVSVQQWRKAF-----------GVIPQ 1276
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSL----LRILAglarpDAGE-----VLWQGEPIRRQRDEYhqdllylghqpGIKTE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1277 KvfifsgTFRMNLDPY----GQWNDEEIWKVAEEVGLKsvieqfpGQLDfVLVDggcVLSHGHKQLMCLARSVLSRAKIL 1352
Cdd:PRK13538 89 L------TALENLRFYqrlhGPGDDEALWEALAQVGLA-------GFED-VPVR---QLSAGQQRRVALARLWLTRAPLW 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 1631900066 1353 LLDEPSAHLDPV-TSQVIRKTLKHAFANCTVILSEH 1387
Cdd:PRK13538 152 ILDEPFTAIDKQgVARLEALLAQHAEQGGMVILTTH 187
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1205-1406 |
8.69e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 60.12 E-value: 8.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1205 GEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLfAFLRLLN--TEGDIQIDGVSWNTVS----VQQWRKAFGVIPQKV 1278
Cdd:PRK10535 17 GEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLM-NILGCLDkpTSGTYRVAGQDVATLDadalAQLRREHFGFIFQRY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1279 FIFSG-TFRMNLD-P--YGQWNDEEIWKVAEEV----GLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSRAK 1350
Cdd:PRK10535 96 HLLSHlTAAQNVEvPavYAGLERKQRLLRAQELlqrlGLEDRVEYQPSQL-----------SGGQQQRVSIARALMNGGQ 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1631900066 1351 ILLLDEPSAHLDPVTSQVIRKTLK------HafancTVILSEHRLEAMLECQRFLVIEDNKL 1406
Cdd:PRK10535 165 VILADEPTGALDSHSGEEVMAILHqlrdrgH-----TVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1211-1388 |
8.80e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 57.27 E-value: 8.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1211 VLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLNTE-GDIQIDGVSwntvsVQQWRKAFgvipQKVFIFSGtFRMNL 1289
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEkGEILFERQS-----IKKDLCTY----QKQLCFVG-HRSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1290 DPYGQWNDE---EIWKVAEEVGLKSVIEQFpgQLDFvLVDGGC-VLSHGHKQLMCLARSVLSRAKILLLDEPSAHLDPVT 1365
Cdd:PRK13540 86 NPYLTLRENclyDIHFSPGAVGITELCRLF--SLEH-LIDYPCgLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
170 180
....*....|....*....|....
gi 1631900066 1366 SQVI-RKTLKHAFANCTVILSEHR 1388
Cdd:PRK13540 163 LLTIiTKIQEHRAKGGAVLLTSHQ 186
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1207-1403 |
8.87e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 59.65 E-value: 8.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1207 GGAAVLENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLN-----TEGDIQIDGVSWNTVSVQQWRKAfGV--IPQKV- 1278
Cdd:COG1129 15 GGVKALDGVSLELRPGEVHALLGENGAGKSTL----MKILSgvyqpDSGEILLDGEPVRFRSPRDAQAA-GIaiIHQELn 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1279 -F--------IFSGTFRMNldpYGQWNDEEIWKVAEEVgLKSVieqfpgQLDF---VLVDGgcvLSHGHKQLMCLARSVL 1346
Cdd:COG1129 90 lVpnlsvaenIFLGREPRR---GGLIDWRAMRRRAREL-LARL------GLDIdpdTPVGD---LSVAQQQLVEIARALS 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1631900066 1347 SRAKILLLDEPSAHLDPVTSQ----VIRKtLKHafANCTVILSEHRLEAMLE-CQRFLVIED 1403
Cdd:COG1129 157 RDARVLILDEPTASLTEREVErlfrIIRR-LKA--QGVAIIYISHRLDEVFEiADRVTVLRD 215
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1198-1362 |
9.63e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 58.96 E-value: 9.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1198 KDLTAKYGEggAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSVQQwrKAFGVIPQ 1276
Cdd:PRK11432 10 KNITKRFGS--NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKpTEGQIFIDGEDVTHRSIQQ--RDICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1277 KVFIFSgtfRMNLDP---YG----QWNDEEIWKVAEE----VGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSV 1345
Cdd:PRK11432 86 SYALFP---HMSLGEnvgYGlkmlGVPKEERKQRVKEalelVDLAGFEDRYVDQ-----------ISGGQQQRVALARAL 151
|
170
....*....|....*..
gi 1631900066 1346 LSRAKILLLDEPSAHLD 1362
Cdd:PRK11432 152 ILKPKVLLFDEPLSNLD 168
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1195-1389 |
1.01e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 57.82 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTAKYGEggAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQidgvswntvsvQQWRKAFGV 1273
Cdd:PRK09544 5 VSLENVSVSFGQ--RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVApDEGVIK-----------RNGKLRIGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1274 IPQKVFI-----FSGTFRMNLDPYGQwnDEEIWKVAEEVGLKSVIEQfPGQldfvlvdggcVLSHGHKQLMCLARSVLSR 1348
Cdd:PRK09544 72 VPQKLYLdttlpLTVNRFLRLRPGTK--KEDILPALKRVQAGHLIDA-PMQ----------KLSGGETQRVLLARALLNR 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1631900066 1349 AKILLLDEPSAHLDpVTSQV--------IRKTLkhafaNCTVILSEHRL 1389
Cdd:PRK09544 139 PQLLVLDEPTQGVD-VNGQValydlidqLRREL-----DCAVLMVSHDL 181
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1195-1401 |
1.09e-08 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 56.29 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTakygegGAAVLENISFSIDSGQRVGLLGRTGSGKSTL---LFAFLRLlnTEGDIQIDGVSWNTVSVQQWRKA- 1270
Cdd:cd03215 5 LEVRGLS------VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELaeaLFGLRPP--ASGEITLDGKPVTRRSPRDAIRAg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1271 FGVIP---QKVFIFSGtfrmnldpygqwndeeiWKVAEEVGLksvieqfpgqldfvlvdgGCVLSHGHKQLMCLARSVLS 1347
Cdd:cd03215 77 IAYVPedrKREGLVLD-----------------LSVAENIAL------------------SSLLSGGNQQKVVLARWLAR 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1631900066 1348 RAKILLLDEPSAHLDPVTSQVIRKTL-KHAFANCTVIL--SEhrLEAMLE-CQRFLVI 1401
Cdd:cd03215 122 DPRVLILDEPTRGVDVGAKAEIYRLIrELADAGKAVLLisSE--LDELLGlCDRILVM 177
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1191-1390 |
1.20e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 57.67 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1191 SGGKMTVKDLTAKYGEggAAVLENISFSIDSGQRVGLLGRTGSGKSTllfaFLRLLN-----TEGDIQIDGVSWNTVsvq 1265
Cdd:PRK10619 2 SENKLNVIDLHKRYGE--HEVLKGVSLQANAGDVISIIGSSGSGKST----FLRCINflekpSEGSIVVNGQTINLV--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1266 qwRKAFGVIpqKVF------IFSGTFRMNLDPYGQWND----EEIWKVAEEV-GLKSVI--EQFPGQLDFVLVDGGCV-- 1330
Cdd:PRK10619 73 --RDKDGQL--KVAdknqlrLLRTRLTMVFQHFNLWSHmtvlENVMEAPIQVlGLSKQEarERAVKYLAKVGIDERAQgk 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1631900066 1331 ----LSHGHKQLMCLARSVLSRAKILLLDEPSAHLDP-VTSQVIRKTLKHAFANCTVILSEHRLE 1390
Cdd:PRK10619 149 ypvhLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPeLVGEVLRIMQQLAEEGKTMVVVTHEMG 213
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
409-605 |
1.52e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 57.82 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 409 NNLFFSNFPLHASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGRIsFSPQVSW--------- 479
Cdd:PRK13650 8 KNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL-LTEENVWdirhkigmv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 480 -------IMPGTIKENIIFG-----VSYDEYRyKSVIKACQLEeDISKFPEKDYTVLgeggiilSGGQRARISLARAVYK 547
Cdd:PRK13650 87 fqnpdnqFVGATVEDDVAFGlenkgIPHEEMK-ERVNEALELV-GMQDFKEREPARL-------SGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1631900066 548 DADLYLLDS------PFGHLD-IFTEKEIFEScvcklmANKTRILVTSKLEHLKIADKILILHEG 605
Cdd:PRK13650 158 RPKIIILDEatsmldPEGRLElIKTIKGIRDD------YQMTVISITHDLDEVALSDRVLVMKNG 216
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1195-1432 |
2.27e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 57.05 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTAKYGEGGAA-VLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLNTE-GDIQIDGVSWNTVSVQQWRKAFG 1272
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAEsGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1273 VI---PQKVFI---FSGTFRMNLDPYGQWNDEEIWKVAEE---VGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLAR 1343
Cdd:PRK13650 85 MVfqnPDNQFVgatVEDDVAFGLENKGIPHEEMKERVNEAlelVGMQDFKEREPAR-----------LSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1344 SVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFA--NCTVILSEHRLEAMLECQRFLVIEDNKLrqyESIqkllnekSS 1421
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQV---EST-------ST 223
|
250
....*....|.
gi 1631900066 1422 FRQAISHADRL 1432
Cdd:PRK13650 224 PRELFSRGNDL 234
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1205-1391 |
2.32e-08 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 55.70 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1205 GEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSwntvsvqqwRKAFgvIPQKVFI--- 1280
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRpTSGTVRRAGGA---------RVAY--VPQRSEVpds 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1281 FSGTFRmNLDPYGQWNDEEIWK---------VA---EEVGLksviEQFPG-QLDfvlvdggcVLSHGHKQLMCLARSVLS 1347
Cdd:NF040873 70 LPLTVR-DLVAMGRWARRGLWRrltrddraaVDdalERVGL----ADLAGrQLG--------ELSGGQRQRALLAQGLAQ 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1631900066 1348 RAKILLLDEPSAHLDPVTSQVIRKTLKHAFA-NCTVILSEHRLEA 1391
Cdd:NF040873 137 EADLLLLDEPTTGLDAESRERIIALLAEEHArGATVVVVTHDLEL 181
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
423-616 |
2.37e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 56.98 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 423 VLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGR-------------ISFSPQVSWIMPG------ 483
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkdifqidaIKLRKEVGMVFQQpnpfph 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 484 -TIKENIIFGVSYDEYRYKSVIKACqLEEDISKFP--EKDYTVLGEGGIILSGGQRARISLARAVYKDADLYLLDSPFGH 560
Cdd:PRK14246 105 lSIYDNIAYPLKSHGIKEKREIKKI-VEECLRKVGlwKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1631900066 561 LDIFTEKEIfESCVCKLMANKTRILVTSKLEHL-KIADKILILHEGSCYFYGTFSEL 616
Cdd:PRK14246 184 IDIVNSQAI-EKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1195-1394 |
2.40e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 56.81 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTAKYGEGGAAvLENISFSIDSGQRVGLLGRTGSGKSTL---LFAFLRLlnTEGDIQIDGVSWNTVSVQQ----- 1266
Cdd:PRK15056 7 IVVNDVTVTWRNGHTA-LRDASFTVPGGSIAALVGVNGSGKSTLfkaLMGFVRL--ASGKISILGQPTRQALQKNlvayv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1267 -------WrkAFGVIPQKVFIFSGTFRMNLDPYGQWNDEEIWKVA-EEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQL 1338
Cdd:PRK15056 84 pqseevdW--SFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAAlARVDMVEFRHRQIGE-----------LSGGQKKR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1631900066 1339 MCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFAN-CTVILSEHRLEAMLE 1394
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTE 207
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
423-605 |
3.19e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 57.02 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 423 VLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKI----KHSGRISFSPQVSWIMP---------------- 482
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifKDEKNKKKTKEKEKVLEklviqktrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 483 -------------------GTIKENIIFG-VSYD------EYRYKSVIKACQLEED-ISKFPEKdytvlgeggiiLSGGQ 535
Cdd:PRK13651 102 eirrrvgvvfqfaeyqlfeQTIEKDIIFGpVSMGvskeeaKKRAAKYIELVGLDESyLQRSPFE-----------LSGGQ 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 536 RARISLARAVYKDADLYLLDSPFGHLDIFTEKEIFESCVCKLMANKTRILVTSKLEH-LKIADKILILHEG 605
Cdd:PRK13651 171 KRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNvLEWTKRTIFFKDG 241
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1212-1387 |
3.25e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 58.13 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1212 LENISFSIDSGQRVGLLGRTGSGKSTLL--FAFLRLLNTE--GDIQIDGVSWNTvSVQQWRKAFgVIPQKVFI------- 1280
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMnaLAFRSPKGVKgsGSVLLNGMPIDA-KEMRAISAY-VQQDDLFIptltvre 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1281 ---FSGTFRMNLDPYGQWNDEEIWKVAEEVGLKS---VIEQFPGQLDfvlvdggcVLSHGHKQLMCLARSVLSRAKILLL 1354
Cdd:TIGR00955 119 hlmFQAHLRMPRRVTKKEKRERVDEVLQALGLRKcanTRIGVPGRVK--------GLSGGERKRLAFASELLTDPPLLFC 190
|
170 180 190
....*....|....*....|....*....|....
