|
Name |
Accession |
Description |
Interval |
E-value |
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
125-709 |
0e+00 |
|
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: 878.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 125 LSYVWPKDRPDLRARVAISLGFLGGAKAMNIVVPFMFKYAVDslnqmsgnmlNLSDAPNTVATMATAVLIGYGVSRAGAA 204
Cdd:COG5265 23 LLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAID----------ALLSGAAALLVVPVGLLLAYGLLRLLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 205 FFNEVRNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIVFEMTLVSSV 284
Cdd:COG5265 93 LFGELRDALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGGLSRDIERGTKGIEFLLRFLLFNILPTLLEIALVAGI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 285 LYYKCGAQFALVTLGTLGAYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNEKYEAQRYDGFLKTYE 364
Cdd:COG5265 173 LLVKYDWWFALITLVTVVLYIAFTVVVTEWRTKFRREMNEADSEANTRAVDSLLNYETVKYFGNEAREARRYDEALARYE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 365 TASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGALTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 444
Cdd:COG5265 253 RAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVYREIRQALADMERM 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 445 FTLLKVDTRIKDKAMASPLQITPqtATVAFDNVHFEYIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEP 524
Cdd:COG5265 333 FDLLDQPPEVADAPDAPPLVVGG--GEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDV 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 525 QKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNINASPEEVYAVAKLAGLHDAILRMPHGYDTQVGE 604
Cdd:COG5265 411 TSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGE 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 605 RGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIFIAHRLSTVVDADEIIVLSQGKV 684
Cdd:COG5265 491 RGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRI 570
|
570 580
....*....|....*....|....*
gi 47058990 685 AERGTHYGLLAnSSSIYSEMWHTQS 709
Cdd:COG5265 571 VERGTHAELLA-QGGLYAQMWARQQ 594
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
116-709 |
1.98e-179 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 525.50 E-value: 1.98e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 116 DTRKIIKAMLSYVWPkdrpdLRARVAISLGFLGGAKAMNIVVPFMFKYAVDSLnqmsgnmlnLSDAPNTVATMATAVLIG 195
Cdd:COG1132 4 SPRKLLRRLLRYLRP-----YRGLLILALLLLLLSALLELLLPLLLGRIIDAL---------LAGGDLSALLLLLLLLLG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 196 YGVSRAGAAFFnevRNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIV 275
Cdd:COG1132 70 LALLRALLSYL---QRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 276 FEMTLVSSVLYYKcGAQFALVTLGTLGAYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNEKYEAQR 355
Cdd:COG1132 147 VTLIGALVVLFVI-DWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELER 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 356 YDGFLKTYETASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGALTVGDLVMVNGLLFQLSLPLNFLGTVYRETR 435
Cdd:COG1132 226 FREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 436 QALIDMNTLFTLLKVDTRIKDKAMASPLqiTPQTATVAFDNVHFEYIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIV 515
Cdd:COG1132 306 RALASAERIFELLDEPPEIPDPPGAVPL--PPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 516 RLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNINASPEEVYAVAKLAGLHDAILRMP 595
Cdd:COG1132 384 NLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 596 HGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIFIAHRLSTVVDADE 675
Cdd:COG1132 464 DGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADR 543
|
570 580 590
....*....|....*....|....*....|....
gi 47058990 676 IIVLSQGKVAERGTHYGLLANsSSIYSEMWHTQS 709
Cdd:COG1132 544 ILVLDDGRIVEQGTHEELLAR-GGLYARLYRLQF 576
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
143-444 |
5.49e-166 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 479.69 E-value: 5.49e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 143 SLGFLGGAKAMNIVVPFMFKYAVDSLnqmsgnmlnlSDAPNTVATMATAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSI 222
Cdd:cd18582 1 ALLLLVLAKLLNVAVPFLLKYAVDAL----------SAPASALLAVPLLLLLAYGLARILSSLFNELRDALFARVSQRAV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 223 RRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIVFEMTLVSSVLYYKCGAQFALVTLGTLG 302
Cdd:cd18582 71 RRLALRVFRHLHSLSLRFHLSRKTGALSRAIERGTRGIEFLLRFLLFNILPTILELLLVCGILWYLYGWSYALITLVTVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 303 AYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNEKYEAQRYDGFLKTYETASLKSTSTLAMLNFGQS 382
Cdd:cd18582 151 LYVAFTIKVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQA 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47058990 383 AIFSVGLTAIMVLASQGIVAGALTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 444
Cdd:cd18582 231 LIISLGLTAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFLGFVYREIRQSLIDMEKL 292
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
472-708 |
2.78e-142 |
|
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: 417.02 E-value: 2.78e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVV 551
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 552 PQDAVLFHNTIYYNLLYGNINASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVIL 631
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47058990 632 YDEATSSLDSITEETILGAMRDVVKHRTSIFIAHRLSTVVDADEIIVLSQGKVAERGTHYGLLAnSSSIYSEMWHTQ 708
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLA-KGGLYAEMWKAQ 236
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
71-708 |
2.11e-137 |
|
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: 421.94 E-value: 2.11e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 71 KNNSRQLLDASKVLQAWPLIEKRTCWHGHAgggLHTDPKEGLKDVDTRKI-IKAMLSYVWPkDRPDLRArvAISLGFLGG 149
Cdd:COG2274 96 DGDKVTIADPATGRRKLSLEEFAESWTGVA---LLLEPTPEFDKRGEKPFgLRWFLRLLRR-YRRLLLQ--VLLASLLIN 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 150 AkaMNIVVPFMFKYAVDSLnqMSGNMLNlsdapnTVATMATAVLIGYGVSragaAFFNEVRNAVFGKVAQNSIRRIAKNV 229
Cdd:COG2274 170 L--LALATPLFTQVVIDRV--LPNQDLS------TLWVLAIGLLLALLFE----GLLRLLRSYLLLRLGQRIDLRLSSRF 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 230 FLHLHNLDLGFHLSRQTGALSKAIdRGTRGI-SFVLSALVFNLLPIVFemTLVSSVL--YYkcGAQFALVTLGTLGAYTA 306
Cdd:COG2274 236 FRHLLRLPLSFFESRSVGDLASRF-RDVESIrEFLTGSLLTALLDLLF--VLIFLIVlfFY--SPPLALVVLLLIPLYVL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 307 FTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNEKYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAIFS 386
Cdd:COG2274 311 LGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQ 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 387 VGLTAIMVLASQGIVAGALTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTLFTLLkvDTRIKDKAMASPLQIT 466
Cdd:COG2274 391 LATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDIL--DLPPEREEGRSKLSLP 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 467 PQTATVAFDNVHFEYIE-GQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLR 545
Cdd:COG2274 469 RLKGDIELENVSFRYPGdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLR 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 546 RAVGVVPQDAVLFHNTIYYNLLYGNINASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILK 625
Cdd:COG2274 549 RQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLR 628
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 626 DPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIFIAHRLSTVVDADEIIVLSQGKVAERGTHYGLLANsSSIYSEMW 705
Cdd:COG2274 629 NPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR-KGLYAELV 707
|
...
gi 47058990 706 HTQ 708
Cdd:COG2274 708 QQQ 710
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
472-705 |
5.16e-101 |
|
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: 310.32 E-value: 5.16e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYI-EGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGV 550
Cdd:cd03251 1 VEFKNVTFRYPgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 551 VPQDAVLFHNTIYYNLLYGNINASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVI 630
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47058990 631 LYDEATSSLDSITEETILGAMRDVVKHRTSIFIAHRLSTVVDADEIIVLSQGKVAERGTHYGLLAnSSSIYSEMW 705
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLA-QGGVYAKLH 234
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
143-444 |
2.01e-99 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 308.77 E-value: 2.01e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 143 SLGFLGGAKAMNIVVPFMFKYAVDSLnqmsgnmlnlSDAPNTVATMATAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSI 222
Cdd:cd18560 1 SLLLLILGKACNVLAPLFLGRAVNAL----------TLAKVKDLESAVTLILLYALLRFSSKLLKELRSLLYRRVQQNAY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 223 RRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIVFEMTLVSSVLYYKCGAQFALVTLGTLG 302
Cdd:cd18560 71 RELSLKTFAHLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLELIVVSVVFAFHFGAWLALIVFLSVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 303 AYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNEKYEAQRYDGFLKTYETASLKSTSTLAMLNFGQS 382
Cdd:cd18560 151 LYGVFTIKVTEWRTKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQ 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47058990 383 AIFSVGLTAIMVLASQGIVAGALTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 444
Cdd:cd18560 231 LIIQLGLTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSLTDMENL 292
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
125-695 |
4.66e-99 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 317.41 E-value: 4.66e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 125 LSYVWPKDRPdLRARVAISLGFLGGAKAMNIVVPFMFKYAVD-SLNQMSGNMLNLSDAPNTVATMATAVLIG---YGVSR 200
Cdd:TIGR02204 6 LAALWPFVRP-YRGRVLAALVALLITAAATLSLPYAVRLMIDhGFSKDSSGLLNRYFAFLLVVALVLALGTAarfYLVTW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 201 AGAAFFNEVRNAVFGkvaqnsirriaknvflHLHNLDLGFHLSRQTGALskaIDRGTRGISFVLSAL-------VFNLLP 273
Cdd:TIGR02204 85 LGERVVADIRRAVFA----------------HLISLSPSFFDKNRSGEV---VSRLTTDTTLLQSVIgsslsmaLRNALM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 274 IV--FEMTLVSSVlyykcgaQFALVTLGTLGAYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNEKY 351
Cdd:TIGR02204 146 CIggLIMMFITSP-------KLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 352 EAQRYDGFLKTYETASLKSTSTLAMLNfgQSAIFSV--GLTAIMVLASQGIVAGALTVGDL-------VMVNGLLFQLSl 422
Cdd:TIGR02204 219 ERSRFGGAVEKAYEAARQRIRTRALLT--AIVIVLVfgAIVGVLWVGAHDVIAGKMSAGTLgqfvfyaVMVAGSIGTLS- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 423 plnflgTVYRETRQALIDMNTLFTLLKVDTRIKdkAMASPLQI-TPQTATVAFDNVHFEYIE--GQKVLSGVSFEVPAGK 499
Cdd:TIGR02204 296 ------EVWGELQRAAGAAERLIELLQAEPDIK--APAHPKTLpVPLRGEIEFEQVNFAYPArpDQPALDGLNLTVRPGE 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 500 KVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNINASPEEVY 579
Cdd:TIGR02204 368 TVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVE 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 580 AVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHRT 659
Cdd:TIGR02204 448 AAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRT 527
|
570 580 590
....*....|....*....|....*....|....*.
gi 47058990 660 SIFIAHRLSTVVDADEIIVLSQGKVAERGTHYGLLA 695
Cdd:TIGR02204 528 TLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIA 563
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
470-695 |
7.61e-99 |
|
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: 304.53 E-value: 7.61e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 470 ATVAFDNVHFEYIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVG 549
Cdd:cd03254 1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 550 VVPQDAVLFHNTIYYNLLYGNINASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPV 629
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47058990 630 ILYDEATSSLDSITEETILGAMRDVVKHRTSIFIAHRLSTVVDADEIIVLSQGKVAERGTHYGLLA 695
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLA 226
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
128-695 |
9.25e-99 |
|
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: 316.66 E-value: 9.25e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 128 VWPKDRPDLRARVAISLGFLGGAKAMNIVVPFMfKYAVDSLnqmsgnmLNLSDaPNTVATMAtAVLIGYGVSRAGAAFFN 207
Cdd:TIGR02203 5 LWSYVRPYKAGLVLAGVAMILVAATESTLAALL-KPLLDDG-------FGGRD-RSVLWWVP-LVVIGLAVLRGICSFVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 208 evrNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAI----DRGTRGISFVLSALVFNLLPIVFemtLVSS 283
Cdd:TIGR02203 75 ---TYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRItfdsEQVASAATDAFIVLVRETLTVIG---LFIV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 284 VLYYKCGAQFALVTLGTLGAytaftVAVTRWRTRFR---IEMNKADNDAGNAAIDSLLNYETVKYFNNEKYEAQRYDGFL 360
Cdd:TIGR02203 149 LLYYSWQLTLIVVVMLPVLS-----ILMRRVSKRLRrisKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 361 KTYETASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGALTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALID 440
Cdd:TIGR02203 224 NRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 441 MNTLFTLLkvDTRIKDKAMASPLQITpqTATVAFDNVHFEYI-EGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLF 519
Cdd:TIGR02203 304 AESLFTLL--DSPPEKDTGTRAIERA--RGDVEFRNVTFRYPgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 520 RFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNI-NASPEEVYAVAKLAGLHDAILRMPHGY 598
Cdd:TIGR02203 380 RFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 599 DTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIFIAHRLSTVVDADEIIV 678
Cdd:TIGR02203 460 DTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVV 539
|
570
....*....|....*..
gi 47058990 679 LSQGKVAERGTHYGLLA 695
Cdd:TIGR02203 540 MDDGRIVERGTHNELLA 556
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
334-696 |
1.67e-98 |
|
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: 315.54 E-value: 1.67e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 334 IDSLLNYETVKYFNNEKYEAQRYDGFLKTYETASLKstsTLAMlNFGQSA----IFSVGLTAIMVLASQGIVAGALTVGD 409
Cdd:COG4988 201 LDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMK---VLRV-AFLSSAvlefFASLSIALVAVYIGFRLLGGSLTLFA 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 410 LVMVngLLfqLS----LPLNFLGTVYRETRQALIDMNTLFTLLkvDTRIKDKAMASPLQITPQTATVAFDNVHFEYIEGQ 485
Cdd:COG4988 277 ALFV--LL--LApeffLPLRDLGSFYHARANGIAAAEKIFALL--DAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGR 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 486 KVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYN 565
Cdd:COG4988 351 PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIREN 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 566 LLYGNINASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEE 645
Cdd:COG4988 431 LRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEA 510
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 47058990 646 TILGAMRDVVKHRTSIFIAHRLSTVVDADEIIVLSQGKVAERGTHYGLLAN 696
Cdd:COG4988 511 EILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
472-708 |
7.74e-98 |
|
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: 302.54 E-value: 7.74e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYIE--GQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVG 549
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 550 VVPQDAVLFHNTIYYNLLYGNINASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPV 629
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47058990 630 ILYDEATSSLDSITEETILGAMRDVVKHRTSIFIAHRLSTVVDADEIIVLSQGKVAERGTHYGLLANsSSIYSEMWHTQ 708
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQ-KGVYAKLVKAQ 238
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
223-695 |
6.94e-95 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 306.89 E-value: 6.94e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 223 RRIA--KNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFV--------LSALV--FNLLPIVFEMTLVSSVLyykcg 290
Cdd:PRK13657 87 RRLAvlTEYFERIIQLPLAWHSQRGSGRALHTLLRGTDALFGLwlefmrehLATLValVVLLPLALFMNWRLSLV----- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 291 aqfaLVTLGtlGAYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNEKYEAQRYDGFLKTYETASLKS 370
Cdd:PRK13657 162 ----LVVLG--IVYTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNRIEAETQALRDIADNLLAAQMPV 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 371 TSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGALTVGDLVMVNG---LLFQ-LSLPLNFLGTVYRETRQalidMNTLFT 446
Cdd:PRK13657 236 LSWWALASVLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGfatLLIGrLDQVVAFINQVFMAAPK----LEEFFE 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 447 LLKVDTRIKDKAMASPLQITpqTATVAFDNVHFEYIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQK 526
Cdd:PRK13657 312 VEDAVPDVRDPPGAIDLGRV--KGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQS 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 527 GSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNINASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERG 606
Cdd:PRK13657 390 GRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERG 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 607 LKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIFIAHRLSTVVDADEIIVLSQGKVAE 686
Cdd:PRK13657 470 RQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVE 549
|
....*....
gi 47058990 687 RGTHYGLLA 695
Cdd:PRK13657 550 SGSFDELVA 558
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
293-706 |
4.20e-90 |
|
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: 293.60 E-value: 4.20e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 293 FALVTLGTLG-AYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNEKYEAQRYDGFLKTYETASLKST 371
Cdd:COG4987 157 LALVLALGLLlAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 372 STLAMLNFGQSAIFSVGLTAIMVLASQGIVAGALTVGDLVMVngLLFQLSL--PLNFLGTVYRETRQALIDMNTLFTLLK 449
Cdd:COG4987 237 RLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALL--VLAALALfeALAPLPAAAQHLGRVRAAARRLNELLD 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 450 VDTRIKDKAMASPLqitPQTATVAFDNVHFEY-IEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGS 528
Cdd:COG4987 315 APPAVTEPAEPAPA---PGGPSLELEDVSFRYpGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGS 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 529 IYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNINASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLK 608
Cdd:COG4987 392 ITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRR 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 609 LSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIFIAHRLSTVVDADEIIVLSQGKVAERG 688
Cdd:COG4987 472 LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQG 551
|
410
....*....|....*...
gi 47058990 689 THYGLLANSSSiYSEMWH 706
Cdd:COG4987 552 THEELLAQNGR-YRQLYQ 568
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
213-708 |
9.78e-85 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 279.98 E-value: 9.78e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 213 VFGKVAQNsIRRiakNVFLHLHNLDLGFHLSRQTGALskaIDRGTRGISFVLSALVFNLLPIVFEMTLVSSVL----YYK 288
Cdd:PRK11176 92 VSGKVVMT-MRR---RLFGHMMGMPVSFFDKQSTGTL---LSRITYDSEQVASSSSGALITVVREGASIIGLFimmfYYS 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 289 CGAQFALVTLGTLGAYTAFTVAvtrwrTRFRIEMNKADNDAG---NAAIDSLLNYETVKYFNNEKYEAQRYDGFLKTYET 365
Cdd:PRK11176 165 WQLSLILIVIAPIVSIAIRVVS-----KRFRNISKNMQNTMGqvtTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 366 ASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGALTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTLF 445
Cdd:PRK11176 240 QGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLF 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 446 TLLKVDTRiKDKAMaspLQITPQTATVAFDNVHFEYIEGQK-VLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEP 524
Cdd:PRK11176 320 AILDLEQE-KDEGK---RVIERAKGDIEFRNVTFTYPGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 525 QKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNINA-SPEEVYAVAKLAGLHDAILRMPHGYDTQVG 603
Cdd:PRK11176 396 DEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIG 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 604 ERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIFIAHRLSTVVDADEIIVLSQGK 683
Cdd:PRK11176 476 ENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGE 555
|
490 500
....*....|....*....|....*
gi 47058990 684 VAERGTHYGLLANsSSIYSEMWHTQ 708
Cdd:PRK11176 556 IVERGTHAELLAQ-NGVYAQLHKMQ 579
|
|
| ABC_6TM_ABCB6 |
cd18581 |
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, ... |
144-441 |
1.56e-80 |
|
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, mitochondrial; This group represents the ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, ABCB6 (ABC transporter subfamily B, member 6) is closely related to yeast ATM1 and human ABCB7, which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350025 [Multi-domain] Cd Length: 300 Bit Score: 259.49 E-value: 1.56e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 144 LGFLGGAKAMNIVVPFMFKYAVDSLnqmsgnmlnLSDAPNTVATMATAVLIGY-------GVSRAGAAFFNEVRNAVFGK 216
Cdd:cd18581 2 LLLLAAGRVVNVLVPILYKKIVDSL---------TPDSADSPLAFPWALILLYvflkflqGGGSGSVGLLSNLRSFLWIP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 217 VAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIVFEMTLVSSVLYYKCGAQFALV 296
Cdd:cd18581 73 VQQFTTREISVKLFAHLHSLSLRWHLSRKTGEVLRVMDRGTSSINSLLSYVLFNIGPTIADIIIAIIYFAIAFNPWFGLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 297 TLGTLGAYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNEKYEAQRYDGFLKTYETASLKSTSTLAM 376
Cdd:cd18581 153 VFVTMALYLILTIIITEWRTKFRREMNKLDNEKRAKAVDSLLNFETVKYYNAERFEVERYRRAIDDYQVAEWKSNASLNL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47058990 377 LNFGQSAIFSVGLTAIMVLASQGIVAGALTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDM 441
Cdd:cd18581 233 LNTAQNLIITIGLLAGSLLCAYFVVEGKLTVGDFVLFLTYIIQLYAPLNFFGTYYRMIQQSFIDM 297
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
223-702 |
4.66e-77 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 262.74 E-value: 4.66e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 223 RRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGT----RGISFVLSALVFNLLpivfeMTLVSSVLYYKCGAQFALVTL 298
Cdd:TIGR00958 234 LRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTqtmsRSLSLNVNVLLRNLV-----MLLGLLGFMLWLSPRLTMVTL 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 299 GTLGAYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNEKYEAQRYDGFLKtyETASLKSTSTLA-ML 377
Cdd:TIGR00958 309 INLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALE--ETLQLNKRKALAyAG 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 378 NFGQSAIFSVGL-TAIMVLASQGIVAGALTVGDLVMVngLLFQLSL--PLNFLGTVYRETRQALIDMNTLFTLLKVDTRI 454
Cdd:TIGR00958 387 YLWTTSVLGMLIqVLVLYYGGQLVLTGKVSSGNLVSF--LLYQEQLgeAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNI 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 455 KDKAMASPLqitPQTATVAFDNVHFEYIE--GQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLA 532
Cdd:TIGR00958 465 PLTGTLAPL---NLEGLIEFQDVSFSYPNrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLD 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 533 GQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNINASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGG 612
Cdd:TIGR00958 542 GVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGG 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 613 EKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRdvVKHRTSIFIAHRLSTVVDADEIIVLSQGKVAERGTHYG 692
Cdd:TIGR00958 622 QKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRS--RASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQ 699
|
490
....*....|
gi 47058990 693 LLANSSSIYS 702
Cdd:TIGR00958 700 LMEDQGCYKH 709
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
472-683 |
6.58e-77 |
|
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: 244.99 E-value: 6.58e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYIEG-QKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGV 550
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 551 VPQDAVLFHNTIYYNLlygninaspeevyavaklaglhdailrmphgydtqvgerglkLSGGEKQRVAIARAILKDPPVI 630
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 47058990 631 LYDEATSSLDSITEETILGAMRDVVKHRTSIFIAHRLSTVVDADEIIVLSQGK 683
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
472-708 |
1.04e-76 |
|
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: 247.01 E-value: 1.04e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEY-IEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGV 550
Cdd:cd03252 1 ITFEHVRFRYkPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 551 VPQDAVLFHNTIYYNLLYGNINASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVI 630
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47058990 631 LYDEATSSLDSITEETILGAMRDVVKHRTSIFIAHRLSTVVDADEIIVLSQGKVAERGTHYGLLAnSSSIYSEMWHTQ 708
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLA-ENGLYAYLYQLQ 237
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
182-706 |
1.75e-71 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 247.35 E-value: 1.75e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 182 PNTVATMATAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALskaIDRGTrGIS 261
Cdd:TIGR01193 188 PHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEI---VSRFT-DAS 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 262 FVLSALVFNLLPIVFEMTL---VSSVLYYKcGAQFALVTLGTLGAYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLL 338
Cdd:TIGR01193 264 SIIDALASTILSLFLDMWIlviVGLFLVRQ-NMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLN 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 339 NYETVKYFNNEKYEAQRYDGFLKTYetasLKSTSTLAMLNFGQSAIFSV-GLTAIMVL---ASQGIVAGALTVGDLVMVN 414
Cdd:TIGR01193 343 GIETIKSLTSEAERYSKIDSEFGDY----LNKSFKYQKADQGQQAIKAVtKLILNVVIlwtGAYLVMRGKLTLGQLITFN 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 415 GLLFQLSLPLNFLGTVYRETRQALIDMNTLFTLLKVDTRIKDKAMASPLqiTPQTATVAFDNVHFEYIEGQKVLSGVSFE 494
Cdd:TIGR01193 419 ALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTEL--NNLNGDIVINDVSYSYGYGSNILSDISLT 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 495 VPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNI-NA 573
Cdd:TIGR01193 497 IKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKeNV 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 574 SPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRD 653
Cdd:TIGR01193 577 SQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN 656
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 47058990 654 vVKHRTSIFIAHRLSTVVDADEIIVLSQGKVAERGTHYGLLaNSSSIYSEMWH 706
Cdd:TIGR01193 657 -LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELL-DRNGFYASLIH 707
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
472-689 |
4.02e-71 |
|
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: 231.61 E-value: 4.02e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYIEGQK-VLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGV 550
Cdd:cd03244 3 IEFKNVSLRYRPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 551 VPQDAVLFHNTIYYNLLYGNInASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVI 630
Cdd:cd03244 83 IPQDPVLFSGTIRSNLDPFGE-YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 47058990 631 LYDEATSSLDSITEETILGAMRDVVKHRTSIFIAHRLSTVVDADEIIVLSQGKVAERGT 689
Cdd:cd03244 162 VLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
223-695 |
7.42e-69 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 240.23 E-value: 7.42e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 223 RRIAKNVFLHLHNLDLGFHLSRQTGALSKAI---DRGTRGISFVLSALVFNLLPIVFE---MTLVSSVLyykcgaqfALV 296
Cdd:TIGR03796 227 VGMSARFLWHILRLPVRFFAQRHAGDIASRVqlnDQVAEFLSGQLATTALDAVMLVFYallMLLYDPVL--------TLI 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 297 TLGTlgayTAFTVAVTRWRTRFRIEMN-KADNDAG---NAAIDSLLNYETVKYFNNEKYEAQRYDGflktYETASLKSTS 372
Cdd:TIGR03796 299 GIAF----AAINVLALQLVSRRRVDANrRLQQDAGkltGVAISGLQSIETLKASGLESDFFSRWAG----YQAKLLNAQQ 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 373 TLAMLNfgqsAIFSV------GLTAIMVLASQG--IVAGALTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 444
Cdd:TIGR03796 371 ELGVLT----QILGVlptlltSLNSALILVVGGlrVMEGQLTIGMLVAFQSLMSSFLEPVNNLVGFGGTLQELEGDLNRL 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 445 FTLLK--VDTRIKDKAMASPLQITPQ--TATVAFDNVHFEY-IEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLF 519
Cdd:TIGR03796 447 DDVLRnpVDPLLEEPEGSAATSEPPRrlSGYVELRNITFGYsPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVA 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 520 RFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNINASPEEVYAVAKLAGLHDAILRMPHGYD 599
Cdd:TIGR03796 527 GLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYD 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 600 TQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRdvvkHR--TSIFIAHRLSTVVDADEII 677
Cdd:TIGR03796 607 AELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLR----RRgcTCIIVAHRLSTIRDCDEII 682
|
490
....*....|....*...
gi 47058990 678 VLSQGKVAERGTHYGLLA 695
Cdd:TIGR03796 683 VLERGKVVQRGTHEELWA 700
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
472-684 |
1.92e-68 |
|
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: 224.39 E-value: 1.92e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYIEGQ-KVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGV 550
Cdd:cd03245 3 IEFRNVSFSYPNQEiPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 551 VPQDAVLFHNTIYYNLLYGNINASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVI 630
Cdd:cd03245 83 VPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 47058990 631 LYDEATSSLDSITEETILGAMRDVVKHRTSIFIAHRLSTVVDADEIIVLSQGKV 684
Cdd:cd03245 163 LLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
147-444 |
1.12e-65 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 219.71 E-value: 1.12e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 147 LGGAKAMNIVVPFMFKYAVDSLNQMSGNMlnlsdapntvatMATAVLIgYGVSR--AGAAFFNEVRNAVFGKVAQNSIRR 224
Cdd:cd18583 5 LLAERVLNVLVPRQLGIIVDSLSGGSGKS------------PWKEIGL-YVLLRflQSGGGLGLLRSWLWIPVEQYSYRA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 225 IAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTrGISFVLSALVFNLLPIVFEMTLVSSVLYYKCGAQFALVTLGTLGAY 304
Cdd:cd18583 72 LSTAAFNHVMNLSMDFHDSKKSGEVLKAIEQGS-SINDLLEQILFQIVPMIIDLVIAIVYLYYLFDPYMGLIVAVVMVLY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 305 TAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNEKYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAI 384
Cdd:cd18583 151 VWSTIKLTSWRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYREAVKNYQKAERKYLFSLNLLNAVQSLI 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 385 FSVGLTAIMVLASQGIVAGALTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 444
Cdd:cd18583 231 LTLGLLAGCFLAAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDLIDAERL 290
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
465-684 |
1.23e-64 |
|
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: 214.64 E-value: 1.23e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 465 ITPQT--ATVAFDNVHFEYIE--GQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS 540
Cdd:cd03248 3 LAPDHlkGIVKFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 541 LESLRRAVGVVPQDAVLFHNTIYYNLLYGNINASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIA 620
Cdd:cd03248 83 HKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47058990 621 RAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIFIAHRLSTVVDADEIIVLSQGKV 684
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
152-702 |
2.25e-64 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 225.15 E-value: 2.25e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 152 AMNIVVPFMFKYAVDSLnqmsgnmlnlSDAPNTVATMAtaVLIGYGVSRAgAAFFNEVRNAvfGKVAQNSIRRIAKNVFL 231
Cdd:TIGR01192 33 AITIAEPILFGRIIDAI----------SSKSDVLPTLA--LWAGFGVFNT-IAYVLVAREA--DRLAHGRRATLLTEAFG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 232 HLHNLDLGFHLSRQTGALSKAIDRGTRGISFV--------LSALV--FNLLPIVFEMTLVSSvlyykcgaqFALVTLGTL 301
Cdd:TIGR01192 98 RIISMPLSWHQQRGTSNALHTLLRATETLFGLwlefmrqhLATFValFLLIPTAFAMDWRLS---------IVLMVLGIL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 302 GAYTAftvavtrwrtrfRIEMNKADNdaGNAAI------------DSLLNYETVKYFNN---EKYEAQRYDGFLKTYETA 366
Cdd:TIGR01192 169 YILIA------------KLVMQRTKN--GQAAVehhyhnvfkhvsDSISNVSVVHSYNRieaETSALKQFTNNLLSAQYP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 367 SLKSTSTLAMLNFGQSaifSVGLTAIMVLASQGIVAGALTVGDLVMVNG----LLFQLSLPLNFLGTVYrETRQALIDmn 442
Cdd:TIGR01192 235 VLDWWALASGLNRMAS---TISMMCILVIGTVLVIKGELSVGEVIAFIGfanlLIGRLDQMSGFITQIF-EARAKLED-- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 443 tlFTLLKVDTRIKDKAMASPlQITPQTATVAFDNVHFEYIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFY 522
Cdd:TIGR01192 309 --FFDLEDSVFQREEPADAP-ELPNVKGAVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVY 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 523 EPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNINASPEEVYAVAKLAGLHDAILRMPHGYDTQV 602
Cdd:TIGR01192 386 DPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLV 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 603 GERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIFIAHRLSTVVDADEIIVLSQG 682
Cdd:TIGR01192 466 GERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQG 545
|
570 580
....*....|....*....|
gi 47058990 683 KVAERGTHYGLLANSSSIYS 702
Cdd:TIGR01192 546 RLIEKGSFQELIQKDGRFYK 565
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
400-708 |
6.07e-62 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 218.04 E-value: 6.07e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 400 IVAGALTVGDL---VMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTLFTLLKVdtrIKDKAMASPlqitPQTATVAFDN 476
Cdd:PRK10789 246 VVNGSLTLGQLtsfVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPV---VKDGSEPVP----EGRGELDVNI 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 477 VHFEYIEGQK-VLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDA 555
Cdd:PRK10789 319 RQFTYPQTDHpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTP 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 556 VLFHNTIYYNLLYGNINASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEA 635
Cdd:PRK10789 399 FLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDA 478
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47058990 636 TSSLDSITEETILGAMRDVVKHRTSIFIAHRLSTVVDADEIIVLSQGKVAERGTHyGLLANSSSIYSEMWHTQ 708
Cdd:PRK10789 479 LSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNH-DQLAQQSGWYRDMYRYQ 550
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
422-679 |
9.22e-61 |
|
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: 213.69 E-value: 9.22e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 422 LPLNFLGTVYRETRQALIDMNTLFTLLKVDTRIKdkAMASPLQITPqTATVAFDNVHFEYIEGQKVLSGVSFEVPAGKKV 501
Cdd:TIGR02857 275 LPLRQLGAQYHARADGVAAAEALFAVLDAAPRPL--AGKAPVTAAP-ASSLEFSGVSVAYPGRRPALRPVSFTVPPGERV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 502 AIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNINASPEEVYAV 581
Cdd:TIGR02857 352 ALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREA 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 582 AKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHRTSI 661
Cdd:TIGR02857 432 LERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVL 511
|
250
....*....|....*...
gi 47058990 662 FIAHRLSTVVDADEIIVL 679
Cdd:TIGR02857 512 LVTHRLALAALADRIVVL 529
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
402-708 |
4.68e-58 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 207.65 E-value: 4.68e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 402 AGALTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTLFTLlkvdtrikdkaMASPLQ------ITPQTATVAFD 475
Cdd:PRK10790 276 SGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFEL-----------MDGPRQqygnddRPLQSGRIDID 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 476 NVHFEYIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDA 555
Cdd:PRK10790 345 NVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDP 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 556 VLFHNTIYYNLLYGNiNASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEA 635
Cdd:PRK10790 425 VVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEA 503
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47058990 636 TSSLDSITEETILGAMRDVVKHRTSIFIAHRLSTVVDADEIIVLSQGKVAERGTHYGLLAnSSSIYSEMWHTQ 708
Cdd:PRK10790 504 TANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLA-AQGRYWQMYQLQ 575
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
464-696 |
4.84e-58 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 207.37 E-value: 4.84e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 464 QITPQTATVAFDNVHFEYIEG-QKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLE 542
Cdd:PRK11160 331 TAAADQVSLTLNNVSFTYPDQpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 543 SLRRAVGVVPQDAVLFHNTIYYNLLYGNINASPEEVYAVAKLAGLhDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARA 622
Cdd:PRK11160 411 ALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGL-EKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARA 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47058990 623 ILKDPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIFIAHRLSTVVDADEIIVLSQGKVAERGTHYGLLAN 696
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQ 563
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
355-667 |
6.63e-55 |
|
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: 197.58 E-value: 6.63e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 355 RYDGFLKTYETASLKST----STLAMLNFGQSA-IFSVGLTAIMVL--ASQGIVAGALTVGDLVMVngLLFQLSL--PLN 425
Cdd:TIGR02868 211 ALPAALAQVEEADRELTraerRAAAATALGAALtLLAAGLAVLGALwaGGPAVADGRLAPVTLAVL--VLLPLAAfeAFA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 426 FLGTVYRETRQALIDMNTLFTLLKVDTRIKDKAMASPLQITPQTATVAFDNVHFEYIEGQKVLSGVSFEVPAGKKVAIVG 505
Cdd:TIGR02868 289 ALPAAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILG 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 506 GSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNINASPEEVYAVAKLA 585
Cdd:TIGR02868 369 PSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERV 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 586 GLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIFIAH 665
Cdd:TIGR02868 449 GLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITH 528
|
..
gi 47058990 666 RL 667
Cdd:TIGR02868 529 HL 530
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
293-685 |
7.72e-55 |
|
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: 198.05 E-value: 7.72e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 293 FALVTLGTLGAYTAFTVAVTRwrtRFRIEMNKADNDAGNAAIDSLLNYETVkyfnnekyEA------------QRYDGFL 360
Cdd:COG4618 160 LALVGALVLVALALLNERLTR---KPLKEANEAAIRANAFAEAALRNAEVI--------EAmgmlpalrrrwqRANARAL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 361 KTYETASLKSTSTLAML----NFGQSAIFSVGltAIMVLASQgIVAGALTVGDLVMVNGLLfqlslPL-NFLGT--VYRE 433
Cdd:COG4618 229 ALQARASDRAGGFSALSkflrLLLQSAVLGLG--AYLVIQGE-ITPGAMIAASILMGRALA-----PIeQAIGGwkQFVS 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 434 TRQALidmNTLFTLLKvDTRIKDKAMASPlqiTPQtATVAFDNVHFEYIEGQK-VLSGVSFEVPAGKKVAIVGGSGSGKS 512
Cdd:COG4618 301 ARQAY---RRLNELLA-AVPAEPERMPLP---RPK-GRLSVENLTVVPPGSKRpILRGVSFSLEPGEVLGVIGPSGSGKS 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 513 TIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYynllyGNI----NASPEEVYAVAKLAGLH 588
Cdd:COG4618 373 TLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIA-----ENIarfgDADPEKVVAAAKLAGVH 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 589 DAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIF-IAHRL 667
Cdd:COG4618 448 EMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVvITHRP 527
|
410
....*....|....*...
gi 47058990 668 STVVDADEIIVLSQGKVA 685
Cdd:COG4618 528 SLLAAVDKLLVLRDGRVQ 545
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
467-689 |
5.26e-54 |
|
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: 184.92 E-value: 5.26e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 467 PQTATVAFDNVHFEYI-EGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLR 545
Cdd:cd03369 2 PEHGEIEVENLSVRYApDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 546 RAVGVVPQDAVLFHNTIYYNL-LYGNInaSPEEVYAVAKlaglhdailrmphgydtqVGERGLKLSGGEKQRVAIARAIL 624
Cdd:cd03369 82 SSLTIIPQDPTLFSGTIRSNLdPFDEY--SDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47058990 625 KDPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIFIAHRLSTVVDADEIIVLSQGKVAERGT 689
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
423-712 |
4.16e-52 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 190.83 E-value: 4.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 423 PLNFLGTVYRETRQALIDMNTLFTLLKVDTrikdKAMASPLQITPQTATVAFDNVHFEYI--EGQKVLSGVSFEVPAGKK 500
Cdd:PRK11174 303 PLRDLGTFYHAKAQAVGAAESLVTFLETPL----AHPQQGEKELASNDPVTIEAEDLEILspDGKTLAGPLNFTLPAGQR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 501 VAIVGGSGSGKSTIVRLLFRFYePQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNINASPEEVYA 580
Cdd:PRK11174 379 IALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQ 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 581 VAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHRTS 660
Cdd:PRK11174 458 ALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTT 537
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 47058990 661 IFIAHRLSTVVDADEIIVLSQGKVAERGtHYGLLANSSSIYSEMWHTQSTRI 712
Cdd:PRK11174 538 LMVTHQLEDLAQWDQIWVMQDGQIVQQG-DYAELSQAGGLFATLLAHRQEEI 588
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
472-689 |
5.72e-51 |
|
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: 177.52 E-value: 5.72e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVV 551
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 552 PQDAV--LFHNTIYYNLLYG--NINASPEE----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAI 623
Cdd:COG1122 81 FQNPDdqLFAPTVEEDVAFGpeNLGLPREEirerVEEALELVGLEHLADRPPH-----------ELSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47058990 624 LKDPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIFIA-HRLSTVVD-ADEIIVLSQGKVAERGT 689
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVAElADRVIVLDDGRIVADGT 217
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
472-688 |
2.07e-48 |
|
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: 168.65 E-value: 2.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYIE-GQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSlESLRRAVGV 550
Cdd:cd03247 1 LSINNVSFSYPEqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 551 VPQDAVLFHNTIYYNLlygninaspeevyavaklaglhdailrmphgydtqvgerGLKLSGGEKQRVAIARAILKDPPVI 630
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 47058990 631 LYDEATSSLDSITEETILGAMRDVVKHRTSIFIAHRLSTVVDADEIIVLSQGKVAERG 688
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
474-689 |
2.14e-48 |
|
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: 170.76 E-value: 2.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 474 FDNVHFEYiEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLRRAVGV 550
Cdd:cd03261 3 LRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRRRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 551 VPQDAVLF-HNTIYYNL---LYGNINASPEEVYAVA--KLA--GLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARA 622
Cdd:cd03261 82 LFQSGALFdSLTVFENVafpLREHTRLSEEEIREIVleKLEavGLRGAEDLYPA-----------ELSGGMKKRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 623 ILKDPPVILYDEATSSLDSITEETILGAMRDVVKHR--TSIFIAHRLSTVVD-ADEIIVLSQGKVAERGT 689
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELglTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGT 220
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
474-684 |
1.35e-47 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 167.69 E-value: 1.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 474 FDNVHFEyIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQ 553
Cdd:COG4619 3 LEGLSFR-VGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 554 DAVLFHNTIYYNLL----YGNINASPEEVYAVAKLAGLHDAILrmphgyDTQVGErglkLSGGEKQRVAIARAILKDPPV 629
Cdd:COG4619 82 EPALWGGTVRDNLPfpfqLRERKFDRERALELLERLGLPPDIL------DKPVER----LSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47058990 630 ILYDEATSSLDSITEETILGAMRDVVKH--RTSIFIAH------RLstvvdADEIIVLSQGKV 684
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAEegRAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
472-689 |
2.60e-47 |
|
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: 167.85 E-value: 2.60e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYiEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLRRAV 548
Cdd:COG1127 6 IEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 549 GVVPQDAVLFHN-TIYYNLLYG---NINASPEEVYAVA--KLA--GLHDAILRMPhgydtqvGErglkLSGGEKQRVAIA 620
Cdd:COG1127 85 GMLFQGGALFDSlTVFENVAFPlreHTDLSEAEIRELVleKLElvGLPGAADKMP-------SE----LSGGMRKRVALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47058990 621 RAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHR--TSIFIAHRLSTVVD-ADEIIVLSQGKVAERGT 689
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAiADRVAVLADGKIIAEGT 225
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
371-728 |
9.41e-46 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 177.09 E-value: 9.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 371 TSTLAMLNFGQSAiFSVGLTAIMVLasqgIVAGALTVGDLVmvNGLLFQLSLPLNFLGTVYRETRqaLIDMNTLFTLLKV 450
Cdd:PLN03232 1151 TATFAVLRNGNAE-NQAGFASTMGL----LLSYTLNITTLL--SGVLRQASKAENSLNSVERVGN--YIDLPSEATAIIE 1221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 451 DTRikdkamasPLQITPQTATVAFDNVHFEYIEG-QKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSI 529
Cdd:PLN03232 1222 NNR--------PVSGWPSRGSIKFEDVHLRYRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRI 1293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 530 YLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNL-LYGNINASpeEVYAVAKLAGLHDAILRMPHGYDTQVGERGLK 608
Cdd:PLN03232 1294 MIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIdPFSEHNDA--DLWEALERAHIKDVIDRNPFGLDAEVSEGGEN 1371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 609 LSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIFIAHRLSTVVDADEIIVLSQGKVAERG 688
Cdd:PLN03232 1372 FSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYD 1451
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 47058990 689 THYGLLANSSSIYSEMWH-TQSTRIQNHDNLGWDAKKESLS 728
Cdd:PLN03232 1452 SPQELLSRDTSAFFRMVHsTGPANAQYLSNLVFERRENGMS 1492
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
472-701 |
1.85e-45 |
|
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: 170.47 E-value: 1.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEY----IEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESL 544
Cdd:COG1123 261 LEVRNLSKRYpvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 545 RRAVGVVPQD--AVLF-HNTIYYNL-----LYGNINAS--PEEVYAVAKLAGLHDAIL-RMPHGydtqvgerglkLSGGE 613
Cdd:COG1123 341 RRRVQMVFQDpySSLNpRMTVGDIIaeplrLHGLLSRAerRERVAELLERVGLPPDLAdRYPHE-----------LSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 614 KQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHR--TSIFIAHRLSTVVD-ADEIIVLSQGKVAERGTH 690
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELglTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPT 489
|
250
....*....|.
gi 47058990 691 YGLLANSSSIY 701
Cdd:COG1123 490 EEVFANPQHPY 500
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
415-739 |
8.29e-45 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 174.16 E-value: 8.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 415 GLLfqLSLPLNFLGTVYRETRQALIDMNTLFTLLKVDTRIKDKAMAsPLQIT--------PQTATVAFDNVHFEY-IEGQ 485
Cdd:PLN03130 1176 GLL--LSYALNITSLLTAVLRLASLAENSLNAVERVGTYIDLPSEA-PLVIEnnrpppgwPSSGSIKFEDVVLRYrPELP 1252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 486 KVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYN 565
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFN 1332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 566 LLYGNiNASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEE 645
Cdd:PLN03130 1333 LDPFN-EHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDA 1411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 646 TILGAMRDVVKHRTSIFIAHRLSTVVDADEIIVLSQGKVAERGTHYGLLANSSSIYSEMwhTQSTRIQNHDNLGWDA--K 723
Cdd:PLN03130 1412 LIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKM--VQSTGAANAQYLRSLVfgG 1489
|
330
....*....|....*.
gi 47058990 724 KESLSKEEERKKLQEE 739
Cdd:PLN03130 1490 DEDRLAREESKALDGQ 1505
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
472-686 |
9.54e-45 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 160.22 E-value: 9.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLRRAV 548
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 549 GVVPQDA-VLFHNTIYYNLLY-----GninASPEE----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVA 618
Cdd:COG2884 82 GVVFQDFrLLPDRTVYENVALplrvtG---KSRKEirrrVREVLDLVGLSDKAKALPH-----------ELSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47058990 619 IARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIFIA-HRLSTVvdaDE----IIVLSQGKVAE 686
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELV---DRmpkrVLELEDGRLVR 217
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
474-683 |
4.77e-44 |
|
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: 157.63 E-value: 4.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 474 FDNVHFEYIEG-QKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVP 552
Cdd:cd03225 2 LKNLSFSYPDGaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 553 QDA--VLFHNTIYYNLLYG--NINASPEEVYAVAKLA----GLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAIL 624
Cdd:cd03225 82 QNPddQFFGPTVEEEVAFGleNLGLPEEEIEERVEEAlelvGLEGLRDRSPF-----------TLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47058990 625 KDPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIFIA-HRLSTVVD-ADEIIVLSQGK 683
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
484-688 |
3.03e-43 |
|
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: 155.37 E-value: 3.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 484 GQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEslRRAVGVVPQDAVLF-HNTI 562
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFpHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 563 YYNLLYG-NINASPEE-----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYDEAT 636
Cdd:cd03259 90 AENIAFGlKLRGVPKAeirarVRELLELVGLEGLLNRYPH-----------ELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 47058990 637 SSLDSITEETILGAMRDVVK--HRTSIFIAHRLSTVVD-ADEIIVLSQGKVAERG 688
Cdd:cd03259 159 SALDAKLREELREELKELQRelGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
475-702 |
4.21e-43 |
|
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: 156.50 E-value: 4.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 475 DNVHFEY---IEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVV 551
Cdd:COG1124 5 RNLSVSYgqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 552 PQDAVL-FH--NTIYYNL-----LYGnINASPEEVYAVAKLAGLHDAIL-RMPHgydtqvgerglKLSGGEKQRVAIARA 622
Cdd:COG1124 85 FQDPYAsLHprHTVDRILaeplrIHG-LPDREERIAELLEQVGLPPSFLdRYPH-----------QLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 623 ILKDPPVILYDEATSSLDSITEETILGAMRDVVKHR--TSIFIAHRLStVVD--ADEIIVLSQGKVAERGTHYGLLANSS 698
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLA-VVAhlCDRVAVMQNGRIVEELTVADLLAGPK 231
|
....