gi 1631900066 1355 DEPSAHLDPVTSQVIRKTLKH-AFANCTVILSEH 1387
Cdd:TIGR00955 191 DEPTSGLDSFMAYSVVQVLKGlAQKGKTIICTIH 224
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1207-1362 |
3.77e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 57.26 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1207 GGAAVLENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLN-----TEGDIQIDGVSWNTVSVQQwRK------------ 1269
Cdd:PRK09452 25 DGKEVISNLDLTINNGEFLTLLGPSGCGKTTV----LRLIAgfetpDSGRIMLDGQDITHVPAEN-RHvntvfqsyalfp 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1270 --------AFGVIPQKVfifsgtfrmnldPygqwnDEEIWKVAEE----VGLKSVIEQFPGQldfvlvdggcvLSHGHKQ 1337
Cdd:PRK09452 100 hmtvfenvAFGLRMQKT------------P-----AAEITPRVMEalrmVQLEEFAQRKPHQ-----------LSGGQQQ 151
|
170 180
....*....|....*....|....*
gi 1631900066 1338 LMCLARSVLSRAKILLLDEPSAHLD 1362
Cdd:PRK09452 152 RVAIARAVVNKPKVLLLDESLSALD 176
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
1212-1389 |
3.78e-08 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 56.00 E-value: 3.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1212 LENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLNTEGDIQIDGVSWNTVSVQQWRKAFGVIPQKVfifSGTFRMnldP 1291
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQGEILLNGRPLSDWSAAELARHRAYLSQQQ---SPPFAM---P 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1292 YGQWNDEEIWKVAEEVGLKSVIEQFPGQLDfvLVDG-GCVLSH---GHKQLMCLARSVL-------SRAKILLLDEPSAH 1360
Cdd:COG4138 86 VFQYLALHQPAGASSEAVEQLLAQLAEALG--LEDKlSRPLTQlsgGEWQRVRLAAVLLqvwptinPEGQLLLLDEPMNS 163
|
170 180 190
....*....|....*....|....*....|.
gi 1631900066 1361 LDpVTSQVIRKTLKHAFANC--TVILSEHRL 1389
Cdd:COG4138 164 LD-VAQQAALDRLLRELCQQgiTVVMSSHDL 193
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1208-1368 |
5.15e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 55.95 E-value: 5.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1208 GAAVLENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLN-----TEGDIQIDGV---SWNTVSV--------QQWRKAF 1271
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTL----LKMLGrhqppSEGEILLDAQpleSWSSKAFarkvaylpQQLPAAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1272 GV-IPQKVFIFSGTFRMNLDPYGQWNDEEIWKVAEEVGLKSVIEQfpgqldfvLVDGgcvLSHGHKQLMCLARSVLSRAK 1350
Cdd:PRK10575 99 GMtVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHR--------LVDS---LSGGERQRAWIAMLVAQDSR 167
|
170
....*....|....*...
gi 1631900066 1351 ILLLDEPSAHLDpVTSQV 1368
Cdd:PRK10575 168 CLLLDEPTSALD-IAHQV 184
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
423-616 |
5.22e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 55.67 E-value: 5.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 423 VLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEpsqgkiKHSGRISFSPQVSWIMPgtIKENIIFGVSY-----DE 497
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVP------RDAGNIIIDDEDISLLP--LHARARRGIGYlpqeaSI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 498 YR----YKSVIKACQLEEDISKFPEKDYT--VLGEGGII---------LSGGQRARISLARAVYKDADLYLLDSPFGHLD 562
Cdd:PRK10895 90 FRrlsvYDNLMAVLQIRDDLSAEQREDRAneLMEEFHIEhlrdsmgqsLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1631900066 563 ---IFTEKEIFEscvcKLMANKTRILVTSK--LEHLKIADKILILHEGSCYFYGTFSEL 616
Cdd:PRK10895 170 pisVIDIKRIIE----HLRDSGLGVLITDHnvRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
425-605 |
5.62e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 56.58 E-value: 5.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 425 QDINFRIEKGQLLAVSGSTGAGKTSLLMMI-----------------MGELEPSQ---GKIKHSgrISFSPQVSwimpgt 484
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIagleditsgdlfigekrMNDVPPAErgvGMVFQS--YALYPHLS------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 485 IKENIIFGV-------SYDEYRYKSVIKACQLEEDISKFPeKDytvlgeggiiLSGGQRARISLARAVYKDADLYLLDSP 557
Cdd:PRK11000 92 VAENMSFGLklagakkEEINQRVNQVAEVLQLAHLLDRKP-KA----------LSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 558 FGHLDIFTEKEIfESCVCKLMA--NKTRILVT-SKLEHLKIADKILILHEG 605
Cdd:PRK11000 161 LSNLDAALRVQM-RIEISRLHKrlGRTMIYVThDQVEAMTLADKIVVLDAG 210
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
424-620 |
6.06e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 56.01 E-value: 6.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 424 LQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGR-ISFSPQvsWIMpgTIKENIifGVSYDEYRYKs 502
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpIDYSRK--GLM--KLRESV--GMVFQDPDNQ- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 503 vIKACQLEEDIS------KFPEKDY-----TVLGEGGI---------ILSGGQRARISLARAVYKDADLYLLDSPFGHLD 562
Cdd:PRK13636 95 -LFSASVYQDVSfgavnlKLPEDEVrkrvdNALKRTGIehlkdkpthCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLD 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1631900066 563 IFTEKEIFEscVCKLMANK---TRILVTSKLEHLKI-ADKILILHEGSCYFYGTFSELQGQR 620
Cdd:PRK13636 174 PMGVSEIMK--LLVEMQKElglTIIIATHDIDIVPLyCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
423-616 |
6.92e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 55.58 E-value: 6.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 423 VLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGR---------------ISFSPQVSWIMPGTIKE 487
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfvgLVFQNPDDQIFSPTVEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 488 NIIFG---VSYDE----YRYKSVIKACQLEEDISKFPEKdytvlgeggiiLSGGQRARISLARAVYKDADLYLLDSPFGH 560
Cdd:PRK13652 99 DIAFGpinLGLDEetvaHRVSSALHMLGLEELRDRVPHH-----------LSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1631900066 561 LDIFTEKEIFescvckLMANK-------TRILVTSKLEHL-KIADKILILHEGSCYFYGTFSEL 616
Cdd:PRK13652 168 LDPQGVKELI------DFLNDlpetygmTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
419-605 |
7.07e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 55.14 E-value: 7.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 419 HASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKH-----SGRISFSPQVSWI------------- 480
Cdd:PRK11264 14 HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditiDTARSLSQQKGLIrqlrqhvgfvfqn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 481 ---MPG-TIKENIIFG--VSYDEYRYKSVIKACQL--------EEDisKFPEKdytvlgeggiiLSGGQRARISLARAVY 546
Cdd:PRK11264 94 fnlFPHrTVLENIIEGpvIVKGEPKEEATARARELlakvglagKET--SYPRR-----------LSGGQQQRVAIARALA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 547 KDADLYLLDSPFGHLDIFTEKEIFESCVCKLMANKTRILVTSKLEHLK-IADKILILHEG 605
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARdVADRAIFMDQG 220
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1195-1405 |
1.15e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.09 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTAKYGegGAAVLENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLL-------NTEGDIQIDG--VSWNTVSVQ 1265
Cdd:PRK13549 6 LEMKNITKTFG--GVKALDNVSLKVRAGEIVSLCGENGAGKSTL----MKVLsgvyphgTYEGEIIFEGeeLQASNIRDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1266 QwRKAFGVIPQKVF----------IFSGTfrmNLDPYGQWNDEEIWKVAEEVgLKSVieqfpgQLDfvlVDGGCVLSH-- 1333
Cdd:PRK13549 80 E-RAGIAIIHQELAlvkelsvlenIFLGN---EITPGGIMDYDAMYLRAQKL-LAQL------KLD---INPATPVGNlg 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1631900066 1334 -GHKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQV---IRKTLKHAFANCTVIlsEHRLEAMLE-CQRFLVIEDNK 1405
Cdd:PRK13549 146 lGQQQLVEIAKALNKQARLLILDEPTASLTESETAVlldIIRDLKAHGIACIYI--SHKLNEVKAiSDTICVIRDGR 220
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
422-617 |
1.22e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 55.09 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGK----------------IKHSGRISFSPQVSWIMPGTI 485
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKvyvdgldtsdeenlwdIRNKAGMVFQNPDNQIVATIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 486 KENIIF-----GVSYDEYRYK--SVIKACQLEEDISKFPEkdytvlgeggiILSGGQRARISLARAVYKDADLYLLDSPF 558
Cdd:PRK13633 104 EEDVAFgpenlGIPPEEIRERvdESLKKVGMYEYRRHAPH-----------LLSGGQKQRVAIAGILAMRPECIIFDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1631900066 559 GHLDIFTEKEIFeSCVCKLmaNK----TRILVTSKLEHLKIADKILILHEGSCYFYGT----FSELQ 617
Cdd:PRK13633 173 AMLDPSGRREVV-NTIKEL--NKkygiTIILITHYMEEAVEADRIIVMDSGKVVMEGTpkeiFKEVE 236
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1212-1389 |
1.30e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 54.55 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1212 LENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLNTEGDIQIDGVSWNTVS-----------VQQWRKAFGVipqKVFI 1280
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLEAWSaaelarhraylSQQQTPPFAM---PVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1281 FSGTFRMNLDPYGQWNDeEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVL-------SRAKILL 1353
Cdd:PRK03695 89 YLTLHQPDKTRTEAVAS-ALNEVAEALGLDDKLGRSVNQ-----------LSGGEWQRVRLAAVVLqvwpdinPAGQLLL 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 1631900066 1354 LDEPSAHLDpVTSQVIRKTLKHAFANC--TVILSEHRL 1389
Cdd:PRK03695 157 LDEPMNSLD-VAQQAALDRLLSELCQQgiAVVMSSHDL 193
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
426-631 |
1.32e-07 |
|
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: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 426 DINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGRISFSPQVSWIMP------G------------TIKE 487
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPphrrriGyvfqearlfphlSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 488 NIIFG----------VSYDEyryksVIKACQLEEDISKFPEKdytvlgeggiiLSGGQRARISLARAVYKDADLYLLDSP 557
Cdd:COG4148 97 NLLYGrkrapraerrISFDE-----VVELLGIGHLLDRRPAT-----------LSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 558 FGHLDIFTEKEI---FEScvcklMANKTRI---LVT-SKLEHLKIADKILILHEGSCYFYGTFSELQGqRPDFSSELMGF 630
Cdd:COG4148 161 LAALDLARKAEIlpyLER-----LRDELDIpilYVShSLDEVARLADHVVLLEQGRVVASGPLAEVLS-RPDLLPLAGGE 234
|
.
gi 1631900066 631 D 631
Cdd:COG4148 235 E 235
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
424-618 |
1.41e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.07 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 424 LQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGR-ISFSPQVSWIMPG--------------TIKEN 488
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQeMRFASTTAALAAGvaiiyqelhlvpemTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 489 IIFG--------VSYDEYRYKSVIKACQLEEDISkfPEkdyTVLGEggiiLSGGQRARISLARAVYKDADLYLLDSPFGH 560
Cdd:PRK11288 100 LYLGqlphkggiVNRRLLNYEAREQLEHLGVDID--PD---TPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTSS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 561 LDIfTEKEIFESCVCKLMANKTRIL-VTSKLEHL-KIADKILILHEGScyFYGTFSELQG 618
Cdd:PRK11288 171 LSA-REIEQLFRVIRELRAEGRVILyVSHRMEEIfALCDAITVFKDGR--YVATFDDMAQ 227
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1199-1369 |
1.45e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 54.05 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1199 DLTAKYGEGGAA--VLENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLN-----TEGDIQIDGVSWNTVS----VQQW 1267
Cdd:PRK11629 10 NLCKRYQEGSVQtdVLHNVSFSIGEGEMMAIVGSSGSGKSTL----LHLLGgldtpTSGDVIFNGQPMSKLSsaakAELR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1268 RKAFGVIPQ-----KVFIFSGTFRMNLdPYGQWNDEEIWKVAEE----VGLKSVIEQFPGQldfvlvdggcvLSHGHKQL 1338
Cdd:PRK11629 86 NQKLGFIYQfhhllPDFTALENVAMPL-LIGKKKPAEINSRALEmlaaVGLEHRANHRPSE-----------LSGGERQR 153
|
170 180 190
....*....|....*....|....*....|.
gi 1631900066 1339 MCLARSVLSRAKILLLDEPSAHLDPVTSQVI 1369
Cdd:PRK11629 154 VAIARALVNNPRLVLADEPTGNLDARNADSI 184
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
423-615 |
1.67e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 56.04 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 423 VLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPS--QGKIKHSG---------RISFSPQVSWIMPG-TIKENII 490
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNrkptkqilkRTGFVTQDDILYPHlTVRETLV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 491 F--------GVSYDEyryksviKACQLEEDISKF--PEKDYTVLGEGGII-LSGGQRARISLARAVYKDADLYLLDSPFG 559
Cdd:PLN03211 163 FcsllrlpkSLTKQE-------KILVAESVISELglTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 560 HLDIFTEKEIFESCVCklMANKTRILVTSKLEH----LKIADKILILHEGSCYFYGTFSE 615
Cdd:PLN03211 236 GLDATAAYRLVLTLGS--LAQKGKTIVTSMHQPssrvYQMFDSVLVLSEGRCLFFGKGSD 293
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
416-543 |
1.79e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 53.56 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 416 FPLHASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG-------------RISFSPQVSWIMP 482
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGedistlkpeiyrqQVSYCAQTPTLFG 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 483 GTIKENIIFGVsydEYRYKSVIKAcQLEEDISKFpEKDYTVLGEGGIILSGGQRARISLAR 543
Cdd:PRK10247 95 DTVYDNLIFPW---QIRNQQPDPA-IFLDDLERF-ALPDTILTKNIAELSGGEKQRISLIR 150
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
424-602 |
1.90e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.42 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 424 LQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGR-ISF-SPQVSwIMPG--------------TIKE 487
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpVRIrSPRDA-IALGigmvhqhfmlvpnlTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 488 NIIFGVsydEYRYKSVIKACQLEEDISKFPEK-----D-YTVLGEggiiLSGGQRARISLARAVYKDADLYLLDSPFGHL 561
Cdd:COG3845 100 NIVLGL---EPTKGGRLDRKAARARIRELSERygldvDpDAKVED----LSVGEQQRVEILKALYRGARILILDEPTAVL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1631900066 562 difTEKEI---FEscVCKLMAN--KTRILVTSKL-EHLKIADKILIL 602
Cdd:COG3845 173 ---TPQEAdelFE--ILRRLAAegKSIIFITHKLrEVMAIADRVTVL 214
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
104-283 |
1.92e-07 |
|
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: 54.35 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 104 YYLGIGLCLLFLVRTLLIHPAIFGLHHIG----MQMRIAMFsliyKKILKLSSRVLDKISTGQLVSLLSNNLNKFDEGL- 178
Cdd:cd18552 39 LLVPLAIIGLFLLRGLASYLQTYLMAYVGqrvvRDLRNDLF----DKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALt 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 179 -ALAHFVwIAPLQVALLMGLL----WDMleasAFSGLAFLIVLAFFQAWLGQMMMKYRNK---RAGKINERLvitSEIIE 250
Cdd:cd18552 115 sALTVLV-RDPLTVIGLLGVLfyldWKL----TLIALVVLPLAALPIRRIGKRLRKISRRsqeSMGDLTSVL---QETLS 186
|
170 180 190
....*....|....*....|....*....|....*..
gi 1631900066 251 NIQSVKAYCWEDAM----EKMIESIRETELKLTRKAA 283
Cdd:cd18552 187 GIRVVKAFGAEDYEikrfRKANERLRRLSMKIARARA 223
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
422-476 |
2.06e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.28 E-value: 2.06e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHS--GRISFSPQ 476
Cdd:PRK15064 333 PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSenANIGYYAQ 389
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1195-1367 |
2.18e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 55.48 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTAKYGEGGAA--VLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLNT------EGDIQIDGVSWNTVSVQQ 1266
Cdd:PRK15134 6 LAIENLSVAFRQQQTVrtVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSppvvypSGDIRFHGESLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1267 WRKAFGviPQKVFIFSGTFrMNLDPYGQWNDE------------------EIWKVAEEVGLKSV---IEQFPGQldfvlv 1325
Cdd:PRK15134 86 LRGVRG--NKIAMIFQEPM-VSLNPLHTLEKQlyevlslhrgmrreaargEILNCLDRVGIRQAakrLTDYPHQ------ 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1631900066 1326 dggcvLSHGHKQLMCLARSVLSRAKILLLDEPSAHLDpVTSQ 1367
Cdd:PRK15134 157 -----LSGGERQRVMIAMALLTRPELLIADEPTTALD-VSVQ 192
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1195-1256 |
2.38e-07 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 53.55 E-value: 2.38e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1631900066 1195 MTVKDLTAKYGegGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDG 1256
Cdd:COG4604 2 IEIKNVSKRYG--GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPpDSGEVLVDG 62
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
433-583 |
3.75e-07 |
|
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: 51.22 E-value: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 433 KGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIkhsgrISFSPQVSWIMPGTIKENIIFgvsydeyryksvikacqleed 512
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV-----IYIDGEDILEEVLDQLLLIIV--------------------- 54
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 513 iskfpekdytvlGEGGIILSGGQRARISLARAVYKDADLYLLDSPFGHLDIFTEKEIFESCVCKLMANKTR 583
Cdd:smart00382 55 ------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKS 113
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
438-628 |
3.79e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 54.11 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 438 AVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGRISF-SPQVSWIMP-----G------------TIKENIIFGVS-YDEY 498
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFdAEKGICLPPekrriGyvfqdarlfphyKVRGNLRYGMAkSMVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 499 RYKSVIKACQLEEDISKFPekdytvlgeggIILSGGQRARISLARAVYKDADLYLLDSPFGHLDIFTEKEifescvckLM 578
Cdd:PRK11144 108 QFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRE--------LL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 579 AN--------KTRIL-VTSKL-EHLKIADKILILHEGSCYFYGTFSELqgqrpdFSSELM 628
Cdd:PRK11144 169 PYlerlareiNIPILyVSHSLdEILRLADRVVVLEQGKVKAFGPLEEV------WASSAM 222
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
424-686 |
4.22e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.51 E-value: 4.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 424 LQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGR---ISFSPQVSWIMPGTikENI-----IFGVSY 495
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSaalIAISSGLNGQLTGI--ENIelkglMMGLTK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 496 DEyrYKSVIKACQLEEDISKF---PEKDYtvlgeggiilSGGQRARISLARAVYKDADLYLLDSPFGHLD-IFTEKeife 571
Cdd:PRK13545 118 EK--IKEIIPEIIEFADIGKFiyqPVKTY----------SSGMKSRLGFAISVHINPDILVIDEALSVGDqTFTKK---- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 572 sCVCKL----MANKTRILVTSKLEHLK-IADKILILHEGSCYFYGTFSELQGQRPDFSSElmgfdsFDQFSAERRNSILT 646
Cdd:PRK13545 182 -CLDKMnefkEQGKTIFFISHSLSQVKsFCTKALWLHYGQVKEYGDIKEVVDHYDEFLKK------YNQMSVEERKDFRE 254
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1631900066 647 ETLRRFS--IEGEGMGSRNEIKKQSFKQTSDFndKRKSSIII 686
Cdd:PRK13545 255 EQISQFQhgLLQEDQTGRERKRKKGKKTSRKF--KKKRVLIT 294
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
416-544 |
5.17e-07 |
|
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: 53.52 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 416 FPLHASPV--LQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGeLEPSQGKIkhSGRISF--------SP---------Q 476
Cdd:COG0444 11 FPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILG-LLPPPGIT--SGEILFdgedllklSEkelrkirgrE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 477 VSWIM--PGT-----------IKENII--FGVSYDEyRYKSVIKACQL------EEDISKFP-EkdytvlgeggiiLSGG 534
Cdd:COG0444 88 IQMIFqdPMTslnpvmtvgdqIAEPLRihGGLSKAE-ARERAIELLERvglpdpERRLDRYPhE------------LSGG 154
|
170
....*....|
gi 1631900066 535 QRARISLARA 544
Cdd:COG0444 155 MRQRVMIARA 164
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
423-605 |
5.31e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 54.34 E-value: 5.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 423 VLQDINFRIEKGQLLAVSGSTGAGKtSLLMMIMGELE-PSQGKIKHSGRisfspQVSWIMPGTI----KENiiFGVSYDE 497
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGK-STLMNILGCLDkPTSGTYRVAGQ-----DVATLDADALaqlrREH--FGFIFQR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 498 YRYKSVIKACQ----------------------------LEEDISKFPEKdytvlgeggiiLSGGQRARISLARAVYKDA 549
Cdd:PRK10535 95 YHLLSHLTAAQnvevpavyaglerkqrllraqellqrlgLEDRVEYQPSQ-----------LSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1631900066 550 DLYLLDSPFGHLDIFTEKEIFesCVCKLMANK--TRILVTSKLEHLKIADKILILHEG 605
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVM--AILHQLRDRghTVIIVTHDPQVAAQAERVIEIRDG 219
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
422-616 |
5.86e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.90 E-value: 5.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGR--------------ISFSPQVSWIMPG-TIK 486
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpakahqlgIYLVPQEPLLFPNlSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 487 ENIIFGVSY---DEYRYKSVIKA--CQLEEDISkfpekdytvlgegGIILSGGQRARISLARAVYKDADLYLLDSPFGHL 561
Cdd:PRK15439 105 ENILFGLPKrqaSMQKMKQLLAAlgCQLDLDSS-------------AGSLEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1631900066 562 DIFtEKEIFESCVCKLMANKTRILVTS-KL-EHLKIADKILILHEGSCYFYGTFSEL 616
Cdd:PRK15439 172 TPA-ETERLFSRIRELLAQGVGIVFIShKLpEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1207-1364 |
5.86e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.90 E-value: 5.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1207 GGAAVLENISFSIDSGQRVGLLGRTGSGKSTLL--FAFLRLLNTeGDIQIDGVSWNTVSVQQWRKaFGV--IPQKVFIFS 1282
Cdd:PRK15439 22 SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMkiIAGIVPPDS-GTLEIGGNPCARLTPAKAHQ-LGIylVPQEPLLFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1283 G-------TFRMnldPYGQWNDEEiwkvaeevgLKSVIEQFPGQLDFVLVDGgcVLSHGHKQLMCLARSVLSRAKILLLD 1355
Cdd:PRK15439 100 NlsvkeniLFGL---PKRQASMQK---------MKQLLAALGCQLDLDSSAG--SLEVADRQIVEILRGLMRDSRILILD 165
|
....*....
gi 1631900066 1356 EPSAHLDPV 1364
Cdd:PRK15439 166 EPTASLTPA 174
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1195-1394 |
5.95e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 53.32 E-value: 5.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTAKYGEGGA---AVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLNTE-GDIQIDGVsWNTVSVQQWRKA 1270
Cdd:PRK13631 22 LRVKNLYCVFDEKQEnelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKyGTIQVGDI-YIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1271 FGVIPQKVFIFSgTFRMNLDPYGQWNDEEIWKVAEE-------VGLKSVIEQFPGQLDFVLVDGGC----------VLSH 1333
Cdd:PRK13631 101 TNPYSKKIKNFK-ELRRRVSMVFQFPEYQLFKDTIEkdimfgpVALGVKKSEAKKLAKFYLNKMGLddsylerspfGLSG 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1631900066 1334 GHKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFA-NCTVILSEHRLEAMLE 1394
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAnNKTVFVITHTMEHVLE 241
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1195-1269 |
6.29e-07 |
|
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: 53.92 E-value: 6.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTAKYGEGGAA--VLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLL-----NTEGDIQIDGVSWNTVSVQQW 1267
Cdd:COG4172 7 LSVEDLSVAFGQGGGTveAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLpdpaaHPSGSILFDGQDLLGLSEREL 86
|
..
gi 1631900066 1268 RK 1269
Cdd:COG4172 87 RR 88
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
930-1016 |
6.63e-07 |
|
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: 52.82 E-value: 6.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 930 TVSKTLHQKMVHAVLHAPMSTFNSWKAGGMLNRFAKDTAVLDDLLPLTVFDFVQLILIVIGAITVVSILQPYIF---LAS 1006
Cdd:cd18551 66 RVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTlvtLAV 145
|
90
....*....|
gi 1631900066 1007 VPVIAAFIVL 1016
Cdd:cd18551 146 VPLAFLIILP 155
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
423-605 |
6.67e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 52.28 E-value: 6.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 423 VLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG-------------RISFSPQVSWIMPG------ 483
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgqlKVADKNQLRLLRTRltmvfq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 484 --------TIKENI------IFGVSYDEYRYKSVI---KACQLEEDISKFPekdytvlgeggIILSGGQRARISLARAVY 546
Cdd:PRK10619 100 hfnlwshmTVLENVmeapiqVLGLSKQEARERAVKylaKVGIDERAQGKYP-----------VHLSGGQQQRVSIARALA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 547 KDADLYLLDSPFGHLDIFTEKEIFESCVCKLMANKTRILVTSKLEHLK-IADKILILHEG 605
Cdd:PRK10619 169 MEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARhVSSHVIFLHQG 228
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1195-1402 |
6.89e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 52.30 E-value: 6.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTAKYGeGGAAVlENISFSIDSGQRVGLLGRTGSGKSTL---LFAFLRllNTEGDIQIDGVSWNTVSVQQ-WRKa 1270
Cdd:PRK11300 6 LSVSGLMMRFG-GLLAV-NNVNLEVREQEIVSLIGPNGAGKTTVfncLTGFYK--PTGGTILLRGQHIEGLPGHQiARM- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1271 fGVIP--QKVFIF------------------SGTFR--MNLDPYGQWNDEEIWKVA---EEVGLKSVIEQFPGQLdfvlv 1325
Cdd:PRK11300 81 -GVVRtfQHVRLFremtvienllvaqhqqlkTGLFSglLKTPAFRRAESEALDRAAtwlERVGLLEHANRQAGNL----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1326 dggcvlSHGHKQLMCLARSVLSRAKILLLDEPSAHLDPVT----SQVIRKtLKHAFaNCTVILSEHRLE-AMLECQRFLV 1400
Cdd:PRK11300 155 ------AYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKEtkelDELIAE-LRNEH-NVTVLLIEHDMKlVMGISDRIYV 226
|
..