gi 47058990 699 SIYS 702
Cdd:COG1124 232 HPYT 235
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
476-688 |
8.48e-43 |
|
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: 154.97 E-value: 8.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 476 NVHF-EYIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLRRAVGVV 551
Cdd:cd03257 8 SVSFpTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKEIQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 552 PQDAVLFHN---TIYYNL---LYGNINASPEEVYAVAKLA-----GLHDAILRM-PHgydtqvgerglKLSGGEKQRVAI 619
Cdd:cd03257 88 FQDPMSSLNprmTIGEQIaepLRIHGKLSKKEARKEAVLLllvgvGLPEEVLNRyPH-----------ELSGGQRQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47058990 620 ARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHR--TSIFIAHRLSTVVD-ADEIIVLSQGKVAERG 688
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
475-684 |
8.58e-43 |
|
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: 152.76 E-value: 8.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 475 DNVHFEYIEGQK-VLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQ 553
Cdd:cd03246 4 ENVSFRYPGAEPpVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 554 DAVLFHNTIyynllYGNInaspeevyavaklaglhdailrmphgydtqvgerglkLSGGEKQRVAIARAILKDPPVILYD 633
Cdd:cd03246 84 DDELFSGSI-----AENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 47058990 634 EATSSLDSITEETILGAMRDV-VKHRTSIFIAHRLSTVVDADEIIVLSQGKV 684
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
488-637 |
2.91e-42 |
|
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: 150.49 E-value: 2.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 488 LSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLF-HNTIYYNL 566
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47058990 567 LYGninASPEEVYAVAKLAGLHDAI--LRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATS 637
Cdd:pfam00005 81 RLG---LLLKGLSKREKDARAEEALekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
472-688 |
4.37e-42 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 152.72 E-value: 4.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYIEGQkVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE-----PQKGSIYLAGQNI--QDVSLESL 544
Cdd:cd03260 1 IELRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIydLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 545 RRAVGVVPQDAVLFHNTIYYNLLYG-------NINASPEEVYAVAKLAGLHDAILRMPHGydtqvgergLKLSGGEKQRV 617
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKAALWDEVKDRLHA---------LGLSGGQQQRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47058990 618 AIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIFIAH------RLstvvdADEIIVLSQGKVAERG 688
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHnmqqaaRV-----ADRTAFLLNGRLVEFG 222
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
450-704 |
5.36e-42 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 165.72 E-value: 5.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 450 VDTRIKDKAMASPLQ----ITPQTATVA-----------FDNVHFEYIEGQK-VLSGVSFEVPAGKKVAIVGGSGSGKST 513
Cdd:PTZ00243 1272 VDALERRTGMAADVTgtvvIEPASPTSAaphpvqagslvFEGVQMRYREGLPlVLRGVSFRIAPREKVGIVGRTGSGKST 1351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 514 IVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNlLYGNINASPEEVYAVAKLAGLHDAILR 593
Cdd:PTZ00243 1352 LLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQN-VDPFLEASSAEVWAALELVGLRERVAS 1430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 594 MPHGYDTQVGERGLKLSGGEKQRVAIARAILK-DPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIFIAHRLSTVVD 672
Cdd:PTZ00243 1431 ESEGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQ 1510
|
250 260 270
....*....|....*....|....*....|..
gi 47058990 673 ADEIIVLSQGKVAERGTHYGLLANSSSIYSEM 704
Cdd:PTZ00243 1511 YDKIIVMDHGAVAEMGSPRELVMNRQSIFHSM 1542
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
472-689 |
6.12e-42 |
|
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: 153.74 E-value: 6.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYIEGQK-VLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS-LESLRRAVG 549
Cdd:TIGR04520 1 IEVENVSFSYPESEKpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEnLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 550 VVpqdavlFHN--------TIYYNLLYG--NINASPEE----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQ 615
Cdd:TIGR04520 81 MV------FQNpdnqfvgaTVEDDVAFGleNLGVPREEmrkrVDEALKLVGMEDFRDREPH-----------LLSGGQKQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47058990 616 RVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHR--TSIFIAHRLSTVVDADEIIVLSQGKVAERGT 689
Cdd:TIGR04520 144 RVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEAVLADRVIVMNKGKIVAEGT 219
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
472-689 |
6.29e-41 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 149.83 E-value: 6.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYiEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEsLRRAVGVV 551
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 552 PQDAVLFHN-TIYYNL-----LYG-NINASPEEVYAVAKLAGLHDAIlrmphgyDTQVGerglKLSGGEKQRVAIARAIL 624
Cdd:COG1131 79 PQEPALYPDlTVRENLrffarLYGlPRKEARERIDELLELFGLTDAA-------DRKVG----TLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47058990 625 KDPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIFIA-HRLSTVVD-ADEIIVLSQGKVAERGT 689
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAERlCDRVAIIDKGRIVADGT 214
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
474-683 |
6.88e-41 |
|
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: 147.72 E-value: 6.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 474 FDNVHFEYiEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLES--LRRAVGVV 551
Cdd:cd03229 3 LKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 552 PQDAVLF-HNTIYYNLLYGninaspeevyavaklaglhdailrmphgydtqvgerglkLSGGEKQRVAIARAILKDPPVI 630
Cdd:cd03229 82 FQDFALFpHLTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 47058990 631 LYDEATSSLDSITEETILGAMRDVVKH--RTSIFIAHRLSTVVD-ADEIIVLSQGK 683
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
469-689 |
1.22e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 150.14 E-value: 1.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 469 TATVAFDNVHFEYIEGQK-VLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRA 547
Cdd:PRK13632 5 SVMIKVENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 548 VGVVPQ--DAVLFHNTIYYNLLYG--NINASPEE----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAI 619
Cdd:PRK13632 85 IGIIFQnpDNQFIGATVEDDIAFGleNKKVPPKKmkdiIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47058990 620 ARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHR--TSIFIAHRLSTVVDADEIIVLSQGKVAERGT 689
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGK 225
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
472-698 |
1.31e-40 |
|
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: 148.88 E-value: 1.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYIEGQK---VLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLR 545
Cdd:cd03258 2 IELKNVSKVFGDTGGkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkeLRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 546 RAVGVVPQdavlfhntiYYNLL-----YGNInASPEEVYAVAK------------LAGLHDAIlrmpHGYDTQvgerglk 608
Cdd:cd03258 82 RRIGMIFQ---------HFNLLssrtvFENV-ALPLEIAGVPKaeieervlelleLVGLEDKA----DAYPAQ------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 609 LSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHR--TSIFIAHRLSTVVD-ADEIIVLSQGKVA 685
Cdd:cd03258 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRiCDRVAVMEKGEVV 220
|
250
....*....|...
gi 47058990 686 ERGTHYGLLANSS 698
Cdd:cd03258 221 EEGTVEEVFANPQ 233
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
476-703 |
4.95e-40 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 159.42 E-value: 4.95e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 476 NVHFEYIEGQKV--LSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE------------------------------ 523
Cdd:PTZ00265 1170 DVNFRYISRPNVpiYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqn 1249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 524 ------------------------PQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNINASPEEVY 579
Cdd:PTZ00265 1250 vgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVK 1329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 580 AVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKH-- 657
Cdd:PTZ00265 1330 RACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKad 1409
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 47058990 658 RTSIFIAHRLSTVVDADEIIVLSQGK-----VAERGTHYGLLANSSSIYSE 703
Cdd:PTZ00265 1410 KTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLSVQDGVYKK 1460
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
460-702 |
5.41e-40 |
|
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: 159.34 E-value: 5.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 460 ASPLQITPQTATVAFDNVHFEYIEGQK-VLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQD 538
Cdd:TIGR00957 1273 TAPPSGWPPRGRVEFRNYCLRYREDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAK 1352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 539 VSLESLRRAVGVVPQDAVLFHNTIYYNL-LYGNInaSPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRV 617
Cdd:TIGR00957 1353 IGLHDLRFKITIIPQDPVLFSGSLRMNLdPFSQY--SDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLV 1430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 618 AIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIFIAHRLSTVVDADEIIVLSQGKVAERGTHYGLLANS 697
Cdd:TIGR00957 1431 CLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQR 1510
|
....*
gi 47058990 698 SSIYS 702
Cdd:TIGR00957 1511 GIFYS 1515
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
472-686 |
6.76e-40 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 146.73 E-value: 6.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYIEGQ---KVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLR 545
Cdd:COG1136 5 LELRNLTKSYGTGEgevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSereLARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 546 R-AVGVVPQdavlFHN-----TIYYN----LLYGNINAS--PEEVYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGE 613
Cdd:COG1136 85 RrHIGFVFQ----FFNllpelTALENvalpLLLAGVSRKerRERARELLERVGLGDRLDHRPS-----------QLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47058990 614 KQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVK--HRTSIFIAHRLSTVVDADEIIVLSQGKVAE 686
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
472-696 |
7.17e-40 |
|
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: 147.06 E-value: 7.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVV 551
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 552 PQDAVLF-HNTIYYNL-LYGNINASPEE-----VYAVAKLAGLHDAIL--RMPHgydtqvgerglKLSGGEKQRVAIARA 622
Cdd:cd03295 81 IQQIGLFpHMTVEENIaLVPKLLKWPKEkirerADELLALVGLDPAEFadRYPH-----------ELSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47058990 623 ILKDPPVILYDEATSSLDSITEETILGAMRDVVK--HRTSIFIAHRL-STVVDADEIIVLSQGKVAERGTHYGLLAN 696
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
472-696 |
7.70e-40 |
|
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: 154.29 E-value: 7.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYIEGQK-VLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ---KGSIYLAGQNIQDVSLESLRRA 547
Cdd:COG1123 5 LEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 548 VGVVPQD--AVLFHNTIYYNLLYG--NINASPEE----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAI 619
Cdd:COG1123 85 IGMVFQDpmTQLNPVTVGDQIAEAleNLGLSRAEararVLELLEAVGLERRLDRYPH-----------QLSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 620 ARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHR--TSIFIAHRLSTVVD-ADEIIVLSQGKVAERGTHYGLLAN 696
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
433-733 |
4.02e-39 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 156.73 E-value: 4.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 433 ETRQALIDMNTLFTLLKVDTRIKDKAMASPLqitPQTATVAFDNVHFEYIEGQKV--LSGVSFEVPAGKKVAIVGGSGSG 510
Cdd:PTZ00265 347 EYMKSLEATNSLYEIINRKPLVENNDDGKKL---KDIKKIQFKNVRFHYDTRKDVeiYKDLNFTLTEGKTYAFVGESGCG 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 511 KSTIVRLLFRFYEPQKGSIYLA-GQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYG----------------NINA 573
Cdd:PTZ00265 424 KSTILKLIERLYDPTEGDIIINdSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyneDGND 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 574 SPE-----------------------------------------EVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGG 612
Cdd:PTZ00265 504 SQEnknkrnscrakcagdlndmsnttdsneliemrknyqtikdsEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGG 583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 613 EKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVV--KHRTSIFIAHRLSTVVDADEIIVLS---------- 680
Cdd:PTZ00265 584 QKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSnrergstvdv 663
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 681 --------------------QGK-----------------VAERGTHYGLLANSSSIYSEMWHTQ---STRIQNHDNLGW 720
Cdd:PTZ00265 664 diigedptkdnkennnknnkDDNnnnnnnnnnkinnagsyIIEQGTHDALMKNKNGIYYTMINNQkvsSKKSSNNDNDKD 743
|
410
....*....|...
gi 47058990 721 DAKKESLSKEEER 733
Cdd:PTZ00265 744 SDMKSSAYKDSER 756
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
474-683 |
5.58e-39 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 141.61 E-value: 5.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 474 FDNVHFEYiEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQ 553
Cdd:cd00267 2 IENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 554 davlfhntiyynllygninaspeevyavaklaglhdailrmphgydtqvgerglkLSGGEKQRVAIARAILKDPPVILYD 633
Cdd:cd00267 81 -------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 47058990 634 EATSSLDSITEETILGAMRDVVKH-RTSIFIAHRLSTVVDA-DEIIVLSQGK 683
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
472-684 |
5.92e-39 |
|
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: 143.78 E-value: 5.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYIEG---QKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLR 545
Cdd:cd03255 1 IELKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekeLAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 546 RA-VGVVPQdavlFHN-----TIYYN-----LLYGNINASPEE-VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGE 613
Cdd:cd03255 81 RRhIGFVFQ----SFNllpdlTALENvelplLLAGVPKKERRErAEELLERVGLGDRLNHYPS-----------ELSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47058990 614 KQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHR--TSIFIAHRLSTVVDADEIIVLSQGKV 684
Cdd:cd03255 146 QQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
472-689 |
1.76e-38 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 142.83 E-value: 1.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYiEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQD--VSLESLRRAVG 549
Cdd:COG1126 2 IEIENLHKSF-GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDskKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 550 VVPQDAVLF-HNTIYYNLLYGNI---NASPEEVYAVAK--LA--GLHDAILRMPHgydtqvgerglKLSGGEKQRVAIAR 621
Cdd:COG1126 81 MVFQQFNLFpHLTVLENVTLAPIkvkKMSKAEAEERAMelLErvGLADKADAYPA-----------QLSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47058990 622 AILKDPPVILYDEATSSLD--SITEetILGAMRDVVK-HRTSIFIAHRLS---TVvdADEIIVLSQGKVAERGT 689
Cdd:COG1126 150 ALAMEPKVMLFDEPTSALDpeLVGE--VLDVMRDLAKeGMTMVVVTHEMGfarEV--ADRVVFMDGGRIVEEGP 219
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
472-687 |
9.83e-38 |
|
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: 140.30 E-value: 9.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYIEGQ---KVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSleslrRAV 548
Cdd:cd03293 1 LEVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 549 GVVPQDAVLF-HNTIYYNLLYG-NINASP-----EEVYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIAR 621
Cdd:cd03293 76 GYVFQQDALLpWLTVLDNVALGlELQGVPkaearERAEELLELVGLSGFENAYPH-----------QLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47058990 622 AILKDPPVILYDEATSSLDSITEETILGAMRDVVKHR--TSIFIAHRLSTVVD-ADEIIVLSQ--GKVAER 687
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDEAVFlADRVVVLSArpGRIVAE 215
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
468-689 |
9.62e-37 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 141.39 E-value: 9.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 468 QTATVAFDNVHFEYiEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEslRRA 547
Cdd:COG3842 2 AMPALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 548 VGVVPQDAVLF-HNTIYYNLLYG--NINASPEEVYAVAK-------LAGLHDailRMPHgydtqvgerglKLSGGEKQRV 617
Cdd:COG3842 79 VGMVFQDYALFpHLTVAENVAFGlrMRGVPKAEIRARVAellelvgLEGLAD---RYPH-----------QLSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 618 AIARAILKDPPVILYDEATSSLDSITEEtilgAMRDVVK--HR----TSIFIAHrlstvvD-------ADEIIVLSQGKV 684
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLRE----EMREELRrlQRelgiTFIYVTH------DqeealalADRIAVMNDGRI 214
|
....*
gi 47058990 685 AERGT 689
Cdd:COG3842 215 EQVGT 219
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
472-683 |
9.66e-37 |
|
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: 136.83 E-value: 9.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYIEGQ----KVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQniqdvsleslrra 547
Cdd:cd03250 1 ISVEDASFTWDSGEqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 548 VGVVPQDAVLFHNTIYYNLLYGninaSP--EEVY-AVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAIL 624
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFG----KPfdEERYeKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47058990 625 KDPPVILYDEATSSLDS-----ITEETILGAMRDvvkHRTSIFIAHRLSTVVDADEIIVLSQGK 683
Cdd:cd03250 144 SDADIYLLDDPLSAVDAhvgrhIFENCILGLLLN---NKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
475-688 |
1.71e-36 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 135.26 E-value: 1.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 475 DNVHFEYiEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQd 554
Cdd:cd03214 3 ENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 555 avlfhntiyynllygninaspeevyaVAKLAGLHDAILRmphGYDTqvgerglkLSGGEKQRVAIARAILKDPPVILYDE 634
Cdd:cd03214 81 --------------------------ALELLGLAHLADR---PFNE--------LSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 47058990 635 ATSSLDSITEETILGAMRDVVKHR--TSIFIAHRLSTVVD-ADEIIVLSQGKVAERG 688
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARERgkTVVMVLHDLNLAARyADRVILLKDGRIVAQG 180
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
487-699 |
6.35e-36 |
|
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: 135.54 E-value: 6.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 487 VLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEslRRAVGVVPQDAVLF-HNTIYYN 565
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 566 LLYGNINAS------PEEVYAVAKLAGLHDAILRMPhgydtqvgergLKLSGGEKQRVAIARAILKDPPVILYDEATSSL 639
Cdd:cd03299 92 IAYGLKKRKvdkkeiERKVLEIAEMLGIDHLLNRKP-----------ETLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47058990 640 DSITEETILGAMRDVVKHR--TSIFIAHRLSTV-VDADEIIVLSQGKVAERGTHYGLLANSSS 699
Cdd:cd03299 161 DVRTKEKLREELKKIRKEFgvTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVFKKPKN 223
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
476-696 |
6.55e-36 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 138.26 E-value: 6.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 476 NVHFEYIEGQ-KVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ---KGSIYLAGQNIQDVSLESLR----RA 547
Cdd:COG0444 8 KVYFPTRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELRkirgRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 548 VGVVPQD-----------------AVLFHNtiyynllygniNASPEEVYAVA----KLAGLHDAILRM---PHgydtQvg 603
Cdd:COG0444 88 IQMIFQDpmtslnpvmtvgdqiaePLRIHG-----------GLSKAEARERAiellERVGLPDPERRLdryPH----E-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 604 erglkLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVK-HRTS-IFIAHRLSTVVD-ADEIIVLS 680
Cdd:COG0444 151 -----LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQReLGLAiLFITHDLGVVAEiADRVAVMY 225
|
250
....*....|....*.
gi 47058990 681 QGKVAERGTHYGLLAN 696
Cdd:COG0444 226 AGRIVEEGPVEELFEN 241
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
472-684 |
7.47e-36 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 135.95 E-value: 7.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLRRAV 548
Cdd:COG3638 3 LELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 549 GVVPQDavlfHN-----TIYYNLLYGNINA-----------SPEEV-YAVAKLA--GLHDAILRmphgydtqvgeRGLKL 609
Cdd:COG3638 83 GMIFQQ----FNlvprlSVLTNVLAGRLGRtstwrsllglfPPEDReRALEALErvGLADKAYQ-----------RADQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47058990 610 SGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHR--TSIFIAHRLSTVVD-ADEIIVLSQGKV 684
Cdd:COG3638 148 SGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDgiTVVVNLHQVDLARRyADRIIGLRDGRV 225
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
475-689 |
7.50e-36 |
|
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: 135.94 E-value: 7.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 475 DNVHFEYiEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQ- 553
Cdd:COG1120 5 ENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQe 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 554 ----------DAVLFHNTIYYNLLYGNINASPEEVYAVAKLAGLHDaiLRmphgyDTQVGErglkLSGGEKQRVAIARAI 623
Cdd:COG1120 84 ppapfgltvrELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEH--LA-----DRPVDE----LSGGERQRVLIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47058990 624 LKDPPVILYDEATSSLDSITEETILGAMRDVVKH--RTSIFIAHRLSTVVD-ADEIIVLSQGKVAERGT 689
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErgRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGP 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
467-686 |
1.64e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 134.83 E-value: 1.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 467 PQTATVAFDNVHFEYiEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVsleslRR 546
Cdd:COG1121 2 MMMPAIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 547 AVGVVPQdavlfHNTIYYNL-----------LYGNINASP-------EEVYAVAKLAGLHDaiLRmphgyDTQVGErglk 608
Cdd:COG1121 76 RIGYVPQ-----RAEVDWDFpitvrdvvlmgRYGRRGLFRrpsradrEAVDEALERVGLED--LA-----DRPIGE---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 609 LSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKH-RTSIFIAHRLSTVVD-ADEIIVLSQGKVAE 686
Cdd:COG1121 140 LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREgKTILVVTHDLGAVREyFDRVLLLNRGLVAH 219
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
472-684 |
2.16e-35 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 133.42 E-value: 2.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYiEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNI--QDVSLESLRRAVG 549
Cdd:cd03262 1 IEIKNLHKSF-GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 550 VVPQDAVLF-HNTIYYNLLYGNINA---SPEEVYAVA----KLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIAR 621
Cdd:cd03262 80 MVFQQFNLFpHLTVLENITLAPIKVkgmSKAEAEERAlellEKVGLADKADAYPA-----------QLSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47058990 622 AILKDPPVILYDEATSSLDSITEETILGAMRDVVK-HRTSIFIAHRLSTVVD-ADEIIVLSQGKV 684
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEeGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
466-686 |
3.36e-35 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 134.45 E-value: 3.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 466 TPQTATVAFDNVHFEYIEGQK---VLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIqdvslE 542
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGGGgvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV-----T 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 543 SLRRAVGVVPQDAVLF-HNTIYYNLLYG--NINASPEEVYAVA----KLAGLHDAILRMPHgydtQvgerglkLSGGEKQ 615
Cdd:COG1116 77 GPGPDRGVVFQEPALLpWLTVLDNVALGleLRGVPKAERRERArellELVGLAGFEDAYPH----Q-------LSGGMRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 616 RVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVK--HRTSIFIAH------RLstvvdADEIIVLSQ--GKVA 685
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQetGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIV 220
|
.