gi 1631900066 1401 IE 1402
Cdd:PRK11300 227 VN 228
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1195-1394 |
7.42e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 52.32 E-value: 7.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTAKYGEggAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLNTegdiQIDGVSWNTVSVQQWRKAFGVI 1274
Cdd:PRK13638 2 LATSDLWFRYQD--EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRP----QKGAVLWQGKPLDYSKRGLLAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1275 PQKVfifSGTFRmnlDPYGQWN----DEEIWKVAEEVGLKSviEQFPGQLD--FVLVDGG--------CvLSHGHKQLMC 1340
Cdd:PRK13638 76 RQQV---ATVFQ---DPEQQIFytdiDSDIAFSLRNLGVPE--AEITRRVDeaLTLVDAQhfrhqpiqC-LSHGQKKRVA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1631900066 1341 LARSVLSRAKILLLDEPSAHLDPV-TSQVIRKTLKHAFANCTVILSEHRLEAMLE 1394
Cdd:PRK13638 147 IAGALVLQARYLLLDEPTAGLDPAgRTQMIAIIRRIVAQGNHVIISSHDIDLIYE 201
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1206-1363 |
8.73e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 52.44 E-value: 8.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1206 EGGAavLENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLN-----TEGDIQIDGVSWNTVS----VQQWRKAFGVIPQ 1276
Cdd:PRK13649 19 EGRA--LFDVNLTIEDGSYTAFIGHTGSGKSTI----MQLLNglhvpTQGSVRVDDTLITSTSknkdIKQIRKKVGLVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1277 --KVFIFSGTFRMNLdPYGQWN----DEEIWKVAEE----VGL-KSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSV 1345
Cdd:PRK13649 93 fpESQLFEETVLKDV-AFGPQNfgvsQEEAEALAREklalVGIsESLFEKNPFE-----------LSGGQMRRVAIAGIL 160
|
170
....*....|....*...
gi 1631900066 1346 LSRAKILLLDEPSAHLDP 1363
Cdd:PRK13649 161 AMEPKILVLDEPTAGLDP 178
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1212-1390 |
8.94e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 52.33 E-value: 8.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1212 LENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGvswNTVSVQQWRKAFGVIPQKVFI---------F 1281
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQpTSGTVTIGE---RVITAGKKNKKLKPLRKKVGIvfqfpehqlF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1282 SGTFRMNLdPYGQWN----DEEIWKVAEE----VGL-KSVIEQFP-----GQLDFVLVDGgcVLShghkqlMclarsvls 1347
Cdd:PRK13634 100 EETVEKDI-CFGPMNfgvsEEDAKQKAREmielVGLpEELLARSPfelsgGQMRRVAIAG--VLA------M-------- 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1631900066 1348 RAKILLLDEPSAHLDPVTsqviRKTLKHAFA------NCTVILSEHRLE 1390
Cdd:PRK13634 163 EPEVLVLDEPTAGLDPKG----RKEMMEMFYklhkekGLTTVLVTHSME 207
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
422-617 |
9.27e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 52.07 E-value: 9.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGRISFSPQVSWIMPGTIKENIIF--GVSY-DEY 498
Cdd:PRK11831 21 CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFqsGALFtDMN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 499 RYKSVikACQLEEDiSKFPEK--DYTVL---------GEGGII---LSGGQRARISLARAVYKDADLYLLDSPFGHLDIF 564
Cdd:PRK11831 101 VFDNV--AYPLREH-TQLPAPllHSTVMmkleavglrGAAKLMpseLSGGMARRAALARAIALEPDLIMFDEPFVGQDPI 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 565 TekeifESCVCKLMA--NK----TRILVTSKL-EHLKIADKILILHEGSCYFYGTFSELQ 617
Cdd:PRK11831 178 T-----MGVLVKLISelNSalgvTCVVVSHDVpEVLSIADHAYIVADKKIVAHGSAQALQ 232
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
423-605 |
9.42e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 51.80 E-value: 9.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 423 VLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGRISFSPQVSWIMPG---------------TIKE 487
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREavaivpegrrvfsrmTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 488 NIIFGVSY-DEYRYKSVIKacQLEEDISKFPEKDYTVLGeggiILSGGQRARISLARAVYKDADLYLLDSPFGHLDIFTE 566
Cdd:PRK11614 100 NLAMGGFFaERDQFQERIK--WVYELFPRLHERRIQRAG----TMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIII 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1631900066 567 KEIFESCVCKLMANKTRILVTSKL-EHLKIADKILILHEG 605
Cdd:PRK11614 174 QQIFDTIEQLREQGMTIFLVEQNAnQALKLADRGYVLENG 213
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
424-639 |
1.09e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 52.02 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 424 LQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGR---------------ISFSPQVSWIMPGTIKEN 488
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGElltaenvwnlrrkigMVFQNPDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 489 IIFGVSYDEYRYKSVIKacQLEEDISKFPEKDYTVLGEGGiiLSGGQRARISLARAVYKDADLYLLDSPFGHLDIFTEKE 568
Cdd:PRK13642 103 VAFGMENQGIPREEMIK--RVDEALLAVNMLDFKTREPAR--LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 569 IFEscVCKLMANK---TRILVTSKLEHLKIADKILILHEGSCYFYGTFSELQGQRPD---------FSSELM------GF 630
Cdd:PRK13642 179 IMR--VIHEIKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDmveigldvpFSSNLMkdlrknGF 256
|
....*....
gi 1631900066 631 DSFDQFSAE 639
Cdd:PRK13642 257 DLPEKYLSE 265
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1212-1363 |
1.13e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 52.04 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1212 LENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSVQQ----WRKAFGVIPQ--KVFIFSGT 1284
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQpTEGKVTVGDIVVSSTSKQKeikpVRKKVGVVFQfpESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1285 FRMNLdPYGQWN----DEEIWKVAEE----VGL-KSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSRAKILLLD 1355
Cdd:PRK13643 102 VLKDV-AFGPQNfgipKEKAEKIAAEklemVGLaDEFWEKSPFE-----------LSGGQMRRVAIAGILAMEPEVLVLD 169
|
....*...
gi 1631900066 1356 EPSAHLDP 1363
Cdd:PRK13643 170 EPTAGLDP 177
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1195-1387 |
1.19e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 52.09 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVK--DLTAKYGEGGA---AVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVS----V 1264
Cdd:PRK13646 1 MTIRfdNVSYTYQKGTPyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKpTTGTVTVDDITITHKTkdkyI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1265 QQWRKAFGVIPQ------------KVFIFS-GTFRMNLDPYgqwnDEEIWKVAEEVGL-KSVIEQFPGQldfvlvdggcv 1330
Cdd:PRK13646 81 RPVRKRIGMVFQfpesqlfedtveREIIFGpKNFKMNLDEV----KNYAHRLLMDLGFsRDVMSQSPFQ----------- 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1631900066 1331 LSHGHKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLK--HAFANCTVILSEH 1387
Cdd:PRK13646 146 MSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKslQTDENKTIILVSH 204
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
82-280 |
1.21e-06 |
|
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: 52.03 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 82 PLLLGRIIASYDPDNSDERSIAYY----LGIGLC---LLFLVRTLLIHPAifglHHIGMQMRIAMFSliykKILKLSSRV 154
Cdd:cd18541 19 PRIIGRAIDALTAGTLTASQLLRYalliLLLALLigiFRFLWRYLIFGAS----RRIEYDLRNDLFA----HLLTLSPSF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 155 LDKISTGQLVSLLSNNLNKFDE--GLALAHFVWIAPLQVALLMGLLWDMLEASAFSgLAFLIVLAFFQAWLGQMMMKyRN 232
Cdd:cd18541 91 YQKNRTGDLMARATNDLNAVRMalGPGILYLVDALFLGVLVLVMMFTISPKLTLIA-LLPLPLLALLVYRLGKKIHK-RF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1631900066 233 KRA----GKINERlviTSEIIENIQSVKAYCWEDAM----EKMIESIRETELKLTR 280
Cdd:cd18541 169 RKVqeafSDLSDR---VQESFSGIRVIKAFVQEEAEierfDKLNEEYVEKNLRLAR 221
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
416-616 |
1.66e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 51.55 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 416 FPLHASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGR---------ISFSPQVSWIMPGtiK 486
Cdd:PRK13638 9 FRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKpldyskrglLALRQQVATVFQD--P 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 487 ENIIFGVSYDEYRYKSVIKACQLEEDISKFPEKDYTVLGEGGI------ILSGGQRARISLARAVYKDADLYLLDSPFGH 560
Cdd:PRK13638 87 EQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFrhqpiqCLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1631900066 561 LDIFTEKEIFeSCVCKLMANKTRILVTSKLEHL--KIADKILILHEGSCYFYGTFSEL 616
Cdd:PRK13638 167 LDPAGRTQMI-AIIRRIVAQGNHVIISSHDIDLiyEISDAVYVLRQGQILTHGAPGEV 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
424-557 |
1.93e-06 |
|
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: 52.38 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 424 LQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGeLEPSQGKIKHSGR------------------I-------SFSPQvs 478
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQdldglsrralrplrrrmqVvfqdpfgSLSPR-- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 479 wiMpgTIKEnII--------FGVSYDEyRYKSVIKAcqLEE------DISKFP-EkdytvlgeggiiLSGGQRARISLAR 543
Cdd:COG4172 379 --M--TVGQ-IIaeglrvhgPGLSAAE-RRARVAEA--LEEvgldpaARHRYPhE------------FSGGQRQRIAIAR 438
|
170
....*....|....