gi 47058990 686 E 686
Cdd:COG1116 221 E 221
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
484-684 |
3.51e-35 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 131.37 E-value: 3.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 484 GQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDvSLESLRRAVGVVPQDAVLfhntiY 563
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPEEPSL-----Y 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 564 YNLlygninaSPEEVyavaklaglhdailrmphgydtqvgergLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSIT 643
Cdd:cd03230 86 ENL-------TVREN----------------------------LKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPES 130
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 47058990 644 EETILGAMRDVVKHRTSIFIA-HRLSTVVD-ADEIIVLSQGKV 684
Cdd:cd03230 131 RREFWELLRELKKEGKTILLSsHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
140-424 |
8.01e-35 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 133.92 E-value: 8.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 140 VAISLGFLGGAKAMNIVVPFMFKYAVDSLNQmsgnmlNLSDAPNTVATMATAVLIGYgvsrAGAAFFNEVRNAVFGKVAQ 219
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLP------DGDPETQALNVYSLALLLLG----LAQFILSFLQSYLLNHTGE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 220 NSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIVFEMTLVSSVLYYKcGAQFALVTLG 299
Cdd:pfam00664 71 RLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYY-GWKLTLVLLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 300 TLGAYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNEKYEAQRYDGFLKTYETASLKSTSTLAMLNF 379
Cdd:pfam00664 150 VLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFG 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 47058990 380 GQSAIFSVGLTAIMVLASQGIVAGALTVGDLVMVNGLLFQLSLPL 424
Cdd:pfam00664 230 ITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
472-684 |
1.24e-34 |
|
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: 131.38 E-value: 1.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDV---SLESLRRAV 548
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 549 GVVPQDA-VLFHNTIYYNLLYGN--INASPEE----VYAVAKLAGLHDAILRMPHGydtqvgerglkLSGGEKQRVAIAR 621
Cdd:cd03292 81 GVVFQDFrLLPDRNVYENVAFALevTGVPPREirkrVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47058990 622 AILKDPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIFIAHRLSTVVDA--DEIIVLSQGKV 684
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTtrHRVIALERGKL 214
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
472-689 |
3.21e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 131.80 E-value: 3.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYIEGQK-VLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGV 550
Cdd:PRK13648 8 IVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 551 VPQ--DAVLFHNTIYYNLLYGNINAS------PEEVYAVAKLAGLHDAILRMPHGydtqvgerglkLSGGEKQRVAIARA 622
Cdd:PRK13648 88 VFQnpDNQFVGSIVKYDVAFGLENHAvpydemHRRVSEALKQVDMLERADYEPNA-----------LSGGQKQRVAIAGV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47058990 623 ILKDPPVILYDEATSSLDSITEETILGAMRDV--VKHRTSIFIAHRLSTVVDADEIIVLSQGKVAERGT 689
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVksEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGT 225
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
475-689 |
7.65e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 130.91 E-value: 7.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 475 DNVHFEYIEGQK-VLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQ 553
Cdd:PRK13635 9 EHISFRYPDAATyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 554 --DAVLFHNTIYYNLLYG--NINASPEE----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILK 625
Cdd:PRK13635 89 npDNQFVGATVQDDVAFGleNIGVPREEmverVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAIAGVLAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47058990 626 DPPVILYDEATSSLDSITEETILGAMRDVVKHR--TSIFIAHRLSTVVDADEIIVLSQGKVAERGT 689
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEGT 223
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
491-689 |
8.71e-34 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 132.93 E-value: 8.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 491 VSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQD----VSLESLRRAVGVVPQDAVLF-HNTIYYN 565
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgIFLPPEKRRIGYVFQEARLFpHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 566 LLYGNINASPEEVYAVaklaglHDAILRMpHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEE 645
Cdd:TIGR02142 96 LRYGMKRARPSERRIS------FERVIEL-LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 47058990 646 TILGAMRDVVKHRT--SIFIAHRLSTVVD-ADEIIVLSQGKVAERGT 689
Cdd:TIGR02142 169 EILPYLERLHAEFGipILYVSHSLQEVLRlADRVVVLEDGRVAAAGP 215
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
140-441 |
1.81e-33 |
|
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: 130.36 E-value: 1.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 140 VAISLGFLGGAKAMNIVVPFMFKYAVDSLnqmsgnmlnLSDAPNTVATMATAVLIGYGVSRAGAAFFnevRNAVFGKVAQ 219
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDV---------IPAGDLSLLLWIALLLLLLALLRALLSYL---RRYLAARLGQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 220 NSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIVFEMTLVSSVLYYKcGAQFALVTLG 299
Cdd:cd07346 69 RVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYL-NWKLTLVALL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 300 TLGAYTAFTVAVTRW-RTRFRIEMNKADNDAGNAAiDSLLNYETVKYFNNEKYEAQRYDGFLKTYETASLKSTSTLAMLN 378
Cdd:cd07346 148 LLPLYVLILRYFRRRiRKASREVRESLAELSAFLQ-ESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFS 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47058990 379 FGQSAIFSVGLTAIMVLASQGIVAGALTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDM 441
Cdd:cd07346 227 PLIGLLTALGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASL 289
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
474-689 |
2.11e-33 |
|
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: 128.45 E-value: 2.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 474 FDNVHFEYIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNI---QDVSLESLRRAVGV 550
Cdd:cd03256 3 VENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklKGKALRQLRRQIGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 551 VPQDavlfHN-----TIYYNLLYGNINASPeevyavaklagLHDAILRMPHGYDTQ--------VG------ERGLKLSG 611
Cdd:cd03256 83 IFQQ----FNlierlSVLENVLSGRLGRRS-----------TWRSLFGLFPKEEKQralaalerVGlldkayQRADQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 612 GEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHR--TSIFIAHRLSTVVD-ADEIIVLSQGKVAERG 688
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLAREyADRIVGLKDGRIVFDG 227
|
.
gi 47058990 689 T 689
Cdd:cd03256 228 P 228
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
472-696 |
1.55e-32 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 129.04 E-value: 1.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYIEGQK---VLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLR 545
Cdd:COG1135 2 IELENLSKTFPTKGGpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSereLRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 546 RAVGVVPQdavlfHntiyYNLL-----YGNInASPEEVYAVAK---------------LAGLHDAilrmphgYDTQvger 605
Cdd:COG1135 82 RKIGMIFQ-----H----FNLLssrtvAENV-ALPLEIAGVPKaeirkrvaellelvgLSDKADA-------YPSQ---- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 606 glkLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHR--TSIFIAHRLSTVVD-ADEIIVLSQG 682
Cdd:COG1135 141 ---LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELglTIVLITHEMDVVRRiCDRVAVLENG 217
|
250
....*....|....
gi 47058990 683 KVAERGTHYGLLAN 696
Cdd:COG1135 218 RIVEQGPVLDVFAN 231
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
474-685 |
2.34e-32 |
|
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: 124.57 E-value: 2.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 474 FDNVHFEYiEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVsleslRRAVGVVPQ 553
Cdd:cd03235 2 VEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 554 -------------DAVLFHNTIYYNLLYGNINASPEEVYAVAKLAGLHDAILRmphgydtQVGErglkLSGGEKQRVAIA 620
Cdd:cd03235 76 rrsidrdfpisvrDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADR-------QIGE----LSGGQQQRVLLA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47058990 621 RAILKDPPVILYDEATSSLDSITEETILGAMRDVVKH-RTSIFIAHRLSTVVD-ADEIIVLSQGKVA 685
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEyFDRVLLLNRTVVA 211
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
475-684 |
2.84e-32 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 124.29 E-value: 2.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 475 DNVHFEYIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIqdvSLESLRRAVGVVPQD 554
Cdd:cd03226 3 ENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 555 A--VLFHNTIYYNLLYGNINAS--PEEVYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVI 630
Cdd:cd03226 80 VdyQLFTDSVREELLLGLKELDagNEQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 47058990 631 LYDEATSSLDSITEETILGAMRDVVKHRTSIF-IAHR---LSTVvdADEIIVLSQGKV 684
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAAQGKAVIvITHDyefLAKV--CDRVLLLANGAI 204
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
472-689 |
3.44e-32 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 125.04 E-value: 3.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYiEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDvsLESLRRAVGVV 551
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN--LPPHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 552 PQDAVLF-HNTIYYNLLYG------NINASPEEVYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAIL 624
Cdd:cd03300 78 FQNYALFpHLTVFENIAFGlrlkklPKAEIKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARALV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 625 KDPPVILYDEATSSLDSITEETILGAMRDVvkHR----TSIFIAHRLS-TVVDADEIIVLSQGKVAERGT 689
Cdd:cd03300 147 NEPKVLLLDEPLGALDLKLRKDMQLELKRL--QKelgiTFVFVTHDQEeALTMSDRIAVMNKGKIQQIGT 214
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
475-689 |
7.15e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 125.55 E-value: 7.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 475 DNVHFEYIEG----QKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQD--VSLESLRRAV 548
Cdd:PRK13637 6 ENLTHIYMEGtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIRKKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 549 GVVPQ--DAVLFHNTIYYNLLYG--NINASPEE----VYAVAKLAGLHdailrmphgYDTQVGERGLKLSGGEKQRVAIA 620
Cdd:PRK13637 86 GLVFQypEYQLFEETIEKDIAFGpiNLGLSEEEienrVKRAMNIVGLD---------YEDYKDKSPFELSGGQKRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47058990 621 RAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHR--TSIFIAHRLSTVVD-ADEIIVLSQGKVAERGT 689
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
486-689 |
1.13e-31 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 126.80 E-value: 1.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 486 KVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIqDVSLESLRRAVGVVPQDAVLF-HNTIYY 564
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL-FTNLPPRERRVGFVFQHYALFpHMTVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 565 NLLYG--NINASPEEVYAVA-------KLAGLHDailRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYDEA 635
Cdd:COG1118 95 NIAFGlrVRPPSKAEIRARVeellelvQLEGLAD---RYPS-----------QLSGGQRQRVALARALAVEPEVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47058990 636 TSSLDSITEETILGAMRDVVK--HRTSIFIAH------RLstvvdADEIIVLSQGKVAERGT 689
Cdd:COG1118 161 FGALDAKVRKELRRWLRRLHDelGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGT 217
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
491-688 |
1.37e-31 |
|
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: 122.40 E-value: 1.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 491 VSFEVPAGKkVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQD----VSLESLRRAVGVVPQDAVLF-HNTIYYN 565
Cdd:cd03297 17 IDFDLNEEV-TGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkINLPPQQRKIGLVFQQYALFpHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 566 LLYG-NINASPEEVYAVAKLAGLHDAilrmphgydTQVGERG-LKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSIT 643
Cdd:cd03297 96 LAFGlKRKRNREDRISVDELLDLLGL---------DHLLNRYpAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 47058990 644 EETILGAMRDVVK--HRTSIFIAHRLSTVVD-ADEIIVLSQGKVAERG 688
Cdd:cd03297 167 RLQLLPELKQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
491-701 |
1.38e-31 |
|
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: 124.29 E-value: 1.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 491 VSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESL----RRAVGVVPQDAVLF-HNTIYYN 565
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpHRTVLEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 566 LLYG----NINASPEEVYA--VAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYDEATSSL 639
Cdd:cd03294 123 VAFGlevqGVPRAEREERAaeALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47058990 640 DSiteeTILGAMRDVV------KHRTSIFIAHRLSTVVD-ADEIIVLSQGKVAERGTHYGLLANSSSIY 701
Cdd:cd03294 192 DP----LIRREMQDELlrlqaeLQKTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
470-688 |
1.72e-31 |
|
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: 121.50 E-value: 1.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 470 ATVAFDNV-----HFEYIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLL--FRFYEPQKGSIYLAGQNIqdvSLE 542
Cdd:cd03213 2 VTLSFRNLtvtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPL---DKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 543 SLRRAVGVVPQDAVLF-HNTIYYNLLYgninaspeevyaVAKLAGLhdailrmphgydtqvgerglklSGGEKQRVAIAR 621
Cdd:cd03213 79 SFRKIIGYVPQDDILHpTLTVRETLMF------------AAKLRGL----------------------SGGERKRVSIAL 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 622 AILKDPPVILYDEATSSLDSITEETILGAMRDVVK-HRTSIFIAHRLSTVV--DADEIIVLSQGKVAERG 688
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADtGRTIICSIHQPSSEIfeLFDKLLLLSQGRVIYFG 194
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
470-689 |
1.87e-31 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 125.96 E-value: 1.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 470 ATVAFDNVHFEYiEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEslRRAVG 549
Cdd:COG3839 2 ASLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 550 VVPQDAVLF-HNTIYYNLLYG--NINASPEE----VYAVAKLAGLhDAIL-RMPhgydtqvgergLKLSGGEKQRVAIAR 621
Cdd:COG3839 79 MVFQSYALYpHMTVYENIAFPlkLRKVPKAEidrrVREAAELLGL-EDLLdRKP-----------KQLSGGQRQRVALGR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 622 AILKDPPVILYDEATSSLDsiteetilgA-----MRDVVK--HR----TSIFIAHrlstvvD-------ADEIIVLSQGK 683
Cdd:COG3839 147 ALVREPKVFLLDEPLSNLD---------AklrveMRAEIKrlHRrlgtTTIYVTH------DqveamtlADRIAVMNDGR 211
|
....*.
gi 47058990 684 VAERGT 689
Cdd:COG3839 212 IQQVGT 217
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
487-702 |
2.69e-31 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 123.10 E-value: 2.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 487 VLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNL 566
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 567 lYGNINASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEET 646
Cdd:cd03288 116 -DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENI 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 47058990 647 ILGAMRDVVKHRTSIFIAHRLSTVVDADEIIVLSQGKVAERGTHYGLLANSSSIYS 702
Cdd:cd03288 195 LQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFA 250
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
459-648 |
5.41e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 122.07 E-value: 5.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 459 MASPLQITPQTATVafDNVHFEYieGQK-VLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE--PQ---KGSIYLA 532
Cdd:COG1117 1 MTAPASTLEPKIEV--RNLNVYY--GDKqALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGarvEGEILLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 533 GQNI--QDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGninaspeevyavAKLAGLH-----DAI----LRmphgydtQ 601
Cdd:COG1117 77 GEDIydPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYG------------LRLHGIKskselDEIveesLR-------K 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47058990 602 VG----------ERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSIT----EETIL 648
Cdd:COG1117 138 AAlwdevkdrlkKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIStakiEELIL 198
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
486-689 |
8.12e-31 |
|
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: 127.49 E-value: 8.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 486 KVLSGVSFEVPAGKKVAIVGGSGSGKST----IVRLLfrfyePQKGSIYLAGQNIQDVS---LESLRRAVGVVPQDAvlf 558
Cdd:COG4172 300 KAVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 559 hntiyynllYGNIN-------------------ASPEEVYA-VAKL---AGLH-DAILRMPHgydtqvgerglKLSGGEK 614
Cdd:COG4172 372 ---------FGSLSprmtvgqiiaeglrvhgpgLSAAERRArVAEAleeVGLDpAARHRYPH-----------EFSGGQR 431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47058990 615 QRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHR--TSIFIAHRLStVVDA--DEIIVLSQGKVAERGT 689
Cdd:COG4172 432 QRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHglAYLFISHDLA-VVRAlaHRVMVMKDGKVVEQGP 509
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
484-696 |
8.56e-31 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 121.40 E-value: 8.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 484 GQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNI--------QDVSLESLRRAVGVVPQDA 555
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqQKGLIRQLRQHVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 556 VLF-HNTIYYNLLYGNI---NASPEEVYAVAK-------LAGLHDAILRmphgydtqvgerglKLSGGEKQRVAIARAIL 624
Cdd:PRK11264 95 NLFpHRTVLENIIEGPVivkGEPKEEATARARellakvgLAGKETSYPR--------------RLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47058990 625 KDPPVILYDEATSSLDSITEETILGAMRDVVKH-RTSIFIAHRLSTVVD-ADEIIVLSQGKVAERGTHYGLLAN 696
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
486-688 |
9.35e-31 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 123.69 E-value: 9.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 486 KVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLRRAVGVVPQD--AVLfhN 560
Cdd:COG4608 32 KAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDpyASL--N 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 561 ---TIyynllyGNINASPEEVYAVAKLAGLHDAILRM--------------PHgydtqvgerglKLSGGEKQRVAIARAI 623
Cdd:COG4608 110 prmTV------GDIIAEPLRIHGLASKAERRERVAELlelvglrpehadryPH-----------EFSGGQRQRIGIARAL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 624 LKDPPVILYDEATSSLD-SItEETILGAMRDVVKHR--TSIFIAHRLStVVD--ADEIIVLSQGKVAERG 688
Cdd:COG4608 173 ALNPKLIVCDEPVSALDvSI-QAQVLNLLEDLQDELglTYLFISHDLS-VVRhiSDRVAVMYLGKIVEIA 240
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
474-689 |
5.21e-30 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 121.83 E-value: 5.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 474 FDNVHFEYIEGQK---VLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLRRA 547
Cdd:PRK11153 4 LKNISKVFPQGGRtihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekeLRKARRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 548 VGVVPQdavlfHntiyYNLL-----YGNI-------NASPEEVYA-VA---KLAGL---HDAilrmphgYDTQvgerglk 608
Cdd:PRK11153 84 IGMIFQ-----H----FNLLssrtvFDNValplelaGTPKAEIKArVTellELVGLsdkADR-------YPAQ------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 609 LSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVK--HRTSIFIAHRLStVVD--ADEIIVLSQGKV 684
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMD-VVKriCDRVAVIDAGRL 219
|
....*
gi 47058990 685 AERGT 689
Cdd:PRK11153 220 VEQGT 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
488-689 |
8.44e-30 |
|
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: 118.21 E-value: 8.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 488 LSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEslRRAVGVVPQDAVLF-HNTIYYNL 566
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFrHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 567 LYG-------------NINASPEEVYAVAKLAGLHDailRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYD 633
Cdd:cd03296 96 AFGlrvkprserppeaEIRAKVHELLKLVQLDWLAD---RYPA-----------QLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 47058990 634 EATSSLDSITEETILGAMRDVVK--HRTSIFIAHRLSTVVD-ADEIIVLSQGKVAERGT 689
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEEALEvADRVVVMNKGRIEQVGT 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
484-685 |
1.09e-29 |
|
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: 115.22 E-value: 1.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 484 GQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS-LESLRRAVGVVPQdavlfhnti 562
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGIAMVYQ--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 563 yynllygninaspeevyavaklaglhdailrmphgydtqvgerglkLSGGEKQRVAIARAILKDPPVILYDEATSSLDSI 642
Cdd:cd03216 83 ----------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPA 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 47058990 643 TEETILGAMRDVVKH-RTSIFIAHRLSTVVD-ADEIIVLSQGKVA 685
Cdd:cd03216 117 EVERLFKVIRRLRAQgVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
420-730 |
1.14e-29 |
|
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: 126.60 E-value: 1.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 420 LSLPLNFLGTVYRETRQALIDMNTLFTLLKVDTRIKDKAMASPLQITPQTAtVAFDNVHFEYIEGQK-VLSGVSFEVPAG 498
Cdd:TIGR00957 586 LRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPGEGNS-ITVHNATFTWARDLPpTLNGITFSIPEG 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 499 KKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGqniqdvsleslrrAVGVVPQDAVLFHNTIYYNLLYG---NINASP 575
Cdd:TIGR00957 665 ALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENILFGkalNEKYYQ 731
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 576 EEVYAVAKLAGLHdailRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITE----ETILGAM 651
Cdd:TIGR00957 732 QVLEACALLPDLE----ILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGkhifEHVIGPE 807
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47058990 652 rDVVKHRTSIFIAHRLSTVVDADEIIVLSQGKVAERGTHYGLLANSSSIYSEMWHTQSTRIQNHDNLGWDAKKESLSKE 730
Cdd:TIGR00957 808 -GVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAPDEQQGHLEDSWTALVSGEGKE 885
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
475-696 |
1.86e-29 |
|
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: 116.76 E-value: 1.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 475 DNVHFEYIEGQkVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLES-LRRAVGVVPQ 553
Cdd:cd03224 4 ENLNAGYGKSQ-ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 554 DAVLFHN-TIYYNLLYG-------NINASPEEVYAV--------AKLAGLhdailrmphgydtqvgerglkLSGGEKQRV 617
Cdd:cd03224 83 GRRIFPElTVEENLLLGayarrraKRKARLERVYELfprlkerrKQLAGT---------------------LSGGEQQML 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 618 AIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIFI----AHRLSTVvdADEIIVLSQGKVAERGTHYGL 693
Cdd:cd03224 142 AIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLveqnARFALEI--ADRAYVLERGRVVLEGTAAEL 219
|
...
gi 47058990 694 LAN 696
Cdd:cd03224 220 LAD 222
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
476-738 |
2.95e-29 |
|
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: 117.65 E-value: 2.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 476 NVHFEYIE-GQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQkGSIYLAGQNIQDVSLESLRRAVGVVPQD 554
Cdd:cd03289 7 DLTAKYTEgGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGVIPQK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 555 AVLFHNTIYYNL-LYGniNASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYD 633
Cdd:cd03289 86 VFIFSGTFRKNLdPYG--KWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 634 EATSSLDSITEETILGAMRDVVKHRTSIFIAHRLSTVVDADEIIVLSQGKVAERGTHYGLLANSSSIYSEMWHTQSTRIQ 713
Cdd:cd03289 164 EPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAISPSDRLKLF 243
|
250 260
....*....|....*....|....*....
gi 47058990 714 NHDNLGWDAKKESLS----KEEERKKLQE 738
Cdd:cd03289 244 PRRNSSKSKRKPRPQiqalQEETEEEVQD 272
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
337-704 |
3.71e-29 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 125.09 E-value: 3.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 337 LLNYETVKYFNNEKYEAQRYDGfLKTYETASLKSTSTLAMLNfgqsaIFSVGLTAIMV-LASQGIVAgaLTVGDLVMVNG 415
Cdd:PLN03232 486 LASMDTVKCYAWEKSFESRIQG-IRNEELSWFRKAQLLSAFN-----SFILNSIPVVVtLVSFGVFV--LLGGDLTPARA 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 416 L----LFQ-LSLPLNFLGTVYRETRQALIDMNTLFTLLKVDTRIKdkAMASPLQitPQTATVAFDNVHFEYIE--GQKVL 488
Cdd:PLN03232 558 FtslsLFAvLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEERIL--AQNPPLQ--PGAPAISIKNGYFSWDSktSKPTL 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 489 SGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPqkgsiylagqnIQDVSLEsLRRAVGVVPQDAVLFHNTIYYNLLY 568
Cdd:PLN03232 634 SDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH-----------AETSSVV-IRGSVAYVPQVSWIFNATVRENILF 701
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 569 GNINASPEEVYAVAKLAGLHDaiLRMPHGYD-TQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDS-ITEET 646
Cdd:PLN03232 702 GSDFESERYWRAIDVTALQHD--LDLLPGRDlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAhVAHQV 779
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 47058990 647 ILGAMRDVVKHRTSIFIAHRLSTVVDADEIIVLSQGKVAERGThYGLLANSSSIYSEM 704
Cdd:PLN03232 780 FDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGT-FAELSKSGSLFKKL 836
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
475-688 |
9.29e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 116.37 E-value: 9.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 475 DNVHFEYIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQD 554
Cdd:PRK13647 8 EDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 555 A--VLFHNTIYYNLLYGNINA--SPEE----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKD 626
Cdd:PRK13647 88 PddQVFSSTVWDDVAFGPVNMglDKDEverrVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47058990 627 PPVILYDEATSSLDSITEETILGAMRDVVKHRTSIFIA-HRLSTVVD-ADEIIVLSQGKVAERG 688
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEG 220
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
491-689 |
2.28e-28 |
|
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: 117.12 E-value: 2.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 491 VSFEVPAGKKVAIVGGSGSGKSTIVRL---LFRfyePQKGSIYLAGQNIQD----VSLESLRRAVGVVPQDAVLF-HNTI 562
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEVLQDsargIFLPPHRRRIGYVFQEARLFpHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 563 YYNLLYG-------NINASPEEVYAVAKLAGLHDailRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYDEA 635
Cdd:COG4148 95 RGNLLYGrkrapraERRISFDEVVELLGIGHLLD---RRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47058990 636 TSSLDSITEETILGAMRDvVKHRTSI---FIAH------RLstvvdADEIIVLSQGKVAERGT 689
Cdd:COG4148 161 LAALDLARKAEILPYLER-LRDELDIpilYVSHsldevaRL-----ADHVVLLEQGRVVASGP 217
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
472-688 |
2.30e-28 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 113.12 E-value: 2.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYiEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVslESLRRAVGVV 551
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDL--PPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 552 PQDAVLF-HNTIYYNLLYG-NINASPEE-----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAIL 624
Cdd:cd03301 78 FQNYALYpHMTVYDNIAFGlKLRKVPKDeiderVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRAIV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47058990 625 KDPPVILYDEATSSLDSITEEtilgAMRDVVK--HR----TSIFIAH-RLSTVVDADEIIVLSQGKVAERG 688
Cdd:cd03301 147 REPKVFLMDEPLSNLDAKLRV----QMRAELKrlQQrlgtTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
486-689 |
3.86e-28 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 115.83 E-value: 3.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 486 KVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLE---SLRRAVGVVpqdavlFHNTi 562
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEaqkLLRQKIQIV------FQNP- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 563 yynllYGNINasPEevyavaKLAGlhdAILRMPHGYDTQVG--ER-----------GLK----------LSGGEKQRVAI 619
Cdd:PRK11308 102 -----YGSLN--PR------KKVG---QILEEPLLINTSLSaaERrekalammakvGLRpehydryphmFSGGQRQRIAI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47058990 620 ARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKH-RTS-IFIAHRLStVVD--ADEIIVLSQGKVAERGT 689
Cdd:PRK11308 166 ARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSyVFISHDLS-VVEhiADEVMVMYLGRCVEKGT 238
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
495-688 |
5.81e-28 |
|
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: 112.20 E-value: 5.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 495 VPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIqdVSLESLRRAVGVVPQDAVLF-HNTIYYNLLYG---N 570
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV--TAAPPADRPVSMLFQENNLFaHLTVEQNVGLGlspG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 571 INASPEEVYAVAKLA---GLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETI 647
Cdd:cd03298 99 LKLTAEDRQAIEVALarvGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 47058990 648 LGAMRDVVKHR--TSIFIAHRLSTVVD-ADEIIVLSQGKVAERG 688
Cdd:cd03298 168 LDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
417-697 |
1.73e-27 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 119.84 E-value: 1.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 417 LFQ-LSLPLNFLGTVYRETRQALIDMNTLFTLLKVDTRIkdkaMASPLQITPQTATVAFDNVHFEY-IEGQK-VLSGVSF 493
Cdd:PLN03130 563 LFAvLRFPLFMLPNLITQAVNANVSLKRLEELLLAEERV----LLPNPPLEPGLPAISIKNGYFSWdSKAERpTLSNINL 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 494 EVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLagqniqdvslesLRRAVGVVPQDAVLFHNTIYYNLLYGNiNA 573
Cdd:PLN03130 639 DVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVAYVPQVSWIFNATVRDNILFGS-PF 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 574 SPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDS-ITEETILGAMR 652
Cdd:PLN03130 706 DPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAhVGRQVFDKCIK 785
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 47058990 653 DVVKHRTSIFIAHRLSTVVDADEIIVLSQGKVAERGTHYGLLANS 697
Cdd:PLN03130 786 DELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNG 830
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
474-689 |
3.86e-27 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 110.23 E-value: 3.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 474 FDNVHFEYieGQKVLSgVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIqdVSLESLRRAVGVVPQ 553
Cdd:COG3840 4 LDDLTYRY--GDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL--TALPPAERPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 554 DAVLF-HNTIYYNLLYG---NINASPEEVYAVAKLA---GLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKD 626
Cdd:COG3840 79 ENNLFpHLTVAQNIGLGlrpGLKLTAEQRAQVEQALervGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47058990 627 PPVILYDEATSSLDSITEETILGAMRDVVKHR--TSIFIAHRLSTVVD-ADEIIVLSQGKVAERGT 689
Cdd:COG3840 148 RPILLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHDPEDAARiADRVLLVADGRIAADGP 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
472-699 |
7.97e-27 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 109.80 E-value: 7.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNV--HFeyieGQ-KVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQD--VSLESLRR 546
Cdd:PRK09493 2 IEFKNVskHF----GPtQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 547 AVGVVPQDAVLF-HNTIYYNLLYGNIN---ASPEEVYAVAK--LA--GLHDailRMPHgYDTQvgerglkLSGGEKQRVA 618
Cdd:PRK09493 78 EAGMVFQQFYLFpHLTALENVMFGPLRvrgASKEEAEKQARelLAkvGLAE---RAHH-YPSE-------LSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 619 IARAILKDPPVILYDEATSSLDSITEETILGAMRD---------VVKHRtsIFIAHRLSTvvdadEIIVLSQGKVAERGT 689
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDlaeegmtmvIVTHE--IGFAEKVAS-----RLIFIDKGRIAEDGD 219
|
250
....*....|
gi 47058990 690 HYGLLANSSS 699
Cdd:PRK09493 220 PQVLIKNPPS 229
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
465-688 |
8.39e-27 |
|
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: 108.99 E-value: 8.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 465 ITPQTATVAFDNVHFEYiegqKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESL 544
Cdd:cd03266 2 ITADALTKRFRDVKKTV----QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 545 RRaVGVVPQDAVLF------HNTIYYNLLYG----NINAspeevyAVAKLAGLhdaiLRMPHGYDTQVGErglkLSGGEK 614
Cdd:cd03266 78 RR-LGFVSDSTGLYdrltarENLEYFAGLYGlkgdELTA------RLEELADR----LGMEELLDRRVGG----FSTGMR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 615 QRVAIARAILKDPPVILYDEATSSLDSITEETIlgamRDVVKH-----RTSIFIAHRLSTVVD-ADEIIVLSQGKVAERG 688
Cdd:cd03266 143 QKVAIARALVHDPPVLLLDEPTTGLDVMATRAL----REFIRQlralgKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
484-683 |
2.13e-26 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 107.18 E-value: 2.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 484 GQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIY 563
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGHADGLKPELTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 564 YNL-----LYGnINASPEEVYAVAKLAGLHDAIlrmphgyDTQVGerglKLSGGEKQRVAIARAILKDPPVILYDEATSS 638
Cdd:COG4133 94 ENLrfwaaLYG-LRADREAIDEALEAVGLAGLA-------DLPVR----QLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 47058990 639 LDSITEETILGAMRDVVKHRTSIFIAHRLSTVVDADEIIVLSQGK 683
Cdd:COG4133 162 LDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAARVLDLGDFK 206
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
467-654 |
2.74e-26 |
|
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: 107.90 E-value: 2.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 467 PQTATVAFDNVHFEYIEGQK---VLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLES 543
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 544 L----RRAVGVVPQDavlFHntiyynlLYGNINASpEEVYAVAKLAGLHDA------IL-------RMPHgYDTQvgerg 606
Cdd:COG4181 84 RarlrARHVGFVFQS---FQ-------LLPTLTAL-ENVMLPLELAGRRDArararaLLervglghRLDH-YPAQ----- 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 47058990 607 lkLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDV 654
Cdd:COG4181 147 --LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFEL 192
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
455-689 |
3.41e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 111.19 E-value: 3.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 455 KDKAMASPLQITPqtaTVAFDNVHFEYiEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQ 534
Cdd:PRK09452 1 SKKLNKQPSSLSP---LVELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 535 NIQDVSLEslRRAVGVVPQDAVLF-HNTIYYNLLYG---------NINASPEEVYAVAKLAGLHDailRMPHgydtqvge 604
Cdd:PRK09452 77 DITHVPAE--NRHVNTVFQSYALFpHMTVFENVAFGlrmqktpaaEITPRVMEALRMVQLEEFAQ---RKPH-------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 605 rglKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSiteeTILGAMRDVVKH--R----TSIFIAH----RLSTvvdAD 674
Cdd:PRK09452 144 ---QLSGGQQQRVAIARAVVNKPKVLLLDESLSALDY----KLRKQMQNELKAlqRklgiTFVFVTHdqeeALTM---SD 213
|
250
....*....|....*
gi 47058990 675 EIIVLSQGKVAERGT 689
Cdd:PRK09452 214 RIVVMRDGRIEQDGT 228
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
476-689 |
3.69e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 108.74 E-value: 3.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 476 NVHFEYIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQ-- 553
Cdd:PRK13652 8 DLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQnp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 554 DAVLFHNTIYYNLLYGNINASPEE------VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDP 627
Cdd:PRK13652 88 DDQIFSPTVEQDIAFGPINLGLDEetvahrVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47058990 628 PVILYDEATSSLDSITEETILGAMRDVVKH--RTSIFIAHRLSTVVD-ADEIIVLSQGKVAERGT 689
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGT 221
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
468-680 |
4.14e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 107.11 E-value: 4.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 468 QTATVAFDNVHFEyIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRA 547
Cdd:PRK10247 4 NSPLLQLQNVGYL-AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 548 VGVVPQDAVLFHNTIYYNLL--YGNINASPEEVYAVAKLA--GLHDAILRMPhgydtqVGErglkLSGGEKQRVAIARAI 623
Cdd:PRK10247 83 VSYCAQTPTLFGDTVYDNLIfpWQIRNQQPDPAIFLDDLErfALPDTILTKN------IAE----LSGGEKQRISLIRNL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47058990 624 LKDPPVILYDEATSSLDS----ITEETILGAMRDvvKHRTSIFIAHRLSTVVDADEIIVLS 680
Cdd:PRK10247 153 QFMPKVLLLDEITSALDEsnkhNVNEIIHRYVRE--QNIAVLWVTHDKDEINHADKVITLQ 211
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
475-688 |
4.57e-26 |
|
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: 106.51 E-value: 4.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 475 DNVHFEYiEGQKVLSGVSFEVPAGKkVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDvSLESLRRAVGVVPQD 554
Cdd:cd03264 4 ENLTKRY-GKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 555 AVLFHN-TIYYNLLY----GNINAS--PEEVYAVAKLAGLHDAilrmphgYDTQVGerglKLSGGEKQRVAIARAILKDP 627
Cdd:cd03264 81 FGVYPNfTVREFLDYiawlKGIPSKevKARVDEVLELVNLGDR-------AKKKIG----SLSGGMRRRVGIAQALVGDP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47058990 628 PVILYDEATSSLDSitEETI--LGAMRDVVKHRTSIFIAHRLSTVVD-ADEIIVLSQGKVAERG 688
Cdd:cd03264 150 SILIVDEPTAGLDP--EERIrfRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
485-684 |
5.11e-26 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 106.82 E-value: 5.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 485 QKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDvSLESLRRAVGVVPQDAVLFHN-TI- 562
Cdd:cd03263 15 KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALFDElTVr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 563 ----YYNLLYG-NINASPEEVYAVAKLAGLHDAIlrmphgyDTQVGErglkLSGGEKQRVAIARAILKDPPVILYDEATS 637
Cdd:cd03263 94 ehlrFYARLKGlPKSEIKEEVELLLRVLGLTDKA-------NKRART----LSGGMKRKLSLAIALIGGPSVLLLDEPTS 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 47058990 638 SLDSITEETILGAMRDVVKHRTSIFIAHRLSTV-VDADEIIVLSQGKV 684
Cdd:cd03263 163 GLDPASRRAIWDLILEVRKGRSIILTTHSMDEAeALCDRIAIMSDGKL 210
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
334-738 |
8.61e-26 |
|
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: 114.24 E-value: 8.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 334 IDSLLNYETVKYFNNEKYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAIFSVGLTAIMVLA------SQGIVAGALTV 407
Cdd:TIGR01271 1068 ITSLKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDIIFVFFFIAVTFIAigtnqdGEGEVGIILTL 1147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 408 GDLVM------------VNGLLFQLSLPLNFLGTVYRETR-QALIDMNTLFTLLKVDTRIKDKAMASPLQITPQTATVAF 474
Cdd:TIGR01271 1148 AMNILstlqwavnssidVDGLMRSVSRVFKFIDLPQEEPRpSGGGGKYQLSTVLVIENPHAQKCWPSGGQMDVQGLTAKY 1227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 475 DNvhfeyiEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQkGSIYLAGQNIQDVSLESLRRAVGVVPQD 554
Cdd:TIGR01271 1228 TE------AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQK 1300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 555 AVLFHNTIYYNLlYGNINASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDE 634
Cdd:TIGR01271 1301 VFIFSGTFRKNL-DPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDE 1379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 635 ATSSLDSITEETILGAMRDVVKHRTSIFIAHRLSTVVDADEIIVLSQGKVAERGTHYGLLANSSSIYSEMWHTQSTRI-- 712
Cdd:TIGR01271 1380 PSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAMSAADRLKLfp 1459
|
410 420
....*....|....*....|....*...
gi 47058990 713 QNHDNLGWDAKKESLS--KEEERKKLQE 738
Cdd:TIGR01271 1460 LHRRNSSKRKPQPKITalREEAEEEVQN 1487
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
472-688 |
1.32e-25 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 106.32 E-value: 1.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYiEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKG-SIYLAGQNIQDVSLESLRRAVGV 550
Cdd:COG1119 4 LELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 551 VPQDavlFHNTIYYNL---------LYGNI----NASPEEVYAVAKLAglhdAILRMPHGYDTQVGErglkLSGGEKQRV 617
Cdd:COG1119 83 VSPA---LQLRFPRDEtvldvvlsgFFDSIglyrEPTDEQRERARELL----ELLGLAHLADRPFGT----LSQGEQRRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47058990 618 AIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKH--RTSIFIAHRLSTVVDA-DEIIVLSQGKVAERG 688
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAG 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
484-684 |
2.92e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 110.11 E-value: 2.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 484 GQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS-LESLRRAVGVVPQDAVLFHN-T 561
Cdd:COG1129 16 GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGIAIIHQELNLVPNlS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 562 IYYNLLYGNINASP-----EEVYAVAK--LAGLH---DAilrmphgyDTQVGErglkLSGGEKQRVAIARAILKDPPVIL 631
Cdd:COG1129 96 VAENIFLGREPRRGglidwRAMRRRARelLARLGldiDP--------DTPVGD----LSVAQQQLVEIARALSRDARVLI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 47058990 632 YDEATSSLDSiTE-ETILGAMRDVVKH-RTSIFIAHRLSTVVD-ADEIIVLSQGKV 684
Cdd:COG1129 164 LDEPTASLTE-REvERLFRIIRRLKAQgVAIIYISHRLDEVFEiADRVTVLRDGRL 218
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
377-687 |
3.25e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 110.67 E-value: 3.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 377 LNFGQSAIFSVGLTAIMVLASQGIVAGALTVGDLVMVNGLLFQLSLPLNFLGTVYRE--TRQALIDmnTLFTLLKVDTRI 454
Cdd:COG4178 268 LTFFTTGYGQLAVIFPILVAAPRYFAGEITLGGLMQAASAFGQVQGALSWFVDNYQSlaEWRATVD--RLAGFEEALEAA 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 455 KDKAMASPLQITPQTATVAFDNVHFEYIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYL-AG 533
Cdd:COG4178 346 DALPEAASRIETSEDGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAG 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 534 QNI----QD--VSLESLRRAvgvvpqdavlfhntiyynLLYGNI--NASPEEVYAVAKLAGLHDAILRMphgydTQVGER 605
Cdd:COG4178 426 ARVlflpQRpyLPLGTLREA------------------LLYPATaeAFSDAELREALEAVGLGHLAERL-----DEEADW 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 606 GLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIFIAHRLSTVVDADEIIVLSQGKVA 685
Cdd:COG4178 483 DQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGDGSW 562
|
..
gi 47058990 686 ER 687
Cdd:COG4178 563 QL 564
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
484-689 |
3.54e-25 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 104.83 E-value: 3.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 484 GQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSL-ESLRRAVGVVPQDAVLFHN-T 561
Cdd:cd03219 12 GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPhEIARLGIGRTFQIPRLFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 562 IYYNLLYGNINASPEEVYAVAKLAGLHDA---------ILRMPHGYDTQVGErglkLSGGEKQRVAIARAILKDPPVILY 632
Cdd:cd03219 92 VLENVMVAAQARTGSGLLLARARREEREAreraeelleRVGLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 633 DEATSSLdSITE-ETILGAMRDVVKHRTSI-FIAHRLSTVVD-ADEIIVLSQGKVAERGT 689
Cdd:cd03219 168 DEPAAGL-NPEEtEELAELIRELRERGITVlLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
476-684 |
3.63e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 105.97 E-value: 3.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 476 NVHFEYIEGQK--VLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQ 553
Cdd:PRK13650 9 NLTFKYKEDQEkyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 554 --DAVLFHNTIYYNLLYGNINAS------PEEVYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILK 625
Cdd:PRK13650 89 npDNQFVGATVEDDVAFGLENKGipheemKERVNEALELVGMQDFKEREPA-----------RLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47058990 626 DPPVILYDEATSSLDSITEETILGAMRDVVKHR--TSIFIAHRLSTVVDADEIIVLSQGKV 684
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
476-699 |
4.08e-25 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 105.05 E-value: 4.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 476 NVHFEYIEgQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDV-------------SLE 542
Cdd:PRK10619 10 DLHKRYGE-HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 543 SLRRAVGVVPQDAVLF-HNTIYYNLLygninASPEEVYAVAKLAGLHDAILRMPH-GYDTQV-GERGLKLSGGEKQRVAI 619
Cdd:PRK10619 89 LLRTRLTMVFQHFNLWsHMTVLENVM-----EAPIQVLGLSKQEARERAVKYLAKvGIDERAqGKYPVHLSGGQQQRVSI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 620 ARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKH-RTSIFIAHRLSTVVD-ADEIIVLSQGKVAERGTHYGLLANS 697
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGNP 243
|
..
gi 47058990 698 SS 699
Cdd:PRK10619 244 QS 245
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
482-689 |
4.35e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 105.24 E-value: 4.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 482 IEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVL-FHN 560
Cdd:PRK13548 12 LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 561 TIyynllygninaspEEVYAVAklaglhdailRMPHGYD------------TQVGERGLK------LSGGEKQRVAIARA 622
Cdd:PRK13548 92 TV-------------EEVVAMG----------RAPHGLSraeddalvaaalAQVDLAHLAgrdypqLSGGEQQRVQLARV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47058990 623 IL------KDPPVILYDEATSSLDSITEETILGAMRDVVKHR--TSIFIAHRLS-TVVDADEIIVLSQGKVAERGT 689
Cdd:PRK13548 149 LAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERglAVIVVLHDLNlAARYADRIVLLHQGRLVADGT 224
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
466-749 |
6.88e-25 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 111.41 E-value: 6.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 466 TPQTATVAFdnvhFEyIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAgqniqdvsleslr 545
Cdd:PTZ00243 659 TPKMKTDDF----FE-LEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE------------- 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 546 RAVGVVPQDAVLFHNTIYYNLLYGNinaspEEvyavaKLAGLHDAI---------LRMPHGYDTQVGERGLKLSGGEKQR 616
Cdd:PTZ00243 721 RSIAYVPQQAWIMNATVRGNILFFD-----EE-----DAARLADAVrvsqleadlAQLGGGLETEIGEKGVNLSGGQKAR 790
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 617 VAIARAILKDPPVILYDEATSSLDS-----ITEETILGAMRDvvkhRTSIFIAHRLSTVVDADEIIVLSQGKVAERGTHY 691
Cdd:PTZ00243 791 VSLARAVYANRDVYLLDDPLSALDAhvgerVVEECFLGALAG----KTRVLATHQVHVVPRADYVVALGDGRVEFSGSSA 866
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 47058990 692 GLLAnsSSIYSEMwhtQSTRIQNHDNLGWDAKKESLSKEEERKKLQEEIVNSVKGCGN 749
Cdd:PTZ00243 867 DFMR--TSLYATL---AAELKENKDSKEGDADAEVAEVDAAPGGAVDHEPPVAKQEGN 919
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
487-696 |
7.24e-25 |
|
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: 103.91 E-value: 7.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 487 VLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESL-RRAVGVVPQDAVLFHN-TIYY 564
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPSlTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 565 NLLYG--------NINASPEEVYAV--------AKLAGLhdailrmphgydtqvgerglkLSGGEKQRVAIARAILKDPP 628
Cdd:COG0410 98 NLLLGayarrdraEVRADLERVYELfprlkerrRQRAGT---------------------LSGGEQQMLAIGRALMSRPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47058990 629 VILYDEATSSLD-SITEEtILGAMRDVVKHRTSIFI----AHRLSTVvdADEIIVLSQGKVAERGTHYGLLAN 696
Cdd:COG0410 157 LLLLDEPSLGLApLIVEE-IFEIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAELLAD 226
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
475-689 |
8.00e-25 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 104.43 E-value: 8.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 475 DNVHFEYieGQK-VLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESL--RRAVgvV 551
Cdd:COG4559 5 ENLSVRL--GGRtLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELarRRAV--L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 552 PQDAVLfhntiyynllygninASPEEVYAVAKLAglhdailRMPHGYDT------------QVGERGLK------LSGGE 613
Cdd:COG4559 81 PQHSSL---------------AFPFTVEEVVALG-------RAPHGSSAaqdrqivrealaLVGLAHLAgrsyqtLSGGE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 614 KQRVAIARAIL-------KDPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIF-IAHRLS-TVVDADEIIVLSQGKV 684
Cdd:COG4559 139 QQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVaVLHDLNlAAQYADRILLLHQGRL 218
|
....*
gi 47058990 685 AERGT 689
Cdd:COG4559 219 VAQGT 223
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
472-682 |
9.99e-25 |
|
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: 102.79 E-value: 9.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESL----RRA 547
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 548 VGVVPQDAVLFHNTIYYNLLYGninaSP---EEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAIL 624
Cdd:cd03290 81 VAYAAQKPWLLNATVEENITFG----SPfnkQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47058990 625 KDPPVILYDEATSSL-----DSITEETILGAMRDvvKHRTSIFIAHRLSTVVDADEIIVLSQG 682
Cdd:cd03290 157 QNTNIVFLDDPFSALdihlsDHLMQEGILKFLQD--DKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
476-700 |
1.07e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 104.39 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 476 NVHFEYIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQ--DVSLESLRRAVGVVPQ 553
Cdd:PRK13639 6 DLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydKKSLLEVRKTVGIVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 554 --DAVLFHNTIYYNLLYG--NINASPEEVYAVAKLA----GLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILK 625
Cdd:PRK13639 86 npDDQLFAPTVEEDVAFGplNLGLSKEEVEKRVKEAlkavGMEGFENKPPH-----------HLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47058990 626 DPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIFIA-HRLSTV-VDADEIIVLSQGKVAERGTHYGLLANSSSI 700
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDIETI 231
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
475-689 |
2.11e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 103.63 E-value: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 475 DNVHFEYIEGQK-----VLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS-LESLRRAV 548
Cdd:PRK13633 8 KNVSYKYESNEEsteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 549 GVVPQ--DAVLFHNTIYYNLLYG--NINASPEEV-----YAVAKLaGLHDAILRMPHgydtqvgerglKLSGGEKQRVAI 619
Cdd:PRK13633 88 GMVFQnpDNQIVATIVEEDVAFGpeNLGIPPEEIrervdESLKKV-GMYEYRRHAPH-----------LLSGGQKQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47058990 620 ARAILKDPPVILYDEATSSLDSITEETILGAMRDVVK--HRTSIFIAHRLSTVVDADEIIVLSQGKVAERGT 689
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
471-690 |
2.40e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 102.40 E-value: 2.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 471 TVAFDNVHFEYIEGQkVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAG------QNIQDVSLESL 544
Cdd:PRK11124 2 SIQLNGINCFYGAHQ-ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 545 RRAVGVVPQDAVLF-HNTIYYNLlygnINAsPEEVYAVAKLAGLHDAI-----LRMphgydTQVGER-GLKLSGGEKQRV 617
Cdd:PRK11124 81 RRNVGMVFQQYNLWpHLTVQQNL----IEA-PCRVLGLSKDQALARAEkllerLRL-----KPYADRfPLHLSGGQQQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 618 AIARAILKDPPVILYDEATSSLD--------SITEE-TILGAMRDVVKHRTSifIAHRLSTVVdadeiIVLSQGKVAERG 688
Cdd:PRK11124 151 AIARALMMEPQVLLFDEPTAALDpeitaqivSIIRElAETGITQVIVTHEVE--VARKTASRV-----VYMENGHIVEQG 223
|
..