gi 1631900066 544 AVYKDADLYLLDSP 557
Cdd:COG4172 439 ALILEPKLLVLDEP 452
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
423-565 |
2.01e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 52.24 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 423 VLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKhsgrisfspqvswiMPGTIKeniifgVSY-DEYR-- 499
Cdd:TIGR03719 337 LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIE--------------IGETVK------LAYvDQSRda 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 500 ---YKSVIkacqleEDISKfpEKDYTVLGEGGI---------------------ILSGGQRARISLARAVYKDADLYLLD 555
Cdd:TIGR03719 397 ldpNKTVW------EEISG--GLDIIKLGKREIpsrayvgrfnfkgsdqqkkvgQLSGGERNRVHLAKTLKSGGNVLLLD 468
|
170
....*....|
gi 1631900066 556 SPFGHLDIFT 565
Cdd:TIGR03719 469 EPTNDLDVET 478
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
418-622 |
2.03e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 51.17 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 418 LHASPVLQDINFRIEKGQLLAVSGSTGAGKTSLLM----MIMGELEPSQ------GKIKHSGRISFSPQVSWIMPG---- 483
Cdd:PRK09984 14 FNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGShiellgRTVQREGRLARDIRKSRANTGyifq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 484 --------TIKENIIFGVSYDEYRYKSVIKACQLEEDiskfpEKDYTVLGEGGII---------LSGGQRARISLARAVY 546
Cdd:PRK09984 94 qfnlvnrlSVLENVLIGALGSTPFWRTCFSWFTREQK-----QRALQALTRVGMVhfahqrvstLSGGQQQRVAIARALM 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1631900066 547 KDADLYLLDSPFGHLDIFTEKEIFESCVCKLMANKTRILVT-SKLEH-LKIADKILILHEGSCYFYGTFSELQGQRPD 622
Cdd:PRK09984 169 QQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTlHQVDYaLRYCERIVALRQGHVFYDGSSQQFDNERFD 246
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
426-605 |
2.13e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 52.13 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 426 DINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPS-QGKIKHSGR--------------ISFSPQ---VSWIMPGT-IK 486
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvdirnpaqairagIAMVPEdrkRHGIVPILgVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 487 ENIIFGVsYDEYRYKSVIKACQ----LEEDISKFPEKDYT-VLGEGGiiLSGGQRARISLARAVYKDADLYLLDSPFGHL 561
Cdd:TIGR02633 358 KNITLSV-LKSFCFKMRIDAAAelqiIGSAIQRLKVKTASpFLPIGR--LSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1631900066 562 DIFTEKEIFescvcKLMANKTR-----ILVTSKL-EHLKIADKILILHEG 605
Cdd:TIGR02633 435 DVGAKYEIY-----KLINQLAQegvaiIVVSSELaEVLGLSDRVLVIGEG 479
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
423-616 |
2.28e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 50.68 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 423 VLQDINFRIEKGQLLAVSGSTGAGKTSLLMMI--MGELEPS---QGKIKHSGRISFSPQVSWI---------MPG----- 483
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrLIELYPEarvSGEVYLDGQDIFKMDVIELrrrvqmvfqIPNpipnl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 484 TIKENIIFGVSYD---------EYRYKSVIKACQLEEDIskfpeKDYtvLGEGGIILSGGQRARISLARAVYKDADLYLL 554
Cdd:PRK14247 98 SIFENVALGLKLNrlvkskkelQERVRWALEKAQLWDEV-----KDR--LDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1631900066 555 DSPFGHLDIFTEKEIfESCVCKLMANKTRILVTS-KLEHLKIADKILILHEGSCYFYGTFSEL 616
Cdd:PRK14247 171 DEPTANLDPENTAKI-ESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
1207-1401 |
2.70e-06 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 50.58 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1207 GGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLfaflRLLN-----TEGDIQIDGVSWNTVSVQQWRKAFGVIPQKV--- 1278
Cdd:TIGR03873 12 GGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLL----RLLAgalrpDAGTVDLAGVDLHGLSRRARARRVALVEQDSdta 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1279 --FIFSGTFRMNLDPY-GQWNDEEiwkvAEEVGLKSVIEQFPGQLDFVLVDGGcVLSHGHKQLMCLARSVLSRAKILLLD 1355
Cdd:TIGR03873 88 vpLTVRDVVALGRIPHrSLWAGDS----PHDAAVVDRALARTELSHLADRDMS-TLSGGERQRVHVARALAQEPKLLLLD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1631900066 1356 EPSAHLDpVTSQ--VIRKTLKHAFANCTVILSEHRLE-AMLECQRFLVI 1401
Cdd:TIGR03873 163 EPTNHLD-VRAQleTLALVRELAATGVTVVAALHDLNlAASYCDHVVVL 210
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1196-1362 |
3.13e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 51.47 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1196 TVKDLTAKYGeGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLntEG-DIQIDGVSWntvsVQQWRKAfGVI 1274
Cdd:TIGR03719 6 TMNRVSKVVP-PKKEILKDISLSFFPGAKIGVLGLNGAGKSTL----LRIM--AGvDKDFNGEAR----PQPGIKV-GYL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1275 PQK------------VFIFSGTFRMNLDPYGQWN------DEEIWKVAEEVG-LKSVIEQFPG-----QLDFVLVDGGC- 1329
Cdd:TIGR03719 74 PQEpqldptktvrenVEEGVAEIKDALDRFNEISakyaepDADFDKLAAEQAeLQEIIDAADAwdldsQLEIAMDALRCp 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1631900066 1330 -------VLSHGHKQLMCLARSVLSRAKILLLDEPSAHLD 1362
Cdd:TIGR03719 154 pwdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1211-1370 |
3.60e-06 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 49.74 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1211 VLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLR-LLNTEGDIQIdgvswntvsvqqwRKAFGVIpqkvfifsgtfrmNL 1289
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnYLPDSGSILV-------------RHDGGWV-------------DL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1290 dpyGQWNDEEIWKV-AEEVGLKSvieQF----P--GQLDFV---LVDGGC-----------VLSH--------------- 1333
Cdd:COG4778 80 ---AQASPREILALrRRTIGYVS---QFlrviPrvSALDVVaepLLERGVdreeararareLLARlnlperlwdlppatf 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 1631900066 1334 --GHKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIR 1370
Cdd:COG4778 154 sgGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVV 192
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1207-1362 |
4.36e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.32 E-value: 4.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1207 GGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLfAFLRllnteGDIQIDGVS------WNTVSVQQWRKAFGViPQKVFI 1280
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLL-ALLK-----NEISADGGSytfpgnWQLAWVNQETPALPQ-PALEYV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1281 FSG--TFRmnldpygqwNDEEIWKVAEEVGLKSVIEQFPGQLDFV-----------LVDGgcvLSHGHKQL--------- 1338
Cdd:PRK10636 85 IDGdrEYR---------QLEAQLHDANERNDGHAIATIHGKLDAIdawtirsraasLLHG---LGFSNEQLerpvsdfsg 152
|
170 180
....*....|....*....|....*....
gi 1631900066 1339 -----MCLARSVLSRAKILLLDEPSAHLD 1362
Cdd:PRK10636 153 gwrmrLNLAQALICRSDLLLLDEPTNHLD 181
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
82-284 |
4.44e-06 |
|
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: 50.14 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 82 PLLLGRIIASYDPdNSDERSIaYYLGIGLCLLFLVRTLL-IHPAIFGlHHIGMQMRIAMFSLIYKKILKLSSRVLDKIST 160
Cdd:cd18549 22 PLIVRYIIDDLLP-SKNLRLI-LIIGAILLALYILRTLLnYFVTYWG-HVMGARIETDMRRDLFEHLQKLSFSFFDNNKT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 161 GQLVSLLSNNLNKFDEglaLAHF----VWIAPLQVALLMGLLWDM-LEASAFSgLAFLIVLAFFQAWLGQMMMK-YRN-- 232
Cdd:cd18549 99 GQLMSRITNDLFDISE---LAHHgpedLFISIITIIGSFIILLTInVPLTLIV-FALLPLMIIFTIYFNKKMKKaFRRvr 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1631900066 233 KRAGKINERLvitSEIIENIQSVKAYCWED-AMEKMIESIRetELKLTRKAAY 284
Cdd:cd18549 175 EKIGEINAQL---EDSLSGIRVVKAFANEEyEIEKFDEGND--RFLESKKKAY 222
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1211-1392 |
4.99e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 49.70 E-value: 4.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1211 VLENISFSIDSGQRVGLLGRTGSGKSTLLFAFL-RLLNTEGDIQIDGVSWNTVSVqqWRKAFGVIpqKVF--IFSGTF-R 1286
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAgSLPPDSGSILIDGKDVTKLPE--YKRAKYIG--RVFqdPMMGTApS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1287 M----NL-------DPYG-QW--NDEEIWKVAEEV-----GLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLS 1347
Cdd:COG1101 97 MtieeNLalayrrgKRRGlRRglTKKRRELFRELLatlglGLENRLDTKVGLL-----------SGGQRQALSLLMATLT 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1631900066 1348 RAKILLLDEPSAHLDPVTS-QVIRKTLKhafanctvILSEHRLEAM 1392
Cdd:COG1101 166 KPKLLLLDEHTAALDPKTAaLVLELTEK--------IVEENNLTTL 203
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1195-1408 |
5.08e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 49.75 E-value: 5.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTAKYGEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSVQQWRKAFGV 1273
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKvKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1274 I---PQKVFI-----FSGTFRM--NLDPYGQWNdEEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLAR 1343
Cdd:PRK13648 88 VfqnPDNQFVgsivkYDVAFGLenHAVPYDEMH-RRVSEALKQVDMLERADYEPNA-----------LSGGQKQRVAIAG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1631900066 1344 SVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFA--NCTVILSEHRLEAMLECQRFLVIEDNKLRQ 1408
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSehNITIISITHDLSEAMEADHVIVMNKGTVYK 222
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1205-1362 |
5.95e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 49.60 E-value: 5.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1205 GEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSVQQWRKAFGVIPQKVFIFSG 1283
Cdd:PRK10253 16 GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTpAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1284 TFRMNLDPYGQWNDEEI---WKVAEEVGLKSVIeQFPGQLDFVL--VDggcVLSHGHKQLMCLARSVLSRAKILLLDEPS 1358
Cdd:PRK10253 96 ITVQELVARGRYPHQPLftrWRKEDEEAVTKAM-QATGITHLADqsVD---TLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
....
gi 1631900066 1359 AHLD 1362
Cdd:PRK10253 172 TWLD 175
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1194-1363 |
6.45e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 50.74 E-value: 6.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1194 KMTVKDLTAKYGEGGAAVlENISFSIDSGQRVGLLGRTGSGKSTllfaFLRLLN-----TEGDIQIDGVSWNTVSVQQWR 1268
Cdd:PRK10522 322 TLELRNVTFAYQDNGFSV-GPINLTIKRGELLFLIGGNGSGKST----LAMLLTglyqpQSGEILLDGKPVTAEQPEDYR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1269 KAFGVIPQKVFIFSGTfrmnLDPYGQWNDEEI---WkvAEEVGLKSVIEqfpgqldfvlVDGGCV----LSHGHKQLMCL 1341
Cdd:PRK10522 397 KLFSAVFTDFHLFDQL----LGPEGKPANPALvekW--LERLKMAHKLE----------LEDGRIsnlkLSKGQKKRLAL 460
|
170 180
....*....|....*....|..
gi 1631900066 1342 ARSVLSRAKILLLDEPSAHLDP 1363
Cdd:PRK10522 461 LLALAEERDILLLDEWAADQDP 482
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1211-1436 |
7.02e-06 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 49.90 E-value: 7.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1211 VLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLNTEGDIQIDGVSWNTV-----SVQQWRKAFG----VIPQ----- 1276
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTADRFRWNGIdllklSPRERRKIIGreiaMIFQepssc 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1277 -----KVF------IFSGTFRMNLDPYGQWNDEEIWKVAEEVGLKS---VIEQFPGQldfvLVDGGCvlshghkQLMCLA 1342
Cdd:COG4170 102 ldpsaKIGdqlieaIPSWTFKGKWWQRFKWRKKRAIELLHRVGIKDhkdIMNSYPHE----LTEGEC-------QKVMIA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1343 RSVLSRAKILLLDEPSAHLDPVT-SQVIRKTLK-HAFANCTVILSEHRLEAMLE-CQRFLV--------------IEDNK 1405
Cdd:COG4170 171 MAIANQPRLLIADEPTNAMESTTqAQIFRLLARlNQLQGTSILLISHDLESISQwADTITVlycgqtvesgpteqILKSP 250
|
250 260 270
....*....|....*....|....*....|.
gi 1631900066 1406 LRQYesIQKLLNEKSSFRQAISHADRLKLLP 1436
Cdd:COG4170 251 HHPY--TKALLRSMPDFRQPLPHKSRLNTLP 279
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1195-1388 |
9.09e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.17 E-value: 9.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTAKYGEggAAVLENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLNTE-----GDIQI-DGVSWNTVSVQQW- 1267
Cdd:PRK10636 313 LKMEKVSAGYGD--RIILDSIKLNLVPGSRIGLLGRNGAGKSTL----IKLLAGElapvsGEIGLaKGIKLGYFAQHQLe 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1268 -------------RKAFGVIPQKVFIFSGTFRMNLDpygqwndeeiwKVAEEVglksviEQFPGqldfvlvdggcvlshG 1334
Cdd:PRK10636 387 flradesplqhlaRLAPQELEQKLRDYLGGFGFQGD-----------KVTEET------RRFSG---------------G 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1631900066 1335 HKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHaFANCTVILSEHR 1388
Cdd:PRK10636 435 EKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALID-FEGALVVVSHDR 487
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1207-1362 |
9.29e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.33 E-value: 9.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1207 GGAAVLENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLNTE-----GDIQI----------------------DGVSW 1259
Cdd:PRK11147 14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTL----MKILNGEvllddGRIIYeqdlivarlqqdpprnvegtvyDFVAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1260 NTVSVQQWRKAFGVIPQKVFIFSGTFRMN--------LDPYGQWN-DEEIWKVAEEVGLKSvieqfpgqlDFVLVDggcv 1330
Cdd:PRK11147 90 GIEEQAEYLKRYHDISHLVETDPSEKNLNelaklqeqLDHHNLWQlENRINEVLAQLGLDP---------DAALSS---- 156
|
170 180 190
....*....|....*....|....*....|..
gi 1631900066 1331 LSHGHKQLMCLARSVLSRAKILLLDEPSAHLD 1362
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1183-1422 |
9.60e-06 |
|
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: 50.78 E-value: 9.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1183 AKEEKNWPSGGKMT----VKDLTAKYGEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLfaflRLLN-----TEGDIQ 1253
Cdd:TIGR01257 1922 AEERQRIISGGNKTdilrLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTF----KMLTgdttvTSGDAT 1997
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1254 IDGVSWNTvSVQQWRKAFGVIPQkvfiFSG-----TFRMNLDPYGQWN---DEEIWKVA----EEVGLKSVIEQFPGqld 1321
Cdd:TIGR01257 1998 VAGKSILT-NISDVHQNMGYCPQ----FDAiddllTGREHLYLYARLRgvpAEEIEKVAnwsiQSLGLSLYADRLAG--- 2069
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1322 fvlvdggcVLSHGHKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFANC-TVILSEHRLEAMLE-CQRFL 1399
Cdd:TIGR01257 2070 --------TYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGrAVVLTSHSMEECEAlCTRLA 2141
|
250 260
....*....|....*....|...