gi 47058990 689 TH 690
Cdd:PRK11124 224 DA 225
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
488-694 |
2.70e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 102.94 E-value: 2.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 488 LSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE-----PQKGSIYLAGQNI--QDVSLESLRRAVGVVPQDAVLFHN 560
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 561 TIYYNLLYG-NINASP----EEVYAVAKLAGLHDAIlrmphgyDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEA 635
Cdd:PRK14243 106 SIYDNIAYGaRINGYKgdmdELVERSLRQAALWDEV-------KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 47058990 636 TSSLDSITEETILGAMRDVVKHRTSIFIAHRLSTVVDADEIIVLSQGKVAERGTHYGLL 694
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGGRYGYL 237
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
472-698 |
3.59e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 102.76 E-value: 3.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS-LESLRRAVGV 550
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 551 VPQ--DAVLFHNTIYYNLLYG--NINASPEEVYAVAKLA----GLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARA 622
Cdd:PRK13644 82 VFQnpETQFVGRTVEEDLAFGpeNLCLPPIEIRKRVDRAlaeiGLEKYRHRSPK-----------TLSGGQGQCVALAGI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47058990 623 ILKDPPVILYDEATSSLDSITEETILGAMRDV-VKHRTSIFIAHRLSTVVDADEIIVLSQGKVAERGTHYGLLANSS 698
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
492-699 |
4.43e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 101.58 E-value: 4.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 492 SFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEslRRAVGVVPQDAVLF-HNTIYYNLLYG- 569
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFsHLTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 570 ----NINASP-EEVYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITE 644
Cdd:PRK10771 97 npglKLNAAQrEKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47058990 645 ETILGAMRDVVKHR--TSIFIAHRLStvvDADEI----IVLSQGKVAERGTHYGLLANSSS 699
Cdd:PRK10771 166 QEMLTLVSQVCQERqlTLLMVSHSLE---DAARIaprsLVVADGRIAWDGPTDELLSGKAS 223
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
472-689 |
4.81e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 102.57 E-value: 4.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYIEGQK-VLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ---KGSIYLAGQNIQDVSLESLRRA 547
Cdd:PRK13640 6 VEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 548 VGVVPQ--DAVLFHNTIYYNLLYGNINAS---PEEVYAVAKL---AGLHDAILRMPHgydtqvgerglKLSGGEKQRVAI 619
Cdd:PRK13640 86 VGIVFQnpDNQFVGATVGDDVAFGLENRAvprPEMIKIVRDVladVGMLDYIDSEPA-----------NLSGGQKQRVAI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47058990 620 ARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHR--TSIFIAHRLSTVVDADEIIVLSQGKVAERGT 689
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
471-684 |
6.11e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 102.60 E-value: 6.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 471 TVAFDNVHFEYIEG----QKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQ----DVSLE 542
Cdd:PRK13641 2 SIKFENVDYIYSPGtpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 543 SLRRAVGVVPQ--DAVLFHNTIYYNLLYG--NINASPEEvyavAKLAGLhDAILRMphGYDTQVGERG-LKLSGGEKQRV 617
Cdd:PRK13641 82 KLRKKVSLVFQfpEAQLFENTVLKDVEFGpkNFGFSEDE----AKEKAL-KWLKKV--GLSEDLISKSpFELSGGQMRRV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47058990 618 AIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKH-RTSIFIAHRLSTVVD-ADEIIVLSQGKV 684
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAgHTVILVTHNMDDVAEyADDVLVLEHGKL 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
471-689 |
6.69e-24 |
|
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: 106.31 E-value: 6.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 471 TVAFDNVHFEyiegQKVLSGVSFEVPAGKKVAIVGGSGSGKS----TIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRR 546
Cdd:COG4172 13 SVAFGQGGGT----VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 547 ----AVGVVPQDA----------------VLfhntiyynLLYGNINASPEEVYAVAKLA--GLHDAILRM---PHgydtq 601
Cdd:COG4172 89 irgnRIAMIFQEPmtslnplhtigkqiaeVL--------RLHRGLSGAAARARALELLErvGIPDPERRLdayPH----- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 602 vgerglKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVK-HRTSI-FIAHRLSTVVD-ADEIIV 678
Cdd:COG4172 156 ------QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQReLGMALlLITHDLGVVRRfADRVAV 229
|
250
....*....|.
gi 47058990 679 LSQGKVAERGT 689
Cdd:COG4172 230 MRQGEIVEQGP 240
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
471-690 |
7.47e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 101.24 E-value: 7.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 471 TVAFDNVHFEYiEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAG------QNIQDVSLESL 544
Cdd:COG4161 2 SIQLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 545 RRAVGVVPQDAVLF-HNTIYYNLLygninASPEEVYAVAKLAGLHDAI-----LRMphgydTQVGER-GLKLSGGEKQRV 617
Cdd:COG4161 81 RQKVGMVFQQYNLWpHLTVMENLI-----EAPCKVLGLSKEQAREKAMkllarLRL-----TDKADRfPLHLSGGQQQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 618 AIARAILKDPPVILYDEATSSLDS---------ITEETILGAMRDVVKHRTSifIAHRLSTVVdadeiIVLSQGKVAERG 688
Cdd:COG4161 151 AIARALMMEPQVLLFDEPTAALDPeitaqvveiIRELSQTGITQVIVTHEVE--FARKVASQV-----VYMEKGRIIEQG 223
|
..
gi 47058990 689 TH 690
Cdd:COG4161 224 DA 225
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
474-689 |
9.13e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 102.02 E-value: 9.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 474 FDNVHFEYIEG----QKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQ----DVSLESLR 545
Cdd:PRK13634 5 FQKVEHRYQYKtpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkkNKKLKPLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 546 RAVGVVPQ--DAVLFHNTIYYNLLYGNIN--ASPEEVYAVAK----LAGLHDAIL-RMPhgydtqvgergLKLSGGEKQR 616
Cdd:PRK13634 85 KKVGIVFQfpEHQLFEETVEKDICFGPMNfgVSEEDAKQKARemieLVGLPEELLaRSP-----------FELSGGQMRR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47058990 617 VAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHR--TSIFIAHRLSTVVD-ADEIIVLSQGKVAERGT 689
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEDAARyADQIVVMHKGTVFLQGT 229
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
486-748 |
2.39e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 101.47 E-value: 2.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 486 KVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYL----AGQNIQDVS------------LESLRRAVG 549
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHElitnpyskkiknFKELRRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 550 VVPQ--DAVLFHNTIYYNLLYGNINASPEEVYAvAKLAGLHdaILRMphGYDTQVGERG-LKLSGGEKQRVAIARAILKD 626
Cdd:PRK13631 120 MVFQfpEYQLFKDTIEKDIMFGPVALGVKKSEA-KKLAKFY--LNKM--GLDDSYLERSpFGLSGGQKRRVAIAGILAIQ 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 627 PPVILYDEATSSLDSITEETILGAMRDVVKH-RTSIFIAHRLSTVVD-ADEIIVLSQGKVAERGTHYGLLANSSSIysem 704
Cdd:PRK13631 195 PEILIFDEPTAGLDPKGEHEMMQLILDAKANnKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEIFTDQHII---- 270
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 47058990 705 whtQSTRIQN-------HDNLGWDAKKESLSKEEER--KKLQEEIVNSVKGCG 748
Cdd:PRK13631 271 ---NSTSIQVprviqviNDLIKKDPKYKKLYQKQPRtiEQLADAINEFIKGGK 320
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
491-684 |
2.86e-23 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 101.87 E-value: 2.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 491 VSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNI----QDVSLESLRRAVGVVPQDAVLF-HNTIYYN 565
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaeKGICLPPEKRRIGYVFQDARLFpHYKVRGN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 566 LLYGNINASPEEVYAVAKLAGLHDAILRMPHGydtqvgerglkLSGGEKQRVAIARAILKDPPVILYDEATSSLDsitee 645
Cdd:PRK11144 97 LRYGMAKSMVAQFDKIVALLGIEPLLDRYPGS-----------LSGGEKQRVAIGRALLTAPELLLMDEPLASLD----- 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 47058990 646 tiLGAMRDVVK--HRTS-------IFIAHRLSTVVD-ADEIIVLSQGKV 684
Cdd:PRK11144 161 --LPRKRELLPylERLAreinipiLYVSHSLDEILRlADRVVVLEQGKV 207
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
472-692 |
4.30e-23 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 98.41 E-value: 4.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNI---QDVSLESLRRAV 548
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 549 GVVPQDA-VLFHNTIYYNLLYGNI--NASPEE----VYAVAKLAGLHDAILRMPhgydtqvgergLKLSGGEKQRVAIAR 621
Cdd:PRK10908 82 GMIFQDHhLLMDRTVYDNVAIPLIiaGASGDDirrrVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47058990 622 AILKDPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIFIA-HRLSTVVDAD-EIIVLSQGKVAerGTHYG 692
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMAtHDIGLISRRSyRMLTLSDGHLH--GGVGG 221
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
486-711 |
7.19e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 100.93 E-value: 7.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 486 KVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQniqDVSLESLR-RAVGVVPQDAVLF-HNTIY 563
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT---DVSRLHARdRKVGFVFQHYALFrHMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 564 YNLLYGNI----NASPEEVYAVAKLAGLHDaILRMPH---GYDTQvgerglkLSGGEKQRVAIARAILKDPPVILYDEAT 636
Cdd:PRK10851 93 DNIAFGLTvlprRERPNAAAIKAKVTQLLE-MVQLAHladRYPAQ-------LSGGQKQRVALARALAVEPQILLLDEPF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 637 SSLDSITEETILGAMRDVvkHR----TSIFIAHRLSTVVD-ADEIIVLSQGKVAERGTHygllansssiySEMWHTQSTR 711
Cdd:PRK10851 165 GALDAQVRKELRRWLRQL--HEelkfTSVFVTHDQEEAMEvADRVVVMSQGNIEQAGTP-----------DQVWREPATR 231
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
471-706 |
2.01e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 97.93 E-value: 2.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 471 TVAFDNVHFEYIEG----QKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNI----QDVSLE 542
Cdd:PRK13646 2 TIRFDNVSYTYQKGtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 543 SLRRAVGVVPQ--DAVLFHNTIYYNLLYG--NINASPEEVYAVAklaglHDaiLRMPHGYDTQVGERG-LKLSGGEKQRV 617
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDTVEREIIFGpkNFKMNLDEVKNYA-----HR--LLMDLGFSRDVMSQSpFQMSGGQMRKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 618 AIARAILKDPPVILYDEATSSLDSITEETILGAMRD--VVKHRTSIFIAHRLSTVVD-ADEIIVLSQGKVAERGTHYGLL 694
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELF 234
|
250
....*....|..
gi 47058990 695 ANSSsiYSEMWH 706
Cdd:PRK13646 235 KDKK--KLADWH 244
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
487-688 |
2.62e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 101.32 E-value: 2.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 487 VLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQkGSIYLAGQNIQDVS---LESLRRAVGVVPQDAVLFHN--- 560
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDPNSSLNprl 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 561 ----------TIYYNLLygNINASPEEVYAVAKLAGLhDAILRmpHGYDTQvgerglkLSGGEKQRVAIARAILKDPPVI 630
Cdd:PRK15134 380 nvlqiieeglRVHQPTL--SAAQREQQVIAVMEEVGL-DPETR--HRYPAE-------FSGGQRQRIAIARALILKPSLI 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47058990 631 LYDEATSSLDSITEETILGAMRDV-VKHRTS-IFIAHRLStVVDA--DEIIVLSQGKVAERG 688
Cdd:PRK15134 448 ILDEPTSSLDKTVQAQILALLKSLqQKHQLAyLFISHDLH-VVRAlcHQVIVLRQGEVVEQG 508
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
482-640 |
2.68e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 95.63 E-value: 2.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 482 IEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ---KGSIYLAGQNIQDVSLEslRRAVGVVPQDAVLF 558
Cdd:COG4136 11 LGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAE--QRRIGILFQDDLLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 559 -HNTIYYNLLYG-----NINASPEEVYAVAKLAGLHDAILRMPhgyDTqvgerglkLSGGEKQRVAIARAILKDPPVILY 632
Cdd:COG4136 89 pHLSVGENLAFAlpptiGRAQRRARVEQALEEAGLAGFADRDP---AT--------LSGGQRARVALLRALLAEPRALLL 157
|
....*...
gi 47058990 633 DEATSSLD 640
Cdd:COG4136 158 DEPFSKLD 165
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
469-696 |
2.88e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 97.77 E-value: 2.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 469 TATVAFDNVHFEYIEGQ----KVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSI----YLAGQNIQDV- 539
Cdd:PRK13645 4 SKDIILDNVSYTYAKKTpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTivgdYAIPANLKKIk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 540 SLESLRRAVGVVPQ--DAVLFHNTIYYNLLYGNIN--ASPEEVYAvaKLAGLHDaILRMPHGYdtqVGERGLKLSGGEKQ 615
Cdd:PRK13645 84 EVKRLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNlgENKQEAYK--KVPELLK-LVQLPEDY---VKRSPFELSGGQKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 616 RVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKH--RTSIFIAHRLSTVVD-ADEIIVLSQGKVAERGTHYG 692
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFE 237
|
....
gi 47058990 693 LLAN 696
Cdd:PRK13645 238 IFSN 241
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
487-689 |
3.10e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 99.02 E-value: 3.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 487 VLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEslRRAVGVVPQDAVLF-HNTIYYN 565
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFpHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 566 LLYG---------NINASPEEVYAVAKLAGLHDAilrmphgYDTQVgerglklSGGEKQRVAIARAILKDPPVILYDEAT 636
Cdd:PRK11432 99 VGYGlkmlgvpkeERKQRVKEALELVDLAGFEDR-------YVDQI-------SGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 637 SSLDSiteeTILGAMRDVVKHR------TSIFIAHRLSTVVD-ADEIIVLSQGKVAERGT 689
Cdd:PRK11432 165 SNLDA----NLRRSMREKIRELqqqfniTSLYVTHDQSEAFAvSDTVIVMNKGKIMQIGS 220
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
475-731 |
3.25e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 97.47 E-value: 3.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 475 DNVHFEYIEGQKV--LSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVP 552
Cdd:PRK13642 8 ENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 553 Q--DAVLFHNTIYYNLLYGNINASPEEVYAVAKLaglhDAILRMPHGYDTQVGERGlKLSGGEKQRVAIARAILKDPPVI 630
Cdd:PRK13642 88 QnpDNQFVGATVEDDVAFGMENQGIPREEMIKRV----DEALLAVNMLDFKTREPA-RLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 631 LYDEATSSLDSITEETILGAMRDVVK--HRTSIFIAHRLSTVVDADEIIVLSQGKVAERGTHYGLLANSSSIYSEMWHT- 707
Cdd:PRK13642 163 ILDESTSMLDPTGRQEIMRVIHEIKEkyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDMVEIGLDVp 242
|
250 260
....*....|....*....|....*
gi 47058990 708 -QSTRIQNHDNLGWDAKKESLSKEE 731
Cdd:PRK13642 243 fSSNLMKDLRKNGFDLPEKYLSEDE 267
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
470-689 |
5.69e-22 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 98.38 E-value: 5.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 470 ATVAFDNVHFEYIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDvsLESLRRAVG 549
Cdd:PRK11650 2 AGLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNE--LEPADRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 550 VVPQDAVLF-HNTIYYNLLYG--NINASPEE----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARA 622
Cdd:PRK11650 80 MVFQNYALYpHMSVRENMAYGlkIRGMPKAEieerVAEAARILELEPLLDRKPR-----------ELSGGQRQRVAMGRA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47058990 623 ILKDPPVILYDEATSSLDSiteeTILGAMRDVVK--HR----TSIFIAH-RLSTVVDADEIIVLSQGKVAERGT 689
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLDA----KLRVQMRLEIQrlHRrlktTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGT 218
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
487-653 |
8.06e-22 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 94.81 E-value: 8.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 487 VLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYL--AGQNIqDVS-------LESLRRAVGVVPQ---- 553
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWV-DLAqaspreiLALRRRTIGYVSQflrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 554 -------DAV---LFHNtiyynllygniNASPEEVYAVAK--LAGLhdailrmphgydtQVGERGLKL-----SGGEKQR 616
Cdd:COG4778 105 iprvsalDVVaepLLER-----------GVDREEARARARelLARL-------------NLPERLWDLppatfSGGEQQR 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 47058990 617 VAIARAILKDPPVILYDEATSSLDSITEETILGAMRD 653
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEE 197
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
486-643 |
9.64e-22 |
|
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: 94.65 E-value: 9.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 486 KVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQK---GSIYLAGQniqDVSLESLRRAVGVVPQ-DAVLFHNT 561
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQ---PRKPDQFQKCVAYVRQdDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 562 IYYNLLYGNINASPEEVYAVAKLAglHDAILRMPHGYDTQVGERGLK-LSGGEKQRVAIARAILKDPPVILYDEATSSLD 640
Cdd:cd03234 98 VRETLTYTAILRLPRKSSDAIRKK--RVEDVLLRDLALTRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
...
gi 47058990 641 SIT 643
Cdd:cd03234 176 SFT 178
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
472-670 |
1.03e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 95.49 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYiEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ-----KGSIYLAGQNIQD--VSLESL 544
Cdd:PRK14258 8 IKVNNLSFYY-DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIYErrVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 545 RRAVGVVPQDAVLFHNTIYYNLLYGN--INASPEE-----VYAVAKLAGLHDAILRMPHgydtqvgERGLKLSGGEKQRV 617
Cdd:PRK14258 87 RRQVSMVHPKPNLFPMSVYDNVAYGVkiVGWRPKLeiddiVESALKDADLWDEIKHKIH-------KSALDLSGGQQQRL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 47058990 618 AIARAILKDPPVILYDEATSSLD---SITEETILGAMRdVVKHRTSIFIAHRLSTV 670
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDpiaSMKVESLIQSLR-LRSELTMVIVSHNLHQV 214
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
491-696 |
1.26e-21 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 95.29 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 491 VSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAG------------QNI----QDVSlESL--RRAVGvvp 552
Cdd:COG4167 32 VSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGhkleygdykyrcKHIrmifQDPN-TSLnpRLNIG--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 553 Q--DAVLFHNTiyyNLlygNINASPEEVYAVAKLAGLH-DAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPV 629
Cdd:COG4167 108 QilEEPLRLNT---DL---TAEEREERIFATLRLVGLLpEHANFYPH-----------MLSSGQKQRVALARALILQPKI 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 630 ILYDEATSSLDSITEETILGAMRDV-VKHRTS-IFIAHRLSTVVD-ADEIIVLSQGKVAERGTHYGLLAN 696
Cdd:COG4167 171 IIADEALAALDMSVRSQIINLMLELqEKLGISyIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVFAN 240
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
484-688 |
2.04e-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: 93.05 E-value: 2.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 484 GQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDvsLESLRRAVGVVpqdavlfhntIY 563
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK--NIEALRRIGAL----------IE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 564 YNLLYGNINASpEEVYAVAKLAGL----HDAILRMPhGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSL 639
Cdd:cd03268 80 APGFYPNLTAR-ENLRLLARLLGIrkkrIDEVLDVV-GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 47058990 640 DSITEETILGAMRDVVKHRTSIFIA-HRLSTVVD-ADEIIVLSQGKVAERG 688
Cdd:cd03268 158 DPDGIKELRELILSLRDQGITVLISsHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
475-668 |
3.06e-21 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 93.34 E-value: 3.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 475 DNVHFEYIEGQ---KVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLES---LR-RA 547
Cdd:PRK11629 9 DNLCKRYQEGSvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRnQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 548 VGVVPQdavlFHN---------TIYYNLLYGNINASPEEVYAVAKLAGLhdailrmphGYDTQVGERGLKLSGGEKQRVA 618
Cdd:PRK11629 89 LGFIYQ----FHHllpdftaleNVAMPLLIGKKKPAEINSRALEMLAAV---------GLEHRANHRPSELSGGERQRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 619 IARAILKDPPVILYDEATSSLDSITEETI---LGAMRD-------VVKHrtSIFIAHRLS 668
Cdd:PRK11629 156 IARALVNNPRLVLADEPTGNLDARNADSIfqlLGELNRlqgtaflVVTH--DLQLAKRMS 213
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
469-684 |
3.27e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 98.64 E-value: 3.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 469 TATVAFDNVHFEYIEGQ---KVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDV---SLE 542
Cdd:PRK10535 2 TALLELKDIRRSYPSGEeqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 543 SLRRA-VGVVPQDavlfhntiyYNLLYGNINASPEEVYAV-------AKLAGLHDAILRMphGYDTQVGERGLKLSGGEK 614
Cdd:PRK10535 82 QLRREhFGFIFQR---------YHLLSHLTAAQNVEVPAVyaglerkQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47058990 615 QRVAIARAILKDPPVILYDEATSSLDSITEE---TILGAMRDvvKHRTSIFIAHRLSTVVDADEIIVLSQGKV 684
Cdd:PRK10535 151 QRVSIARALMNGGQVILADEPTGALDSHSGEevmAILHQLRD--RGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
485-686 |
3.38e-21 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 93.98 E-value: 3.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 485 QKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLE---SLRRAVGVVPQD---AVLF 558
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAqrkAFRRDIQMVFQDsisAVNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 559 HNTIyynllyGNINASP-------------EEVYAVAKLAGLHDAIL-RMPHgydtqvgerglKLSGGEKQRVAIARAIL 624
Cdd:PRK10419 105 RKTV------REIIREPlrhllsldkaerlARASEMLRAVDLDDSVLdKRPP-----------QLSGGQLQRVCLARALA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47058990 625 KDPPVILYDEATSSLDSITEETILGAMRDvVKHRTSI---FIAHRLSTVVD-ADEIIVLSQGKVAE 686
Cdd:PRK10419 168 VEPKLLILDEAVSNLDLVLQAGVIRLLKK-LQQQFGTaclFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
464-688 |
4.78e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 93.05 E-value: 4.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 464 QITPQTATVAFDNVhfeyiegqKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE--PQ---KGSIYLAGQNIQD 538
Cdd:PRK14247 3 KIEIRDLKVSFGQV--------EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 539 VSLESLRRAVGVVPQDAVLFHN-TIYYNLLYG----NINASPEEVYAVAKLAgLHDAIL--RMPHGYDTQVGerglKLSG 611
Cdd:PRK14247 75 MDVIELRRRVQMVFQIPNPIPNlSIFENVALGlklnRLVKSKKELQERVRWA-LEKAQLwdEVKDRLDAPAG----KLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 612 GEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIFIAH------RLStvvdaDEIIVLSQGKVA 685
Cdd:PRK14247 150 GQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIV 224
|
...