gi 1631900066 1400 VIEDNKLRQYESIQKLlneKSSF 1422
Cdd:TIGR01257 2142 IMVKGAFQCLGTIQHL---KSKF 2161
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1195-1367 |
1.02e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 49.35 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTAKYGEGGA---AVlENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLNTEGDIQIDGVSWN-----TVSVQQ 1266
Cdd:PRK11022 4 LNVDKLSVHFGDESApfrAV-DRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLEFNgqdlqRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1267 WRKAFGVipQKVFIFSgtfrmnlDPYGQWND--------EEIWKVAE----------------EVGL---KSVIEQFPGQ 1319
Cdd:PRK11022 83 RRNLVGA--EVAMIFQ-------DPMTSLNPcytvgfqiMEAIKVHQggnkktrrqraidllnQVGIpdpASRLDVYPHQ 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1631900066 1320 ldfvlvdggcvLSHGHKQLMCLARSVLSRAKILLLDEPSAHLDpVTSQ 1367
Cdd:PRK11022 154 -----------LSGGMSQRVMIAMAIACRPKLLIADEPTTALD-VTIQ 189
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
931-1070 |
1.15e-05 |
|
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: 48.96 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 931 VSKTLHQKMVHAVLHAPMSTFNSWKAGGMLNRFAKDTAVLDDLLPLTVFDFVQLILIVIGAITVVSILQPY---IFLASV 1007
Cdd:cd18552 70 VVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKltlIALVVL 149
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1631900066 1008 PVIAAFIV-----LRAYflhTSQQLKQLESearspIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALN 1070
Cdd:cd18552 150 PLAALPIRrigkrLRKI---SRRSQESMGD-----LTSVLQETLSGIRVVKAFGAEDYEIKRFRKANE 209
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1208-1419 |
1.16e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.91 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1208 GAAVLENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLN-----TEGDIQIDGVSWNTVSVqqwRKAFG----VIPQKv 1278
Cdd:PRK11288 16 GVKALDDISFDCRAGQVHALMGENGAGKSTL----LKILSgnyqpDAGSILIDGQEMRFAST---TAALAagvaIIYQE- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1279 fifsgtfrMNLDPygqwndeEIwKVAEEVGLKsvieQFPGQLDFvlVDGGCV-----------------------LSHGH 1335
Cdd:PRK11288 88 --------LHLVP-------EM-TVAENLYLG----QLPHKGGI--VNRRLLnyeareqlehlgvdidpdtplkyLSIGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1336 KQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFANCTVILS-EHRLEAMLE-CQRFLVIEDNKL-RQYESI 1412
Cdd:PRK11288 146 RQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYvSHRMEEIFAlCDAITVFKDGRYvATFDDM 225
|
....*..
gi 1631900066 1413 QKLLNEK 1419
Cdd:PRK11288 226 AQVDRDQ 232
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1196-1362 |
1.29e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.51 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1196 TVKDLTAKYGEGgaAVLENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLntEGDIQIDG--VSWNTVSvqqwrkAFGV 1273
Cdd:PRK15064 321 EVENLTKGFDNG--PLFKNLNLLLEAGERLAIIGENGVGKTTL----LRTL--VGELEPDSgtVKWSENA------NIGY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1274 IPQKVfifSGTFR--MNL-DPYGQWNDEEiwkvAEEVGLKSVIeqfpGQLDFVLVDGG---CVLSHGHKQLMCLARSVLS 1347
Cdd:PRK15064 387 YAQDH---AYDFEndLTLfDWMSQWRQEG----DDEQAVRGTL----GRLLFSQDDIKksvKVLSGGEKGRMLFGKLMMQ 455
|
170
....*....|....*
gi 1631900066 1348 RAKILLLDEPSAHLD 1362
Cdd:PRK15064 456 KPNVLVMDEPTNHMD 470
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
424-605 |
1.49e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 48.25 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 424 LQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKI-------------KHSGRI---------SFSP--QVSW 479
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELliddhplhfgdysYRSQRIrmifqdpstSLNPrqRISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 480 IMPGTIKENIIFGVSYDEYRYKSVIKACQLEED-ISKFPEkdytvlgeggiILSGGQRARISLARAVYKDADLYLLDSPF 558
Cdd:PRK15112 109 ILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDhASYYPH-----------MLAPGQKQRLGLARALILRPKVIIADEAL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1631900066 559 GHLDIFTEKEIFeSCVCKLMANK--TRILVTSKLEHLK-IADKILILHEG 605
Cdd:PRK15112 178 ASLDMSMRSQLI-NLMLELQEKQgiSYIYVTQHLGMMKhISDQVLVMHQG 226
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1211-1390 |
1.49e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 47.65 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1211 VLENISFSIDSGQRVGLLGRTGSGKSTLLfaflrllntegdiqidgvswntvsvqqwRKAFGVIPQKVFifSGTFRMnld 1290
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLL----------------------------RLLAGALKGTPV--AGCVDV--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1291 PYGQWNDEeiwkvaeevglKSVIEQFPGQLDF-----VLVDGGCV-----------LSHGHKQLMCLARSVLSRAKILLL 1354
Cdd:COG2401 92 PDNQFGRE-----------ASLIDAIGRKGDFkdaveLLNAVGLSdavlwlrrfkeLSTGQKFRFRLALLLAERPKLLVI 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 1631900066 1355 DEPSAHLDPVTSQVIRKTLKHAF--ANCTVILSEHRLE 1390
Cdd:COG2401 161 DEFCSHLDRQTAKRVARNLQKLArrAGITLVVATHHYD 198
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
69-285 |
1.61e-05 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 48.62 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 69 IILYLGEVTKSVQPLLLGRIIASYDPDNSDERSIAY-YLGIGLCLLFLVRTLLIHpaIFGlHHIGMQMRIAMFsliyKKI 147
Cdd:cd18577 18 MTIVFGDLFDAFTDFGSGESSPDEFLDDVNKYALYFvYLGIGSFVLSYIQTACWT--ITG-ERQARRIRKRYL----KAL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 148 LKLSSRVLDKISTGQLVSLLSNNLNKFDEGLA--LAHFVW-----IAPLQVALLMGllWDMleasAFSGLAFLIVLAFFQ 220
Cdd:cd18577 91 LRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGekLGLLIQslstfIAGFIIAFIYS--WKL----TLVLLATLPLIAIVG 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1631900066 221 AWLGQMMMKYRNK------RAGKINErlvitsEIIENIQSVKAYCWEDAM-EKMIESIRETELKLTRKAAYV 285
Cdd:cd18577 165 GIMGKLLSKYTKKeqeayaKAGSIAE------EALSSIRTVKAFGGEEKEiKRYSKALEKARKAGIKKGLVS 230
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1200-1375 |
1.69e-05 |
|
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: 47.26 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1200 LTAKYGEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFlrLLNTEGDIQIDG-VSWNTVSVqqwrKAFGVIPQKV 1278
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKAL--ANRTEGNVSVEGdIHYNGIPY----KEFAEKYPGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1279 FIFSGtfrmnldpygqwndEEIWKVAEevglkSVIEQfpgQLDFVL-------VDGgcvLSHGHKQLMCLARSVLSRAKI 1351
Cdd:cd03233 85 IIYVS--------------EEDVHFPT-----LTVRE---TLDFALrckgnefVRG---ISGGERKRVSIAEALVSRASV 139
|
170 180
....*....|....*....|....
gi 1631900066 1352 LLLDEPSAHLDPVTSQVIRKTLKH 1375
Cdd:cd03233 140 LCWDNSTRGLDSSTALEILKCIRT 163
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1212-1363 |
1.75e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 48.47 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1212 LENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLNTE------GDIQIDGVSWNTVSVQQWRKAFGVIPQ--KVFIFSG 1283
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISEtgqtivGDYAIPANLKKIKEVKRLRKEIGLVFQfpEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1284 TFRMNLdPYGQ----WNDEEIWK-VAEEVGLKSVIEQFPGQLDFVLvdggcvlSHGHKQLMCLARSVLSRAKILLLDEPS 1358
Cdd:PRK13645 107 TIEKDI-AFGPvnlgENKQEAYKkVPELLKLVQLPEDYVKRSPFEL-------SGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
....*
gi 1631900066 1359 AHLDP 1363
Cdd:PRK13645 179 GGLDP 183
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1212-1392 |
2.03e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 48.87 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1212 LENISFSIDSGQRVGLLGRTGSGKSTL---LFAFLRLlnTEGDIQIDGvswNTVSVQQWRKAF----GVIPQKvfiFS-- 1282
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLmkiLYGLYQP--DSGEILIDG---KPVRIRSPRDAIalgiGMVHQH---FMlv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1283 --------------GTFRMNLDpygqWND--EEIWKVAEEVGLK----SVIEQfpgqldfvlvdggcvLSHGHKQ----L 1338
Cdd:COG3845 93 pnltvaenivlglePTKGGRLD----RKAarARIRELSERYGLDvdpdAKVED---------------LSVGEQQrveiL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1631900066 1339 MCLARsvlsRAKILLLDEPSAHLDP--VTS--QVIRKtLKHafANCTVILSEHRL-EAM 1392
Cdd:COG3845 154 KALYR----GARILILDEPTAVLTPqeADElfEILRR-LAA--EGKSIIFITHKLrEVM 205
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1212-1369 |
2.10e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.08 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1212 LENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLNT-EGDIQIDGVSWNTVSVQQWRKAFGVIPqkvFIFSGTFrMNLD 1290
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESqGGEIIFNGQRIDTLSPGKLQALRRDIQ---FIFQDPY-ASLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1291 P--------------YGQWNDEEIWK-VA---EEVGLKSVIE-QFPGQldfvlvdggcvLSHGHKQLMCLARSVLSRAKI 1351
Cdd:PRK10261 416 PrqtvgdsimeplrvHGLLPGKAAAArVAwllERVGLLPEHAwRYPHE-----------FSGGQRQRICIARALALNPKV 484
|
170
....*....|....*....
gi 1631900066 1352 LLLDEPSAHLD-PVTSQVI 1369
Cdd:PRK10261 485 IIADEAVSALDvSIRGQII 503
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
417-642 |
2.41e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 48.63 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 417 PLHAspvLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGR--------------ISFSPQ-VSWIM 481
Cdd:PRK09700 17 PVHA---LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInynkldhklaaqlgIGIIYQeLSVID 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 482 PGTIKENIIFG------------VSYDEYRYKSVI--KACQLEEDISKFPEKdytvlgeggiiLSGGQRARISLARAVYK 547
Cdd:PRK09700 94 ELTVLENLYIGrhltkkvcgvniIDWREMRVRAAMmlLRVGLKVDLDEKVAN-----------LSISHKQMLEIAKTLML 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 548 DADLYLLDSPFGHLdifTEKEI---FescvckLMANKTR------ILVTSKL-EHLKIADKILILHEGSCYFYGTFSELQ 617
Cdd:PRK09700 163 DAKVIIMDEPTSSL---TNKEVdylF------LIMNQLRkegtaiVYISHKLaEIRRICDRYTVMKDGSSVCSGMVSDVS 233
|
250 260
....*....|....*....|....*
gi 1631900066 618 GQrpDFSSELMGFDSFDQFSAERRN 642
Cdd:PRK09700 234 ND--DIVRLMVGRELQNRFNAMKEN 256
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
422-557 |
2.47e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 48.48 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGR-ISF-SPQVSW------------IMPG-TIK 486
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpVRFrSPRDAQaagiaiihqelnLVPNlSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 487 ENIIFGvsyDEYR------YKSVIKACQ-----LEEDISkfPEkdyTVLGEggiiLSGGQRARISLARAVYKDADLYLLD 555
Cdd:COG1129 98 ENIFLG---REPRrgglidWRAMRRRARellarLGLDID--PD---TPVGD----LSVAQQQLVEIARALSRDARVLILD 165
|
..
gi 1631900066 556 SP 557
Cdd:COG1129 166 EP 167
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1195-1401 |
2.76e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.18 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1195 MTVKDLTAKYG--EGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLNTEGDI----QIDGVSWNTVSVQQWR 1268
Cdd:PRK09473 13 LDVKDLRVTFStpDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIggsaTFNGREILNLPEKELN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1269 KAFGviPQKVFIFSGTFrMNLDPYGQWNDE--EIWKVAEEVGLKSVIEQFPGQLDFVLVDGG--------CVLSHGHKQL 1338
Cdd:PRK09473 93 KLRA--EQISMIFQDPM-TSLNPYMRVGEQlmEVLMLHKGMSKAEAFEESVRMLDAVKMPEArkrmkmypHEFSGGMRQR 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1631900066 1339 MCLARSVLSRAKILLLDEPSAHLDpVTSQVIRKT----LKHAFaNCTVILSEHRLEAMLE-CQRFLVI 1401
Cdd:PRK09473 170 VMIAMALLCRPKLLIADEPTTALD-VTVQAQIMTllneLKREF-NTAIIMITHDLGVVAGiCDKVLVM 235
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
424-607 |
2.96e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 48.04 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 424 LQDINFRIEKGQLLAVSGSTGAGKTSL---LMMImgElEPSQGKIKHSGRISFSPQvswimPGTIKE-----NIIFGVSY 495
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLarlLTMI--E-TPTGGELYYQGQDLLKAD-----PEAQKLlrqkiQIVFQNPY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 496 DEYRYKSVIKAcQLEE------DISKFP--EKDYTVLGEGGI----------ILSGGQRARISLARAVYKDADLYLLDSP 557
Cdd:PRK11308 103 GSLNPRKKVGQ-ILEEpllintSLSAAErrEKALAMMAKVGLrpehydryphMFSGGQRQRIAIARALMLDPDVVVADEP 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1631900066 558 FGHLDIFTEKEifescVCKLMANKTRILVTSKL---------EHlkIADKILILHEGSC 607
Cdd:PRK11308 182 VSALDVSVQAQ-----VLNLMMDLQQELGLSYVfishdlsvvEH--IADEVMVMYLGRC 233
|
|
| urea_trans_UrtD |
TIGR03411 |
urea ABC transporter, ATP-binding protein UrtD; Members of this protein family are ABC ... |
1197-1390 |
3.29e-05 |
|
urea ABC transporter, ATP-binding protein UrtD; 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: 274568 [Multi-domain] Cd Length: 242 Bit Score: 47.17 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKYGegGAAVLENISFSIDSGQ-RVgLLGRTGSGKSTLLFAFL-RLLNTEGDIQIDGVSWNTVSVQQ------WR 1268
Cdd:TIGR03411 5 LEGLSVSFD--GFKALNDLSLYVDPGElRV-IIGPNGAGKTTMMDVITgKTRPDEGSVLFGGTDLTGLPEHQiaragiGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1269 KaFgvipQKVFIFSG-TFRMNLD-----PYGQWN----------DEEIWKVAEEVGLKSVIEQFPGqldfvlvdggcVLS 1332
Cdd:TIGR03411 82 K-F----QKPTVFENlTVFENLElalprDKSVFAslffrlsaeeKDRIEEVLETIGLADEADRLAG-----------LLS 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 1333 HGHKQLMCLARSVLSRAKILLLDEPSAHLdpvTSQVIRKT---LKHAFANCTVILSEHRLE 1390
Cdd:TIGR03411 146 HGQKQWLEIGMLLMQDPKLLLLDEPVAGM---TDEETEKTaelLKSLAGKHSVVVVEHDME 203
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1196-1258 |
3.50e-05 |
|
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: 46.37 E-value: 3.50e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1631900066 1196 TVKDLTAKYGEGgaAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFL---RLLNTEGDIQIDGVS 1258
Cdd:cd03217 2 EIKDLHVSVGGK--EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghpKYEVTEGEILFKGED 65
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1210-1362 |
4.45e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 47.13 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1210 AVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFL---------RLLNTEGDIQIDGVSWNTVSVQQWRKAFGVIPQ---K 1277
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgdltgggapRGARVTGDVTLNGEPLAAIDAPRLARLRAVLPQaaqP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1278 VFIFSGTFRMNLDPY--------GQWNDEEI-WKVAEEVGLKSVIEQFPGQL---DFVLVDGGCVLSHGHKqlmclARSV 1345
Cdd:PRK13547 95 AFAFSAREIVLLGRYpharragaLTHRDGEIaWQALALAGATALVGRDVTTLsggELARVQFARVLAQLWP-----PHDA 169
|
170
....*....|....*..
gi 1631900066 1346 LSRAKILLLDEPSAHLD 1362
Cdd:PRK13547 170 AQPPRYLLLDEPTAALD 186
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
405-594 |
4.53e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 46.73 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 405 PSTDNNLFFSnfplhaspvLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGRISfspqVSWIMPG- 483
Cdd:PRK13546 30 PKHKNKTFFA---------LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVS----VIAISAGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 484 ----TIKENIIFGVSYDEYRYKS-------VIKACQLEEDISKfPEKDYtvlgeggiilSGGQRARISLARAVYKDADLY 552
Cdd:PRK13546 97 sgqlTGIENIEFKMLCMGFKRKEikamtpkIIEFSELGEFIYQ-PVKKY----------SSGMRAKLGFSINITVNPDIL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1631900066 553 LLDSPFGHLD-IFTEKeifesCVCKLM----ANKTRILVTSKLEHLK 594
Cdd:PRK13546 166 VIDEALSVGDqTFAQK-----CLDKIYefkeQNKTIFFVSHNLGQVR 207
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1197-1406 |
7.60e-05 |
|
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: 47.10 E-value: 7.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKY---GEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQID-GVSW---------NTV 1262
Cdd:TIGR03269 282 VRNVSKRYisvDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEpTSGEVNVRvGDEWvdmtkpgpdGRG 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1263 SVQQW----RKAFGVIPQKVFIFSGTFRMNL---DPYGQWNDEEIWKVA--EEVGLKSVIEQFPGQLdfvlvdggcvlSH 1333
Cdd:TIGR03269 362 RAKRYigilHQEYDLYPHRTVLDNLTEAIGLelpDELARMKAVITLKMVgfDEEKAEEILDKYPDEL-----------SE 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1631900066 1334 GHKQLMCLARSVLSRAKILLLDEPSAHLDPVTSQVIRKTLKHAFA--NCTVILSEHRLEAMLE-CQRFLVIEDNKL 1406
Cdd:TIGR03269 431 GERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKI 506
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
915-1083 |
8.45e-05 |
|
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: 46.28 E-value: 8.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 915 AMGIFRGLPLVHTLITVSKTLHQKMVHAVLHAPMSTFNSWKAGGMLNRFaKDTAVLDDLLPLTVFD-FVQLILIVIGAIT 993
Cdd:cd18570 57 LLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISSTTISlFLDLLMVIISGII 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 994 VVSIlQPYIFLASVPVIA--AFIVLRAYFLHTSQQLKQLESEARSPifTHLVTSLKGLWTLRAFGRQPYF----ETLFHK 1067
Cdd:cd18570 136 LFFY-NWKLFLITLLIIPlyILIILLFNKPFKKKNREVMESNAELN--SYLIESLKGIETIKSLNAEEQFlkkiEKKFSK 212
|
170
....*....|....*...
gi 1631900066 1068 ALN--LHTANWFLYLSTL 1083
Cdd:cd18570 213 LLKksFKLGKLSNLQSSI 230
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
894-1070 |
9.83e-05 |
|
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: 46.01 E-value: 9.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 894 VTDTSAYYIIYIYVgvADTLLAMgiFRGLPLVHTLITVSKTLHQKMVHAVLHAPMSTFNSWKAGGMLNRFAKDTAVLDDL 973
Cdd:cd18557 34 VLNELALILLAIYL--LQSVFTF--VRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 974 LPLTVFDFVQLILIVIGAITVVSILQPYIFLASVPVIAAFIVLRAYFLHTSQQLKQLESEARSPIFTHLVTSLKGLWTLR 1053
Cdd:cd18557 110 VTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVR 189
|
170
....*....|....*..
gi 1631900066 1054 AFGRQPYFETLFHKALN 1070
Cdd:cd18557 190 SFSAEEKEIRRYSEALD 206
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
411-565 |
1.07e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.87 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 411 LFFSNFPLhaspvLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGRISFS------PQVswiMPGT 484
Cdd:PRK11147 11 LSFSDAPL-----LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVArlqqdpPRN---VEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 485 IKENIIFGVS--------Y--------DEYRYKSVIKACQLEEDIS-----KFPEKDYTVLGEGGI-------ILSGGQR 536
Cdd:PRK11147 83 VYDFVAEGIEeqaeylkrYhdishlveTDPSEKNLNELAKLQEQLDhhnlwQLENRINEVLAQLGLdpdaalsSLSGGWL 162
|
170 180
....*....|....*....|....*....
gi 1631900066 537 ARISLARAVYKDADLYLLDSPFGHLDIFT 565
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
416-465 |
1.45e-04 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 45.84 E-value: 1.45e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1631900066 416 FPLHASPV--LQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGeLE-PSQGKI 465
Cdd:COG1135 11 FPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL-LErPTSGSV 62
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
80-280 |
1.63e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 45.22 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 80 VQPLLLGRIIASYDPDNSDERSIaYYLGIGLCLLFLVRTLLIHPAIFGLHHIGMQMRIAMFSLIYKKILKLSSRVLDKIS 159
Cdd:cd18778 17 VPPWLIRELVDLVTIGSKSLGLL-LGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLYDKLQRLSLRYFDDRQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 160 TGQLVSLLSNNLNKFDegLALAH----FVwIAPLQV----ALLMGLLWdMLEASAFSGLAFLIVLAFFQAWLGQMMMKYR 231
Cdd:cd18778 96 TGDLMSRVINDVANVE--RLIADgipqGI-TNVLTLvgvaIILFSINP-KLALLTLIPIPFLALGAWLYSKKVRPRYRKV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1631900066 232 NKRAGKINERLVitsEIIENIQSVKAYCWEDA----MEKMIESIRETELKLTR 280
Cdd:cd18778 172 REALGELNALLQ---DNLSGIREIQAFGREEEeakrFEALSRRYRKAQLRAMK 221
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
431-620 |
1.66e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.32 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 431 IEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGkikhsgriSFSPQVSWIMPGTIKENIIFGVSYDEYRYKSVIKACQLE 510
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGG--------SYTFPGNWQLAWVNQETPALPQPALEYVIDGDREYRQLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 511 EDISKFPEKD-----------------YTVLGEGGIIL-----------------SGGQRARISLARAVYKDADLYLLDS 556
Cdd:PRK10636 96 AQLHDANERNdghaiatihgkldaidaWTIRSRAASLLhglgfsneqlerpvsdfSGGWRMRLNLAQALICRSDLLLLDE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 557 PFGHLD----IFTEKEIFEScvcklmaNKTRILVTSKLEHLK-IADKILILHEGSCYFY-GTFSELQGQR 620
Cdd:PRK10636 176 PTNHLDldavIWLEKWLKSY-------QGTLILISHDRDFLDpIVDKIIHIEQQSLFEYtGNYSSFEVQR 238
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
424-465 |
1.82e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 45.56 E-value: 1.82e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1631900066 424 LQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKI 465
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRV 62
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
938-1072 |
1.97e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 45.14 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 938 KMVHAVLHAPMSTF----NSwkAGGMLNRFAKDTAVLDDLLPLTVFDFVQLILIVIGAItVVSIlqpyIF--------LA 1005
Cdd:cd18578 90 LAFRAILRQDIAWFddpeNS--TGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGL-IIAF----VYgwklalvgLA 162
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1631900066 1006 SVPVIAAFIVLRAYFLHTSQQLKQLESEARSPIFTHLVTSLKglwTLRAFGRQPYFETLFHKALNLH 1072
Cdd:cd18578 163 TVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIR---TVASLTLEDYFLEKYEEALEEP 226
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
144-270 |
2.32e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 44.86 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 144 YKKILKLSSRVLDKISTGQLVSLLS---NNLNKF-DEGL------------ALAHFVWIAPlQVALLmgllwdmleasAF 207
Cdd:cd18565 94 YDHVQRLDMAFFEDRQTGDLMSVLNndvNQLERFlDDGAnsiirvvvtvlgIGAILFYLNW-QLALV-----------AL 161
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1631900066 208 SGLAFLIVLAF-FQAWLGQmmmKYRNKR--AGKINERLvitSEIIENIQSVKAYCWEDAMEKMIES 270
Cdd:cd18565 162 LPVPLIIAGTYwFQRRIEP---RYRAVReaVGDLNARL---ENNLSGIAVIKAFTAEDFERERVAD 221
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1195-1256 |
2.36e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 44.53 E-value: 2.36e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1631900066 1195 MTVKDLTAKYGEGGAavLENISFSIDSGQRVGLLGRTGSGKSTLLFAF-LRLLNTEGDIQIDG 1256
Cdd:PRK11701 7 LSVRGLTKLYGPRKG--CRDVSFDLYPGEVLGIVGESGSGKTTLLNALsARLAPDAGEVHYRM 67
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
426-565 |
2.67e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.49 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 426 DINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKhsgrisfspqvswiMPGTIKeniifgVSY-DEYR----- 499
Cdd:PRK11819 342 DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK--------------IGETVK------LAYvDQSRdaldp 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 500 YKSVIkacqleEDISKfpEKDYTVLGEGGI---------------------ILSGGQRARISLARAVYKDADLYLLDSPF 558
Cdd:PRK11819 402 NKTVW------EEISG--GLDIIKVGNREIpsrayvgrfnfkggdqqkkvgVLSGGERNRLHLAKTLKQGGNVLLLDEPT 473
|
....*..