gi 47058990 686 ERG 688
Cdd:PRK14247 225 EWG 227
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
485-689 |
9.32e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 92.38 E-value: 9.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 485 QKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQ-----DAVLFH 559
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQhhltpEGITVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 560 NTIYY-----NLLYGNINASPEEVYAVAklaglhdailrMPHGYDTQVGERGL-KLSGGEKQRVAIARAILKDPPVILYD 633
Cdd:PRK11231 95 ELVAYgrspwLSLWGRLSAEDNARVNQA-----------MEQTRINHLADRRLtDLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 47058990 634 EATSSLDSITEETILGAMRDV-VKHRTSIFIAHRLSTVVD-ADEIIVLSQGKVAERGT 689
Cdd:PRK11231 164 EPTTYLDINHQVELMRLMRELnTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGT 221
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
475-687 |
1.31e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 92.23 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 475 DNVHFEY---IEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEslrRAVgVV 551
Cdd:COG4525 7 RHVSVRYpggGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD---RGV-VF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 552 PQDAVLFHNTIYYNLLYG----NINASPEEVYAVAKLA--GLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILK 625
Cdd:COG4525 83 QKDALLPWLNVLDNVAFGlrlrGVPKAERRARAEELLAlvGLADFARRRIW-----------QLSGGMRQRVGIARALAA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47058990 626 DPPVILYDEATSSLDSITEETILGAMRDVVK--HRTSIFIAHRL-STVVDADEIIVLS--QGKVAER 687
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQMQELLLDVWQrtGKGVFLITHSVeEALFLATRLVVMSpgPGRIVER 218
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
476-689 |
1.39e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 92.60 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 476 NVHFEYIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIqDVS---LESLRRAVGVVP 552
Cdd:PRK13636 10 ELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSrkgLMKLRESVGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 553 Q--DAVLFHNTIYYNLLYGNINAS-PEevyavaklaglhDAILRMPHGYDTQVGERGLK------LSGGEKQRVAIARAI 623
Cdd:PRK13636 89 QdpDNQLFSASVYQDVSFGAVNLKlPE------------DEVRKRVDNALKRTGIEHLKdkpthcLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47058990 624 LKDPPVILYDEATSSLDSITEETILGAMRDVVKHR--TSIFIAHRLSTV-VDADEIIVLSQGKVAERGT 689
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELglTIIIATHDIDIVpLYCDNVFVMKEGRVILQGN 225
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
484-688 |
1.44e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 94.91 E-value: 1.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 484 GQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAvlfhnTIY 563
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDT-----SLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 564 YNLlygninaspeEVYAVAKLAglhdailRMPH--------GYDTQVGERGLK--------------LSGGEKQRVAIAR 621
Cdd:PRK09536 90 FEF----------DVRQVVEMG-------RTPHrsrfdtwtETDRAAVERAMErtgvaqfadrpvtsLSGGERQRVLLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47058990 622 AILKDPPVILYDEATSSLDSITEETILGAMRDVVKH-RTSIFIAHRLSTVVD-ADEIIVLSQGKVAERG 688
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDgKTAVAAIHDLDLAARyCDELVLLADGRVRAAG 221
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
492-701 |
3.15e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 93.56 E-value: 3.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 492 SFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESL----RRAVGVVPQD-AVLFHNTIYYNL 566
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSfALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 567 LYG-NINASPEEVYAVAKLAGLHDAILR-MPHGYDTQvgerglkLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITE 644
Cdd:PRK10070 128 AFGmELAGINAEERREKALDALRQVGLEnYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 645 ETILGAMRDV-VKH-RTSIFIAHRLSTVVD-ADEIIVLSQGKVAERGTHYGLLANSSSIY 701
Cdd:PRK10070 201 TEMQDELVKLqAKHqRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
469-690 |
7.96e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 91.02 E-value: 7.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 469 TATVAFDNVHFEYIEgQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESlRRAV 548
Cdd:PRK13537 5 VAPIDFRNVEKRYGD-KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 549 GVVPQdavlFHN-----TIYYNLL----YGNINASPeevyAVAKLAGLHDaILRMPHGYDTQVGErglkLSGGEKQRVAI 619
Cdd:PRK13537 83 GVVPQ----FDNldpdfTVRENLLvfgrYFGLSAAA----ARALVPPLLE-FAKLENKADAKVGE----LSGGMKRRLTL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47058990 620 ARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIFI-------AHRLstvvdADEIIVLSQG-KVAERGTH 690
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVIEEGrKIAEGAPH 223
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
484-689 |
1.01e-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: 89.92 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 484 GQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQniqdvsleslrraVGVVPQDAVLFHNTIY 563
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 564 YNLLYGnINASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSIT 643
Cdd:cd03291 116 ENIIFG-VSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 47058990 644 EETIL-GAMRDVVKHRTSIFIAHRLSTVVDADEIIVLSQGKVAERGT 689
Cdd:cd03291 195 EKEIFeSCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGT 241
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
472-689 |
1.05e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 89.80 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYIEGQ----KVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS----LES 543
Cdd:PRK13649 3 INLQNVSYTYQAGTpfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 544 LRRAVGVVPQ--DAVLFHNTIYYNLLYG--NINASPEEVYAVA--KLAGLhdailrmphGYDTQVGERG-LKLSGGEKQR 616
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGpqNFGVSQEEAEALAreKLALV---------GISESLFEKNpFELSGGQMRR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47058990 617 VAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVvkHR---TSIFIAHRLSTVVD-ADEIIVLSQGKVAERGT 689
Cdd:PRK13649 154 VAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKL--HQsgmTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
457-690 |
2.23e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 90.28 E-value: 2.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 457 KAMASPLQITPQTAtVAFDNVHFEYiEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNI 536
Cdd:PRK13536 28 EAKASIPGSMSTVA-IDLAGVSKSY-GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 537 QDVSlESLRRAVGVVPQ-DAVLFHNTIYYNLL-YGN-INASPEEVYAVakLAGLHDaILRMPHGYDTQVGErglkLSGGE 613
Cdd:PRK13536 106 PARA-RLARARIGVVPQfDNLDLEFTVRENLLvFGRyFGMSTREIEAV--IPSLLE-FARLESKADARVSD----LSGGM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 614 KQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIFI-------AHRLstvvdADEIIVLSQG-KVA 685
Cdd:PRK13536 178 KRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVLEAGrKIA 252
|
....*
gi 47058990 686 ERGTH 690
Cdd:PRK13536 253 EGRPH 257
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
486-684 |
2.26e-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: 87.34 E-value: 2.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 486 KVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDvsleSLRRAVGVVPQDAVLFHN-TIYY 564
Cdd:cd03269 14 TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI----AARNRIGYLPEERGLYPKmKVID 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 565 NLLYgninaspeevyaVAKLAGL-HDAILRMPHGYDTQVGERGLK------LSGGEKQRVAIARAILKDPPVILYDEATS 637
Cdd:cd03269 90 QLVY------------LAQLKGLkKEEARRRIDEWLERLELSEYAnkrveeLSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 47058990 638 SLDSITEETILGAMRDVV-KHRTSIFIAHRLSTVVD-ADEIIVLSQGKV 684
Cdd:cd03269 158 GLDPVNVELLKDVIRELArAGKTVILSTHQMELVEElCDRVLLLNKGRA 206
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
470-691 |
2.62e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 90.47 E-value: 2.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 470 ATVAFDNVHFEYieGQKVLS-GVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVslESLRRAV 548
Cdd:PRK11000 2 ASVTLRNVTKAY--GDVVISkDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDV--PPAERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 549 GVVPQDAVLF-HNTIYYNLLYG---------NINASPEEVYAVAKLAGLHDailRMPHGydtqvgerglkLSGGEKQRVA 618
Cdd:PRK11000 78 GMVFQSYALYpHLSVAENMSFGlklagakkeEINQRVNQVAEVLQLAHLLD---RKPKA-----------LSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 619 IARAILKDPPVILYDEATSSLDSiteetilgAMR-----DVVK-H----RTSIFIAH-RLSTVVDADEIIVLSQGKVAER 687
Cdd:PRK11000 144 IGRTLVAEPSVFLLDEPLSNLDA--------ALRvqmriEISRlHkrlgRTMIYVTHdQVEAMTLADKIVVLDAGRVAQV 215
|
....*....
gi 47058990 688 GT-----HY 691
Cdd:PRK11000 216 GKplelyHY 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
481-686 |
3.11e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 87.91 E-value: 3.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 481 YIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE--PQ---KGSIYLAGQNIQDVSLES--LRRAVGVVPQ 553
Cdd:PRK14239 14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIYSPRTDTvdLRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 554 DAVLFHNTIYYNLLYGninaspeevyavAKLAGLHD-AILrmphgyDTQVgERGLK------------------LSGGEK 614
Cdd:PRK14239 94 QPNPFPMSIYENVVYG------------LRLKGIKDkQVL------DEAV-EKSLKgasiwdevkdrlhdsalgLSGGQQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 615 QRVAIARAILKDPPVILYDEATSSLDSIT----EETILGAMRD----VVKH----------RTSIFIAHRLSTVVDADEI 676
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISagkiEETLLGLKDDytmlLVTRsmqqasrisdRTGFFLDGDLIEYNDTKQM 234
|
250
....*....|
gi 47058990 677 IVLSQGKVAE 686
Cdd:PRK14239 235 FMNPKHKETE 244
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
488-688 |
3.61e-19 |
|
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: 87.14 E-value: 3.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 488 LSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSleslrravgvvPQDAVLFHNtiyYNLL 567
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPG-----------PDRMVVFQN---YSLL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 568 -----YGNINASPEEVYAVA------KLAGLHDAILRMPHGYDTQVGErglkLSGGEKQRVAIARAILKDPPVILYDEAT 636
Cdd:TIGR01184 67 pwltvRENIALAVDRVLPDLskserrAIVEEHIALVGLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 47058990 637 SSLDSITEETILGAMRDVVK--HRTSIFIAHRL-STVVDADEIIVLSQGKVAERG 688
Cdd:TIGR01184 143 GALDALTRGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNGPAANIG 197
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
459-684 |
3.88e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 87.81 E-value: 3.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 459 MASPLQITPQTAtVAFDNVHFEYIEgQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIyLAGQniqd 538
Cdd:PRK11247 1 MMNTARLNQGTP-LLLNAVSKRYGE-RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGT---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 539 VSLESLRRAVGVVPQDAVLFH-NTIYYNL---LYGNINASPEEVYAVAKLAglhdailrmphgydTQVGERGLKLSGGEK 614
Cdd:PRK11247 74 APLAEAREDTRLMFQDARLLPwKKVIDNVglgLKGQWRDAALQALAAVGLA--------------DRANEWPAALSGGQK 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47058990 615 QRVAIARAILKDPPVILYDEATSSLDSITE-EtilgaMRDVVK------HRTSIFIAHRLSTVVD-ADEIIVLSQGKV 684
Cdd:PRK11247 140 QRVALARALIHRPGLLLLDEPLGALDALTRiE-----MQDLIEslwqqhGFTVLLVTHDVSEAVAmADRVLLIEEGKI 212
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
488-684 |
6.65e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 90.47 E-value: 6.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 488 LSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGqniQDVSLESLRRA----VGVVPQDAVLFHN-TI 562
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIRSPRDAialgIGMVHQHFMLVPNlTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 563 YYNLLYG---------NINASPEEVYAVAKLAGLH---DAIlrmphgydtqVGErglkLSGGEKQRVAIARAILKDPPVI 630
Cdd:COG3845 98 AENIVLGleptkggrlDRKAARARIRELSERYGLDvdpDAK----------VED----LSVGEQQRVEILKALYRGARIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47058990 631 LYDEATSSLdsiT-EET-----ILGAMRDvvKHRTSIFIAHRLSTVVD-ADEIIVLSQGKV 684
Cdd:COG3845 164 ILDEPTAVL---TpQEAdelfeILRRLAA--EGKSIIFITHKLREVMAiADRVTVLRRGKV 219
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
490-689 |
6.68e-19 |
|
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: 86.27 E-value: 6.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 490 GVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGqniQDVSLES--LRRAVGVVPQDAVL------FHNT 561
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG---HDVVREPreVRRRIGIVFQDLSVddeltgWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 562 IYYNLLYGNINAS-PEEVYAVAKLAGLHDAilrmphgYDTQVGerglKLSGGEKQRVAIARAILKDPPVILYDEATSSLD 640
Cdd:cd03265 95 YIHARLYGVPGAErRERIDELLDFVGLLEA-------ADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 47058990 641 SITEETILGAMRDVVK-HRTSIFI-------AHRLstvvdADEIIVLSQGKVAERGT 689
Cdd:cd03265 164 PQTRAHVWEYIEKLKEeFGMTILLtthymeeAEQL-----CDRVAIIDHGRIIAEGT 215
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
483-640 |
6.82e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 89.51 E-value: 6.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 483 EGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSleSLRRAVGVVPQDAVLF-HNT 561
Cdd:PRK11607 30 DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP--PYQRPINMMFQSYALFpHMT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 562 IYYNLLYG---------NINASPEEVYAvakLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILY 632
Cdd:PRK11607 108 VEQNIAFGlkqdklpkaEIASRVNEMLG---LVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLL 173
|
....*...
gi 47058990 633 DEATSSLD 640
Cdd:PRK11607 174 DEPMGALD 181
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
474-684 |
1.04e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.12 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 474 FDNVHFEYiEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQniqdvslesLRraVGVVPQ 553
Cdd:COG0488 1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG---------LR--IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 554 DAVLF-HNTIYYNLLYGN------------INASPEEVYAV-AKLAGLHDAILRMpHGY--------------------D 599
Cdd:COG0488 69 EPPLDdDLTVLDTVLDGDaelraleaeleeLEAKLAEPDEDlERLAELQEEFEAL-GGWeaearaeeilsglgfpeedlD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 600 TQVGErglkLSGGEKQRVAIARAILKDPPVILYDEATSSLD--SIT--EETIL---GAMrdvvkhrtsIFIAH-R--LST 669
Cdd:COG0488 148 RPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDleSIEwlEEFLKnypGTV---------LVVSHdRyfLDR 214
|
250
....*....|....*
gi 47058990 670 VVdaDEIIVLSQGKV 684
Cdd:COG0488 215 VA--TRILELDRGKL 227
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
488-689 |
1.17e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 90.49 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 488 LSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLfRFYEPQ----KGSIYLAGQNIQdvsLESLRRAVGVVPQDAVLF-HNTI 562
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNAL-AFRSPKgvkgSGSVLLNGMPID---AKEMRAISAYVQQDDLFIpTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 563 YYNLLYGNINASPEEVYAVAKLAGLHDAILRMPHG--YDTQVGERGLK--LSGGEKQRVAIARAILKDPPVILYDEATSS 638
Cdd:TIGR00955 117 REHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRkcANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 47058990 639 LDSITEETILGAMRDVV-KHRTSIFIAHRLSTVVDA--DEIIVLSQGKVAERGT 689
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGLAqKGKTIICTIHQPSSELFElfDKIILMAEGRVAYLGS 250
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
486-696 |
1.25e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 87.45 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 486 KVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSI------------------YLAGQNIQDV------SL 541
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekVLEKLVIQKTrfkkikKI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 542 ESLRRAVGVVPQDA--VLFHNTIYYNLLYGNIN--ASPEEVYAVAK----LAGLHDAIL-RMPHGydtqvgerglkLSGG 612
Cdd:PRK13651 101 KEIRRRVGVVFQFAeyQLFEQTIEKDIIFGPVSmgVSKEEAKKRAAkyieLVGLDESYLqRSPFE-----------LSGG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 613 EKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKH-RTSIFIAHRLSTVVD-ADEIIVLSQGKVAERGTH 690
Cdd:PRK13651 170 QKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVLEwTKRTIFFKDGKIIKDGDT 249
|
....*.
gi 47058990 691 YGLLAN 696
Cdd:PRK13651 250 YDILSD 255
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
487-652 |
1.35e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.93 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 487 VLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGvvPQDAVLFHNTIYYNL 566
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPALTVAENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 567 -----LYGNINASPEEVYAVAKLAGLHDailrMPHGYdtqvgerglkLSGGEKQRVAIARAILKDPPVILYDEATSSLDS 641
Cdd:PRK13539 95 efwaaFLGGEELDIAAALEAVGLAPLAH----LPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
170
....*....|.
gi 47058990 642 ITEETILGAMR 652
Cdd:PRK13539 161 AAVALFAELIR 171
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
491-702 |
1.43e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 90.30 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 491 VSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLRRAVGVVPQD--AVLF-HNTIYY 564
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDpyASLDpRQTVGD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 565 ---------NLLYGniNASPEEVYAVAKLAGLH-DAILRMPHGYdtqvgerglklSGGEKQRVAIARAILKDPPVILYDE 634
Cdd:PRK10261 423 simeplrvhGLLPG--KAAAARVAWLLERVGLLpEHAWRYPHEF-----------SGGQRQRICIARALALNPKVIIADE 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47058990 635 ATSSLDSITEETILGAMRDVVKHR--TSIFIAHRLSTVVD-ADEIIVLSQGKVAERGTHYGLLANSSSIYS 702
Cdd:PRK10261 490 AVSALDVSIRGQIINLLLDLQRDFgiAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFENPQHPYT 560
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
433-702 |
1.73e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 87.45 E-value: 1.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 433 ETRQALIDMNTLftllKVDTRIKDKAmASPLQiTPQTAtvafdnvhfeyiegqKVLSGVSFEVPAGKKVAIVGGSGSGKS 512
Cdd:PRK15079 3 EGKKVLLEVADL----KVHFDIKDGK-QWFWQ-PPKTL---------------KAVDGVTLRLYEGETLGVVGESGCGKS 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 513 TIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRA---VGVVPQDAVLFHN---TIyynllyGNINASPEEVY------- 579
Cdd:PRK15079 62 TFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdIQMIFQDPLASLNprmTI------GEIIAEPLRTYhpklsrq 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 580 --------AVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAM 651
Cdd:PRK15079 136 evkdrvkaMMLKVGLLPNLINRYPH-----------EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLL 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 47058990 652 RDVVKHR--TSIFIAHRLSTVVD-ADEIIVLSQGKVAERGTHYGLLANSSSIYS 702
Cdd:PRK15079 205 QQLQREMglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHNPLHPYT 258
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
141-436 |
1.75e-18 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 86.80 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 141 AISLGFLGGAKAMNIVVPFMFKYAVDS------LNQMSGNMLNLSDAPNTVATMATAVLIGYGVSRAGAAFFNEVrnaVF 214
Cdd:cd18564 2 ALALLALLLETALRLLEPWPLKVVIDDvlgdkpLPGLLGLAPLLGPDPLALLLLAAAALVGIALLRGLASYAGTY---LT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 215 GKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALskaIDRGTRGI----SFVLSA---LVFNLLPIVFeMTLVSSVLyy 287
Cdd:cd18564 79 ALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDL---LSRLTGDVgaiqDLLVSGvlpLLTNLLTLVG-MLGVMFWL-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 288 kcGAQFALVTLGTLgayTAFTVAVTRWRTRFRIEMNKADNDAGN-AAI--DSLLNYETVKYFNNEKYEAQRYDGFLKTYE 364
Cdd:cd18564 153 --DWQLALIALAVA---PLLLLAARRFSRRIKEASREQRRREGAlASVaqESLSAIRVVQAFGREEHEERRFARENRKSL 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47058990 365 TASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGALTVGDLvmvngLLFqlslpLNFLGTVYRETRQ 436
Cdd:cd18564 228 RAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDL-----LVF-----LAYLKNLYKPVRD 289
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
140-428 |
2.55e-18 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 85.95 E-value: 2.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 140 VAISLGFLGGAKAMNIVVPFMFKYAVDSLnQMSGNMLNLsdapntvaTMATAVLIGYGVSRAGAAFfneVRNAVFGKVAQ 219
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSV-IGGGLRELL--------WLLALLILGVALLRGVFRY---LQGYLAEKASQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 220 NSIRRIAKNVFLHLHNLDLGFHLSRQTGALskaIDRGT-------RGISFVLSALVFNLLPIVFEMTLVSSVlyykcGAQ 292
Cdd:cd18542 69 KVAYDLRNDLYDHLQRLSFSFHDKARTGDL---MSRCTsdvdtirRFLAFGLVELVRAVLLFIGALIIMFSI-----NWK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 293 FALVTLgtlgAYTAFTVAVTRW-----RTRFRI------EMNKA--DNDAGNaaidsllnyETVKYFNNEKYEAQRYDGF 359
Cdd:cd18542 141 LTLISL----AIIPFIALFSYVffkkvRPAFEEireqegELNTVlqENLTGV---------RVVKAFAREDYEIEKFDKE 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47058990 360 LKTYETASLKSTSTLA----MLNFgqsaIFSVGLTAIMVLASQGIVAGALTVGDLVMVNGLLFQLSLPLNFLG 428
Cdd:cd18542 208 NEEYRDLNIKLAKLLAkywpLMDF----LSGLQIVLVLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLG 276
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
475-687 |
3.12e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 85.14 E-value: 3.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 475 DNVHFEYiEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEslrRAVgVVPQD 554
Cdd:PRK11248 5 SHLYADY-GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE---RGV-VFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 555 AVLFHNTIYYNLLYGninaspEEVYAVAKLAGLHDAiLRMPhgydTQVGERGL------KLSGGEKQRVAIARAILKDPP 628
Cdd:PRK11248 80 GLLPWRNVQDNVAFG------LQLAGVEKMQRLEIA-HQML----KKVGLEGAekryiwQLSGGQRQRVGIARALAANPQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47058990 629 VILYDEATSSLDSITEETilgaMRDV---VKHRTS---IFIAHRL-STVVDADEIIVLS--QGKVAER 687
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQ----MQTLllkLWQETGkqvLLITHDIeEAVFMATELVLLSpgPGRVVER 212
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
487-689 |
3.38e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 84.75 E-value: 3.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 487 VLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQniqdVS--LEslrraVGVVpqdavlFH----- 559
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR----VSalLE-----LGAG------FHpeltg 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 560 --NtIYYN-LLYGNINASPEEVYA-VAKLAGLHDAIlrmphgyDTQVGerglKLSGGEKQRVAIARAILKDPPVILYDEA 635
Cdd:COG1134 106 reN-IYLNgRLLGLSRKEIDEKFDeIVEFAELGDFI-------DQPVK----TYSSGMRARLAFAVATAVDPDILLVDEV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 47058990 636 TSSLDSITEETILGAMRDVVKH-RTSIFIAHRLSTVVD-ADEIIVLSQGKVAERGT 689
Cdd:COG1134 174 LAVGDAAFQKKCLARIRELRESgRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
481-689 |
3.64e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 85.10 E-value: 3.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 481 YIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE------PQKGSIYLAGQNIQDVSLESLRRAVGVVPQD 554
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 555 AVLF-HNTIYYNLLYGNINASPEEVYAVAKLagLHDAILRMphGYDTQVGER----GLKLSGGEKQRVAIARAILKDPPV 629
Cdd:PRK14246 99 PNPFpHLSIYDNIAYPLKSHGIKEKREIKKI--VEECLRKV--GLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKV 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47058990 630 ILYDEATSSLDSITEETILGAMRDVVKHRTSIFIAHRLSTVVD-ADEIIVLSQGKVAERGT 689
Cdd:PRK14246 175 LLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGS 235
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
482-684 |
4.38e-18 |
|
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: 82.48 E-value: 4.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 482 IEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS-LESLRRAVGVVPQD---AVL 557
Cdd:cd03215 10 LSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAGIAYVPEDrkrEGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 558 FHN-TIYYNLLYGNInaspeevyavaklaglhdailrmphgydtqvgerglkLSGGEKQRVAIARAILKDPPVILYDEAT 636
Cdd:cd03215 90 VLDlSVAENIALSSL-------------------------------------LSGGNQQKVVLARWLARDPRVLILDEPT 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 47058990 637 SSLDSITEETILGAMRDVVKHRTSIFIahrLSTVVD-----ADEIIVLSQGKV 684
Cdd:cd03215 133 RGVDVGAKAEIYRLIRELADAGKAVLL---ISSELDellglCDRILVMYEGRI 182
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
468-688 |
6.31e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 84.55 E-value: 6.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 468 QTATVAFDNVHFEYIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLrra 547
Cdd:PRK15056 3 QQAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 548 VGVVPQD-------AVLFHNTIYYNLlYGninaspeevyavaklaglHDAILRMPHGYDTQVGERGL------------- 607
Cdd:PRK15056 80 VAYVPQSeevdwsfPVLVEDVVMMGR-YG------------------HMGWLRRAKKRDRQIVTAALarvdmvefrhrqi 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 608 -KLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKH-RTSIFIAHRLSTVVDADEIIVLSQGKVA 685
Cdd:PRK15056 141 gELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTVL 220
|
...