gi 1631900066 559 GHLDIFT 565
Cdd:PRK11819 474 NDLDVET 480
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
532-603 |
2.74e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.62 E-value: 2.74e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1631900066 532 SGGQRARISLARAVYKDADLYLLDSPFGHLDIFTEKEIfESCVCKLmaNKTRILVTSKLEHLK-IADKILILH 603
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWL-ETYLLKW--PKTFIVVSHAREFLNtVVTDILHLH 415
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
424-605 |
3.25e-04 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 45.20 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 424 LQDINFRIEKGQLLAVSGSTGAGKtSLLMMIMGELEPS---QGKIKHSGR--------------ISFSPQVSWIMPG-TI 485
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGK-STLMKILSGVYPHgtwDGEIYWSGSplkasnirdteragIVIIHQELTLVPElSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 486 KENIIFG---------VSYDE--YRYKSVIKACQLEEDISKFPEKDYtvlgeggiilSGGQRARISLARAVYKDADLYLL 554
Cdd:TIGR02633 96 AENIFLGneitlpggrMAYNAmyLRAKNLLRELQLDADNVTRPVGDY----------GGGQQQLVEIAKALNKQARLLIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1631900066 555 DSPFGHLdifTEKE--IFESCVCKLMA-NKTRILVTSKLEHLK-IADKILILHEG 605
Cdd:TIGR02633 166 DEPSSSL---TEKEteILLDIIRDLKAhGVACVYISHKLNEVKaVCDTICVIRDG 217
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1184-1369 |
4.03e-04 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 44.31 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1184 KEEKNWPSGGKMTVKdltakygeggaAVlENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTV 1262
Cdd:PRK15079 21 KDGKQWFWQPPKTLK-----------AV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKaTDGEVAWLGKDLLGM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1263 SVQQWRKAFGVIpQKVF---IFSGTFRMNL-----DP----YGQWNDEEIW-KVAE---EVGL-KSVIEQFPGQLdfvlv 1325
Cdd:PRK15079 89 KDDEWRAVRSDI-QMIFqdpLASLNPRMTIgeiiaEPlrtyHPKLSRQEVKdRVKAmmlKVGLlPNLINRYPHEF----- 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1631900066 1326 dggcvlSHGHKQLMCLARSVLSRAKILLLDEPSAHLD-PVTSQVI 1369
Cdd:PRK15079 163 ------SGGQCQRIGIARALILEPKLIICDEPVSALDvSIQAQVV 201
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1194-1256 |
4.32e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 44.45 E-value: 4.32e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1631900066 1194 KMTVKDLTAKYgEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLlfafLRLLN-----TEGDIQIDG 1256
Cdd:PRK11650 3 GLKLQAVRKSY-DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTL----LRMVAgleriTSGEIWIGG 65
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
425-601 |
5.07e-04 |
|
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: 43.03 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 425 QDINFR-IEKGQLLAVSGSTGAGKTSLLMMIMGEL------EPSQGK---IKHSG----RISFSPQVSWIMPGTIKEnii 490
Cdd:cd03279 18 QVIDFTgLDNNGLFLICGPTGAGKSTILDAITYALygktprYGRQENlrsVFAPGedtaEVSFTFQLGGKKYRVERS--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 491 FGVSYDEYRyKSVIKAcqlEEDISKFPEKDYTVlgeggiiLSGGQRARISLARAVY----------KDADLYLLDSPFGH 560
Cdd:cd03279 95 RGLDYDQFT-RIVLLP---QGEFDRFLARPVST-------LSGGETFLASLSLALAlsevlqnrggARLEALFIDEGFGT 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1631900066 561 LDIfTEKEIFESCVCKLMANKTRILVTSKLEHLK--IADKILI 601
Cdd:cd03279 164 LDP-EALEAVATALELIRTENRMVGVISHVEELKerIPQRLEV 205
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1197-1275 |
5.23e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 44.25 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 1197 VKDLTAKyGEGGAAVLENISFSIDSGQRVGLLGRTGSGKSTLLFAFLRLLN-TEGDIQIDGVSWNTVSVQQWRKA-FGVI 1274
Cdd:COG3845 260 VENLSVR-DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPpASGSIRLDGEDITGLSPRERRRLgVAYI 338
|
.
gi 1631900066 1275 P 1275
Cdd:COG3845 339 P 339
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1197-1256 |
7.58e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.11 E-value: 7.58e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1631900066 1197 VKDLTAKYGEGG-AAVLENISFSIDSGQRVGLLGRTGSGKSTL--LFAFLRLLNtEGDIQIDG 1256
Cdd:PRK13545 24 LKDLFFRSKDGEyHYALNNISFEVPEGEIVGIIGLNGSGKSTLsnLIAGVTMPN-KGTVDIKG 85
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
879-1069 |
9.76e-04 |
|
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: 43.03 E-value: 9.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 879 ATQSENSTsdkppvivtdTSAYYIIYIYVGVADTLLAMGIFRGLplvhTLITVSKTLHQKMVHAVLHAPMSTFNSWKAGG 958
Cdd:cd18558 52 EKLEEEMT----------LYAYYYLIIGAIVLITAYIQGSFWGL----AAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 959 MLNRFAKDTAVLDDLLPLTVFDFVQLILIVIGAItVVSILQPY----IFLASVPVIAAFIVLRAYFLhTSQQLKQLESEA 1034
Cdd:cd18558 118 LNTRLADDVSKINEGIGDKIGVIFQNIATFGTGF-IIGFIRGWkltlVILAISPVLGLSAVVWAKIL-SGFTDKEKKAYA 195
|
170 180 190
....*....|....*....|....*....|....*.
gi 1631900066 1035 RS-PIFTHLVTSLKglwTLRAFGRQPYFETLFHKAL 1069
Cdd:cd18558 196 KAgAVAEEVLEAFR---TVIAFGGQQKEETRYAQNL 228
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
80-285 |
1.10e-03 |
|
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: 42.81 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 80 VQPLLLGRIIasydpDNSDERSIAYYLGIGLCLLFLVRTLLIHPAIFGLHHIGMQMriaMFSL---IYKKILKLSSRVLD 156
Cdd:cd18551 17 AQPLLVKNLI-----DALSAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTGERV---VLDLrrrLWRRLLRLPVSFFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 157 KISTGQLVSLLSNNLNKFDEGLA--LAHFVwIAPLQVA---LLMGLL-WDMLeasAFSGLAFLIVLAFFqAWLGQMMMKY 230
Cdd:cd18551 89 RRRSGDLVSRVTNDTTLLRELITsgLPQLV-TGVLTVVgavVLMFLLdWVLT---LVTLAVVPLAFLII-LPLGRRIRKA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1631900066 231 RNK---RAGKINERLvitSEIIENIQSVKAYCWED----AMEKMIESIRETELKLTRKAAYV 285
Cdd:cd18551 164 SKRaqdALGELSAAL---ERALSAIRTVKASNAEEretkRGGEAAERLYRAGLKAAKIEALI 222
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
432-564 |
1.22e-03 |
|
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: 43.23 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 432 EKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKI-----------KHSG---------------RISFSPQ-VSWImP-- 482
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdevlkRFRGtelqdyfkklangeiKVAHKPQyVDLI-Pkv 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 483 --GTIKENIifgVSYDEY-RYKSVIKACQLEE----DISKfpekdytvlgeggiiLSGGQRARISLARAVYKDADLYLLD 555
Cdd:COG1245 176 fkGTVRELL---EKVDERgKLDELAEKLGLENildrDISE---------------LSGGELQRVAIAAALLRDADFYFFD 237
|
....*....
gi 1631900066 556 SPFGHLDIF 564
Cdd:COG1245 238 EPSSYLDIY 246
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
431-564 |
1.29e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.26 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 431 IEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGK----------IKH-SG---------------RISFSPQVSWIMP-- 482
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDyeeepswdevLKRfRGtelqnyfkklyngeiKVVHKPQYVDLIPkv 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 483 --GTIKENIIfgvSYDEY-RYKSVIKACQLEE----DISKfpekdytvlgeggiiLSGGQRARISLARAVYKDADLYLLD 555
Cdd:PRK13409 176 fkGKVRELLK---KVDERgKLDEVVERLGLENildrDISE---------------LSGGELQRVAIAAALLRDADFYFFD 237
|
....*....
gi 1631900066 556 SPFGHLDIF 564
Cdd:PRK13409 238 EPTSYLDIR 246
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1197-1239 |
1.52e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.19 E-value: 1.52e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1631900066 1197 VKDLTAKYGEGGAavLENISFSIDSGQRVGLLGRTGSGKSTLL 1239
Cdd:NF033858 4 LEGVSHRYGKTVA--LDDVSLDIPAGCMVGLIGPDGVGKSSLL 44
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
73-283 |
2.13e-03 |
|
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: 41.70 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 73 LGEVTKSVQPLLLGRIIasydpDN----SDERSIAYY----LGIGL---CLLFLVRTLLIHPAifglHHIGMQMRIAmfs 141
Cdd:cd18543 10 LATLAGLAIPLLTRRAI-----DGpiahGDRSALWPLvlllLALGVaeaVLSFLRRYLAGRLS----LGVEHDLRTD--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 142 lIYKKILKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLlwdMLEASAFSGLAFLIVLAFFqA 221
Cdd:cd18543 78 -LFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPFLLGNLLTLVVGLVV---MLVLSPPLALVALASLPPL-V 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1631900066 222 WLGqmmMKYRNK----------RAGKinerlvITSEIIENIQS---VKAYCWEDAM----EKMIESIRETELKLTRKAA 283
Cdd:cd18543 153 LVA---RRFRRRyfpasrraqdQAGD------LATVVEESVTGirvVKAFGRERREldrfEAAARRLRATRLRAARLRA 222
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
82-266 |
2.23e-03 |
|
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: 41.62 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 82 PLLLGRIIASYDPDNSDERSIAYYLGIGLCLLFLVRTLLIhpAIFGL----------HHIGMQMRIAMFsliyKKILKLS 151
Cdd:cd18547 19 PYLLGKAIDLIIEGLGGGGGVDFSGLLRILLLLLGLYLLS--ALFSYlqnrlmarvsQRTVYDLRKDLF----EKLQRLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 152 SRVLDKISTGQLVSLLSNNLNKFDEGL--ALAHFVwiapLQVALLMGLLWDMLEAS---AFSGLAFLIVLAFFQAWLGQM 226
Cdd:cd18547 93 LSYFDTHSHGDIMSRVTNDVDNISQALsqSLTQLI----SSILTIVGTLIMMLYISpllTLIVLVTVPLSLLVTKFIAKR 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1631900066 227 MMKYRNKRA---GKINErlvITSEIIENIQSVKAYCWEDAMEK 266
Cdd:cd18547 169 SQKYFRKQQkalGELNG---YIEEMISGQKVVKAFNREEEAIE 208
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
424-555 |
2.53e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 40.63 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 424 LQDINFRIEKGQLLAVS------------GSTGAGKTSLLMMIMGELEPSQGKIK-HSGRIS--FSPQVSWI-------M 481
Cdd:PRK13541 4 LHQLQFNIEQKNLFDLSitflpsaityikGANGCGKSSLLRMIAGIMQPSSGNIYyKNCNINniAKPYCTYIghnlglkL 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1631900066 482 PGTIKENIIFGVSYdeyrYKSVIkacQLEEDISKFpeKDYTVLGEGGIILSGGQRARISLARAVYKDADLYLLD 555
Cdd:PRK13541 84 EMTVFENLKFWSEI----YNSAE---TLYAAIHYF--KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLD 148
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
422-605 |
2.74e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.02 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 422 PVLQDINFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSGR------------------------------- 470
Cdd:PRK10982 262 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKkinnhnaneainhgfalvteerrstgiyayl 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 471 -ISFSPQVSWIMPGTIKeniiFGVsYDEYRYKS----VIKACQLeedisKFPEKdYTVLGEggiiLSGGQRARISLARAV 545
Cdd:PRK10982 342 dIGFNSLISNIRNYKNK----VGL-LDNSRMKSdtqwVIDSMRV-----KTPGH-RTQIGS----LSGGNQQKVIIGRWL 406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1631900066 546 YKDADLYLLDSPFGHLDIFTEKEIFESCVCKLMANKTRILVTSKL-EHLKIADKILILHEG 605
Cdd:PRK10982 407 LTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMpELLGITDRILVMSNG 467
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
427-555 |
8.18e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 40.73 E-value: 8.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 427 INFRIEKGQLLAVSGSTGAGKTSLLMMIMGELEPSQGKIKHSG-----------RISFSPQVS--WIMPGTIKENiifGV 493
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGkpvtaeqpedyRKLFSAVFTdfHLFDQLLGPE---GK 418
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1631900066 494 SYDEYRYKSVIKACQLEEdisKFPEKDYTVLgegGIILSGGQRARISLARAVYKDADLYLLD 555
Cdd:PRK10522 419 PANPALVEKWLERLKMAH---KLELEDGRIS---NLKLSKGQKKRLALLLALAEERDILLLD 474
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
892-1054 |
9.90e-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: 350055 [Multi-domain] Cd Length: 294 Bit Score: 39.88 E-value: 9.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 892 VIVT-DTSAYYIIYIYVGVADTLLAM-GIFRGLPLVHTLITVSKTLHQKMVHAVLHAPMSTFNSWKAGGMLNR------- 962
Cdd:cd18782 32 VLVQqDLATLYVIGVVMLVAALLEAVlTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRiseldti 111
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1631900066 963 --FAKDTAvlddllpLTVFDFVQLILIVIGAITVVSILQPYIFLASVPVIAAFIVLRAYFLhtsQQLKQLESEARSPIFT 1040
Cdd:cd18782 112 rgFLTGTA-------LTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPIL---RRQIRRRAEASAKTQS 181
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170
....*....|....
gi 1631900066 1041 HLVTSLKGLWTLRA 1054
Cdd:cd18782 182 YLVESLTGIQTVKA 195
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