gi 47058990 686 ERG 688
Cdd:PRK15056 221 ASG 223
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
476-688 |
6.72e-18 |
|
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: 82.57 E-value: 6.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 476 NVHFEyIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRF--YEPQKGSIYLAGQNIQDVSL-ESLRRAVGVVP 552
Cdd:cd03217 5 DLHVS-VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPeERARLGIFLAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 553 QdavlfhntiyynllygninaSPEEVYAVaKLAGLhdaiLRmphgydtQVGErglKLSGGEKQRVAIARAILKDPPVILY 632
Cdd:cd03217 84 Q--------------------YPPEIPGV-KNADF----LR-------YVNE---GFSGGEKKRNEILQLLLLEPDLAIL 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47058990 633 DEATSSLD----SITEETIlGAMRDvvKHRTSIFIAH--RLSTVVDADEIIVLSQGKVAERG 688
Cdd:cd03217 129 DEPDSGLDidalRLVAEVI-NKLRE--EGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
484-682 |
1.03e-17 |
|
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: 88.43 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 484 GQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQniqdvsleslrraVGVVPQDAVLFHNTIY 563
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 564 YNLLYGnINASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSIT 643
Cdd:TIGR01271 505 DNIIFG-LSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 47058990 644 EETIL-GAMRDVVKHRTSIFIAHRLSTVVDADEIIVLSQG 682
Cdd:TIGR01271 584 EKEIFeSCLCKLMSNKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
468-680 |
1.09e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.89 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 468 QTATVAFDNVHFEYiEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSL-ESLRR 546
Cdd:PRK11288 1 SSPYLSFDGIGKTF-PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTtAALAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 547 AVGVVPQDAVLFHN-TIYYNLLYGN-------INASPEEVYAVAKLAGLHDAIlrMPhgyDTQVGErglkLSGGEKQRVA 618
Cdd:PRK11288 80 GVAIIYQELHLVPEmTVAENLYLGQlphkggiVNRRLLNYEAREQLEHLGVDI--DP---DTPLKY----LSIGQRQMVE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47058990 619 IARAILKDPPVILYDEATSSLdSITEETIL----GAMRDvvKHRTSIFIAHRLstvvdaDEIIVLS 680
Cdd:PRK11288 151 IAKALARNARVIAFDEPTSSL-SAREIEQLfrviRELRA--EGRVILYVSHRM------EEIFALC 207
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
470-696 |
1.63e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 82.63 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 470 ATVAFDNVHFEYiEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSL-ESLRRAV 548
Cdd:PRK10895 2 ATLTAKNLAKAY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 549 GVVPQDAVLFHN-TIYYNLL-----YGNINASPEEVYAVAKLAGLHDAILRmphgydtqvGERGLKLSGGEKQRVAIARA 622
Cdd:PRK10895 81 GYLPQEASIFRRlSVYDNLMavlqiRDDLSAEQREDRANELMEEFHIEHLR---------DSMGQSLSGGERRRVEIARA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 623 ILKDPPVILYDEATSSLDSITEETIlgamRDVVKH-RTS----IFIAHRLSTVVDADE-IIVLSQGKVAERGTHYGLLAN 696
Cdd:PRK10895 152 LAANPKFILLDEPFAGVDPISVIDI----KRIIEHlRDSglgvLITDHNVRETLAVCErAYIVSQGHLIAHGTPTEILQD 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
459-703 |
1.89e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 86.30 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 459 MASPLqITPQTATVAFDNVHfeyiEGQKVLSGVSFEVPAGKKVAIVGGSGSGKS----TIVRLLFR---FYePQkGSIYL 531
Cdd:PRK15134 1 MTQPL-LAIENLSVAFRQQQ----TVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSppvVY-PS-GDIRF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 532 AGQNIQDVSLESLRRAVGvvPQDAVLFHN-TIYYNLLYgNI----------------NASPEEVYAVAKLAGLHDAILRM 594
Cdd:PRK15134 74 HGESLLHASEQTLRGVRG--NKIAMIFQEpMVSLNPLH-TLekqlyevlslhrgmrrEAARGEILNCLDRVGIRQAAKRL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 595 ---PHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVK--HRTSIFIAHRLST 669
Cdd:PRK15134 151 tdyPH-----------QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSI 219
|
250 260 270
....*....|....*....|....*....|....*
gi 47058990 670 VVD-ADEIIVLSQGKVAERGTHYGLLANSSSIYSE 703
Cdd:PRK15134 220 VRKlADRVAVMQNGRCVEQNRAATLFSAPTHPYTQ 254
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
472-686 |
2.27e-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: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYiEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLaGQNIQdvsleslrraVGVV 551
Cdd:COG0488 316 LELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 552 PQDAVLFH--NTIYYNLLYGNINASPEEVYAVakLAGL----HDAilrmphgyDTQVGerglKLSGGEKQRVAIARAILK 625
Cdd:COG0488 384 DQHQEELDpdKTVLDELRDGAPGGTEQEVRGY--LGRFlfsgDDA--------FKPVG----VLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47058990 626 DPPVILYDEATSSLD--SIT--EETIL---GAMrdvvkhrtsIFIAH-R--LSTVvdADEIIVLSQGKVAE 686
Cdd:COG0488 450 PPNVLLLDEPTNHLDieTLEalEEALDdfpGTV---------LLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
487-688 |
2.82e-17 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 81.42 E-value: 2.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 487 VLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGqniQDVSLesLRRAVGVVPqDAVLFHNTIYYNL 566
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG---RVSSL--LGLGGGFNP-ELTGRENIYLNGR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 567 LYGNINASPEEVYA-VAKLAGLHDAIlrmphgyDTQVGErglkLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEE 645
Cdd:cd03220 111 LLGLSRKEIDEKIDeIIEFSELGDFI-------DLPVKT----YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 47058990 646 TILGAMRDVVKH-RTSIFIAHRLSTVVD-ADEIIVLSQGKVAERG 688
Cdd:cd03220 180 KCQRRLRELLKQgKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
481-688 |
3.36e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 81.81 E-value: 3.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 481 YIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ-----KGSIYLAGQNI--QDVSLESLRRAVGVVPQ 553
Cdd:PRK14267 13 YYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPIEVRREVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 554 DAVLF-HNTIY--------YNLLYGNINASPEEVYAVAKLAGLHDAILRMPHGYDTQvgerglkLSGGEKQRVAIARAIL 624
Cdd:PRK14267 93 YPNPFpHLTIYdnvaigvkLNGLVKSKKELDERVEWALKKAALWDEVKDRLNDYPSN-------LSGGQRQRLVIARALA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47058990 625 KDPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIFIAHRLSTVVD-ADEIIVLSQGKVAERG 688
Cdd:PRK14267 166 MKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVG 230
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
484-689 |
3.39e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 82.85 E-value: 3.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 484 GQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDvsleSLRRAVGvvpqdavlfhntiY 563
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP----EDRRRIG-------------Y 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 564 ynLlygninasPEE-------------VYaVAKLAGL--HDAILRMPHGYDT-QVGERGLK----LSGGEKQRVAIARAI 623
Cdd:COG4152 76 --L--------PEErglypkmkvgeqlVY-LARLKGLskAEAKRRADEWLERlGLGDRANKkveeLSKGNQQKVQLIAAL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47058990 624 LKDPPVILYDEATSSLDSITEETILGAMRDVV-KHRTSIFIAHRLSTVVD-ADEIIVLSQGKVAERGT 689
Cdd:COG4152 145 LHDPELLILDEPFSGLDPVNVELLKDVIRELAaKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGS 212
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
485-697 |
3.44e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 82.12 E-value: 3.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 485 QKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLRRAVGVVPQDAVLFHN- 560
Cdd:PRK11831 20 RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrLYTVRKRMSMLFQSGALFTDm 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 561 TIYYNLLYGNINAS--PEEVY---AVAKL--AGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYD 633
Cdd:PRK11831 100 NVFDNVAYPLREHTqlPAPLLhstVMMKLeaVGLRGAAKLMPS-----------ELSGGMARRAALARAIALEPDLIMFD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47058990 634 EATSSLDSITeETILGAMRDVVKHR---TSIFIAHRLSTVVD-ADEIIVLSQGKVAERGTHYGLLANS 697
Cdd:PRK11831 169 EPFVGQDPIT-MGVLVKLISELNSAlgvTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQALQANP 235
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
465-689 |
3.65e-17 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 85.24 E-value: 3.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 465 ITPQTATVAFDnvhfeyieGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLL--FRFYEPQKGSI-----------YL 531
Cdd:TIGR03269 1 IEVKNLTKKFD--------GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIiyhvalcekcgYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 532 -----AGQNI---------QDVSL----ESLRRAVgvVPQDAVLFHNTIyynLLYGN-------INASPEEVYAVAKLAG 586
Cdd:TIGR03269 73 erpskVGEPCpvcggtlepEEVDFwnlsDKLRRRI--RKRIAIMLQRTF---ALYGDdtvldnvLEALEEIGYEGKEAVG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 587 LHDAILRMphgydTQVGER----GLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHR--TS 660
Cdd:TIGR03269 148 RAVDLIEM-----VQLSHRithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSM 222
|
250 260 270
....*....|....*....|....*....|
gi 47058990 661 IFIAHRLSTVVD-ADEIIVLSQGKVAERGT 689
Cdd:TIGR03269 223 VLTSHWPEVIEDlSDKAIWLENGEIKEEGT 252
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
472-689 |
5.45e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 82.09 E-value: 5.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYIE----GQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS----LES 543
Cdd:PRK13643 2 IKFEKVNYTYQPnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 544 LRRAVGVVPQ--DAVLFHNTIYYNLLYG--NINASPEEVYAVAKlaglhdAILRMPhGYDTQVGERG-LKLSGGEKQRVA 618
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGpqNFGIPKEKAEKIAA------EKLEMV-GLADEFWEKSpFELSGGQMRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47058990 619 IARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKH-RTSIFIAHRLSTVVD-ADEIIVLSQGKVAERGT 689
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
143-438 |
9.87e-17 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 81.38 E-value: 9.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 143 SLGFLGGAKAMNIVVPFMFKYAVDSLNQmSGNMLNLsdapNTVATMATAVLigygVSRAGAAFFnevRNAVFGKVAQNSI 222
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAALG-GGDTASL----NQIALLLLGLF----LLQAVFSFF---RIYLFARVGERVV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 223 RRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIVFemTLV-SSVLYYKCGAQFALVTLGTL 301
Cdd:cd18576 69 ADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQIL--TLIgGVVLLFFISWKLTLLMLATV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 302 GAYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNEKYEAQRYDGFLKTYETASLKSTSTLAMLNFGQ 381
Cdd:cd18576 147 PVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFI 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 47058990 382 SAIFSVGLTAIMVLASQGIVAGALTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQAL 438
Cdd:cd18576 227 IFLLFGAIVAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKAL 283
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
488-689 |
1.17e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 80.27 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 488 LSGVSFEVPAGKKVAIVGGSGSGKSTivrLLFRF--YEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVL------FH 559
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKST---LLARMagLLPGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPpfampvFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 560 ntiyYNLLYGNINASPEEV-YAVAKLA---GLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVI----- 630
Cdd:COG4138 89 ----YLALHQPAGASSEAVeQLLAQLAealGLEDKLSRPLT-----------QLSGGEWQRVRLAAVLLQVWPTInpegq 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47058990 631 --LYDEATSSLDsITEETilgAMRDVVKH-----RTSIFIAHRLS-TVVDADEIIVLSQGKVAERGT 689
Cdd:COG4138 154 llLLDEPMNSLD-VAQQA---ALDRLLRElcqqgITVVMSSHDLNhTLRHADRVWLLKQGKLVASGE 216
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
484-711 |
1.31e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 80.91 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 484 GQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEP-----QKGSIYLAGQNI---QDVsLEsLRRAVGVVPQDA 555
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIfnyRDV-LE-FRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 556 VLFHNTIYYNLLYGnINAS---PEEVY---AVAKLA--GLHDAIlrmphgyDTQVGERGLKLSGGEKQRVAIARAILKDP 627
Cdd:PRK14271 111 NPFPMSIMDNVLAG-VRAHklvPRKEFrgvAQARLTevGLWDAV-------KDRLSDSPFRLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 628 PVILYDEATSSLDSITEETILGAMRDVVKHRTSIFIAHRLSTVVD-ADEIIVLSQGKVAERGThygllanSSSIYSEMWH 706
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGP-------TEQLFSSPKH 255
|
....*
gi 47058990 707 TQSTR 711
Cdd:PRK14271 256 AETAR 260
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
185-686 |
1.33e-16 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 83.69 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 185 VATMATAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSIRRIAKnvflhlhnldLGFHlsRQTGALSKAIDrgtrgisfVL 264
Cdd:COG4615 59 VLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLER----------IGAA--RLLAALTEDVR--------TI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 265 SALVFNLLPIVFEMTLVSSVLYYKC--GAQFALVTLGTLGaytaFTVAVTRWRT-RFRIEMNKA--DNDAGNAAIDSL-- 337
Cdd:COG4615 119 SQAFVRLPELLQSVALVLGCLAYLAwlSPPLFLLTLVLLG----LGVAGYRLLVrRARRHLRRAreAEDRLFKHFRALle 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 338 ------LNYETVKYFNNEKYEAQrydgfLKTYETASLKSTSTLAML-NFGQSAIFSV-GLTAIMVL----ASQGIVAGAL 405
Cdd:COG4615 195 gfkelkLNRRRRRAFFDEDLQPT-----AERYRDLRIRADTIFALAnNWGNLLFFALiGLILFLLPalgwADPAVLSGFV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 406 TVgdlvmvngLLFqLSLPL-NFLGTV--YRETRQALIDMNTLFtlLKVDTRIKDKAMASPLQITPQTATVAFDNVHFEYI 482
Cdd:COG4615 270 LV--------LLF-LRGPLsQLVGALptLSRANVALRKIEELE--LALAAAEPAAADAAAPPAPADFQTLELRGVTYRYP 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 483 EGQK----VLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLF 558
Cdd:COG4615 339 GEDGdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 559 HNtiyynlLYG-NINASPEEVYAVAKLaglhdaiLRMphgyDTQVGERG-----LKLSGGEKQRVAIARAILKDPPVILY 632
Cdd:COG4615 419 DR------LLGlDGEADPARARELLER-------LEL----DHKVSVEDgrfstTDLSQGQRKRLALLVALLEDRPILVF 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47058990 633 DEATSSLD----SITEETILGAMRDvvKHRTSIFIAHrlstvvD------ADEIIVLSQGKVAE 686
Cdd:COG4615 482 DEWAADQDpefrRVFYTELLPELKA--RGKTVIAISH------DdryfdlADRVLKMDYGKLVE 537
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
486-697 |
1.43e-16 |
|
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: 79.51 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 486 KVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSL-ESLRRAVGVVPQDAVLFHN-TIY 563
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYLPQEASIFRKlTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 564 YNLLygninaspeevyAVAKLAGLHDAILRmpHGYDTQVGE---------RGLKLSGGEKQRVAIARAILKDPPVILYDE 634
Cdd:cd03218 94 ENIL------------AVLEIRGLSKKERE--EKLEELLEEfhithlrksKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47058990 635 ATSSLDSITEETILGAMRDVVKHRTSIFIA-HRLSTVVD-ADEIIVLSQGKVAERGTHYGLLANS 697
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVRETLSiTDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
474-683 |
1.58e-16 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 77.10 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 474 FDNVHFEYiEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIyLAGQNIQdvsleslrraVGVVPQ 553
Cdd:cd03221 3 LENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV-TWGSTVK----------IGYFEQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 554 davlfhntiyynllygninaspeevyavaklaglhdailrmphgydtqvgerglkLSGGEKQRVAIARAILKDPPVILYD 633
Cdd:cd03221 71 -------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 47058990 634 EATSSLDSITEETILGAMRDvvKHRTSIFIAH-R--LSTVvdADEIIVLSQGK 683
Cdd:cd03221 96 EPTNHLDLESIEALEEALKE--YPGTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
140-438 |
1.59e-16 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 81.02 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 140 VAISLGFLGGAKAMNIVVPFMFKYAVDSLNQMSGNMLNLSDAPNTVATMAtavligygVSRAGAAFFNEVRNAVFGKVAQ 219
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDVLIQLGPGGNTSLLLLLVLGLA--------GAYVLSALLGILRGRLLARLGE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 220 NSIRRIAKNVFLHLHNLDLGFHLSRQTGALskaIDRGTRG-------ISFVLSALVFNLLPIVFemtlVSSVLYYkCGAQ 292
Cdd:cd18563 73 RITADLRRDLYEHLQRLSLSFFDKRQTGSL---MSRVTSDtdrlqdfLSDGLPDFLTNILMIIG----IGVVLFS-LNWK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 293 FALVTLGTLgaytAFTVAVTRW---RTRFRIEMNKADNDAGNAAI-DSLLNYETVKYFNNEKYEAQRYDGFLKTYETASL 368
Cdd:cd18563 145 LALLVLIPV----PLVVWGSYFfwkKIRRLFHRQWRRWSRLNSVLnDTLPGIRVVKAFGQEKREIKRFDEANQELLDANI 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 369 KSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGALTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQAL 438
Cdd:cd18563 221 RAEKLWATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRAL 290
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
491-695 |
3.05e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 79.45 E-value: 3.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 491 VSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQ--DVSLESLRraVGVVPQDAVLFHN------TI 562
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQR--IRMIFQDPSTSLNprqrisQI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 563 YYNLLYGNINASPEE----VYAVAKLAGL-HDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYDEATS 637
Cdd:PRK15112 110 LDFPLRLNTDLEPEQrekqIIETLRQVGLlPDHASYYPH-----------MLAPGQKQRLGLARALILRPKVIIADEALA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47058990 638 SLDSITEETILGAMRDVV-KHRTS-IFIAHRLSTVVD-ADEIIVLSQGKVAERGTHYGLLA 695
Cdd:PRK15112 179 SLDMSMRSQLINLMLELQeKQGISyIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLA 239
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
464-689 |
4.60e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.06 E-value: 4.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 464 QITPQTATVAFDNVHFEyIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLES 543
Cdd:PRK10575 4 YTNHSDTTFALRNVSFR-VPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 544 LRRAVGVVPQDavlfhntiyynlLYGNINASPEEVYAVAKLAgLHDAILRMPHGYDTQVGER----GLK---------LS 610
Cdd:PRK10575 83 FARKVAYLPQQ------------LPAAEGMTVRELVAIGRYP-WHGALGRFGAADREKVEEAislvGLKplahrlvdsLS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 611 GGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHR--TSIFIAHRLSTVVD-ADEIIVLSQGKVAER 687
Cdd:PRK10575 150 GGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINMAARyCDYLVALRGGEMIAQ 229
|
..
gi 47058990 688 GT 689
Cdd:PRK10575 230 GT 231
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
140-438 |
1.01e-15 |
|
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: 78.23 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 140 VAISLGFLGGAKAMNIVVPFMFKYAVDSLNQmsgnmlnlSDAPNTVATMATAVLIGYGVsRAGAAFFNEVrnaVFGKVAQ 219
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFV--------EKDLEALLLVPLAIIGLFLL-RGLASYLQTY---LMAYVGQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 220 NSIRRIAKNVFLHLHNLDLGFHLSRQTGAL-SKA---IDRGTRGISFVLSALVFNLLPIVFemtLVSSVLYYkcGAQFAL 295
Cdd:cd18552 69 RVVRDLRNDLFDKLLRLPLSFFDRNSSGDLiSRItndVNQVQNALTSALTVLVRDPLTVIG---LLGVLFYL--DWKLTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 296 VTLGTLGAYTAFTVAVTRwrtRFRIEMNKADNDAGN---AAIDSLLNYETVKYFNNEKYEAQRYDGFLKTYETASLKSTS 372
Cdd:cd18552 144 IALVVLPLAALPIRRIGK---RLRKISRRSQESMGDltsVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIAR 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47058990 373 TLAMLNFGQSAIFSVGLTAIMVLASQGIVAGALTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQAL 438
Cdd:cd18552 221 ARALSSPLMELLGAIAIALVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGL 286
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
487-684 |
1.01e-15 |
|
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: 77.37 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 487 VLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRaVGVV------------PQD 554
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRR-IGVVfgqktqlwwdlpVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 555 AVLFHNTIYynllygniNASPEEvyAVAKLAGLHDaILRMPHGYDTQVgeRglKLSGGEKQRVAIARAILKDPPVILYDE 634
Cdd:cd03267 115 SFYLLAAIY--------DLPPAR--FKKRLDELSE-LLDLEELLDTPV--R--QLSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 47058990 635 ATSSLDSITEETILGAMRDVVKHR--TSIFIAHRLSTVVD-ADEIIVLSQGKV 684
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRL 232
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
502-689 |
1.06e-15 |
|
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: 81.98 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 502 AIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQdVSLESLRRAVGVVPQDAVLFHNTIY--YNLLYGNINASPEEVY 579
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE-TNLDAVRQSLGMCPQHNILFHHLTVaeHILFYAQLKGRSWEEA 1038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 580 AVAKLAGLHDAilrmphGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHRT 659
Cdd:TIGR01257 1039 QLEMEAMLEDT------GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRT 1112
|
170 180 190
....*....|....*....|....*....|.
gi 47058990 660 SIFIAHRLSTV-VDADEIIVLSQGKVAERGT 689
Cdd:TIGR01257 1113 IIMSTHHMDEAdLLGDRIAIISQGRLYCSGT 1143
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
486-688 |
1.95e-15 |
|
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: 79.85 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 486 KVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIY-LAGQNIQDVS----LESLR--RAVGVVPQDAVLF 558
Cdd:TIGR03269 298 KAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvRVGDEWVDMTkpgpDGRGRakRYIGILHQEYDLY 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 559 -HNTIYYNLLYGNINASPEE------VYaVAKLAGLHD----AIL-RMPHgydtqvgerglKLSGGEKQRVAIARAILKD 626
Cdd:TIGR03269 378 pHRTVLDNLTEAIGLELPDElarmkaVI-TLKMVGFDEekaeEILdKYPD-----------ELSEGERHRVALAQVLIKE 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47058990 627 PPVILYDEATSSLDSITE----ETILGAMRDVvkHRTSIFIAHRLSTVVD-ADEIIVLSQGKVAERG 688
Cdd:TIGR03269 446 PRIVILDEPTGTMDPITKvdvtHSILKAREEM--EQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIG 510
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
468-698 |
3.74e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 75.69 E-value: 3.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 468 QTATVAFDNVHFEYIEGQkVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQD-VSLESLRR 546
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQ-ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKIMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 547 AVGVVPQDAVLFHN-TIYYNLLYGNINASPEEVYA-VAKLAGLhdailrMPHGYDTQVgERGLKLSGGEKQRVAIARAIL 624
Cdd:PRK11614 81 AVAIVPEGRRVFSRmTVEENLAMGGFFAERDQFQErIKWVYEL------FPRLHERRI-QRAGTMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47058990 625 KDPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIFIAHRLS--TVVDADEIIVLSQGKVAERGTHYGLLANSS 698
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNAnqALKLADRGYVLENGHVVLEDTGDALLANEA 229
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
487-647 |
4.18e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 75.20 E-value: 4.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 487 VLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLE---SLR-RAVGVVPQDAVL----- 557
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQSFMLiptln 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 558 -FHNTIYYNLLYG-NINASPEEVYAVAKLAGLHDAILRMPhgydtqvgergLKLSGGEKQRVAIARAILKDPPVILYDEA 635
Cdd:PRK10584 105 aLENVELPALLRGeSSRQSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170
....*....|..
gi 47058990 636 TSSLDSITEETI 647
Cdd:PRK10584 174 TGNLDRQTGDKI 185
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
471-686 |
4.25e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 78.86 E-value: 4.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 471 TVAFDNVHFEYIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGV 550
Cdd:PRK10522 322 TLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 551 VPQDAVLFHNTIyynllygninaSPEEVYAVAKLAGLHDAILRMPHGYDTQVGE-RGLKLSGGEKQRVAIARAILKDPPV 629
Cdd:PRK10522 402 VFTDFHLFDQLL-----------GPEGKPANPALVEKWLERLKMAHKLELEDGRiSNLKLSKGQKKRLALLLALAEERDI 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47058990 630 ILYDEATSSLD----SITEETILGAMRDVVKhrTSIFIAHRLSTVVDADEIIVLSQGKVAE 686
Cdd:PRK10522 471 LLLDEWAADQDphfrREFYQVLLPLLQEMGK--TIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
442-686 |
4.65e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 74.99 E-value: 4.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 442 NTLFTLLKVDtrikdKAMASPLQITPQTATV--AFdNVHFEYIEgQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLF 519
Cdd:COG2401 5 NPFFVLMRVT-----KVYSSVLDLSERVAIVleAF-GVELRVVE-RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 520 RFYE--PQKGSIYLAGQNI-QDVSLeslrravgvvpQDAVLfhntiyynllygnINASPEEVYAVAKLAGLHDAILrmph 596
Cdd:COG2401 78 GALKgtPVAGCVDVPDNQFgREASL-----------IDAIG-------------RKGDFKDAVELLNAVGLSDAVL---- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 597 gYDTQVGErglkLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHR--TSIFIAHRlSTVVDA- 673
Cdd:COG2401 130 -WLRRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAgiTLVVATHH-YDVIDDl 203
|
250
....*....|....*
gi 47058990 674 --DEIIVLSQGKVAE 686
Cdd:COG2401 204 qpDLLIFVGYGGVPE 218
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
484-652 |
1.08e-14 |
|
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: 73.30 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 484 GQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIY 563
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 564 YNL-LYGNINASP--EEVYAVAKLAGLHDAilrmPHGYdtqvgerglkLSGGEKQRVAIARAILKDPPVILYDEATSSLD 640
Cdd:cd03231 92 ENLrFWHADHSDEqvEEALARVGLNGFEDR----PVAQ----------LSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170
....*....|..
gi 47058990 641 SITEETILGAMR 652
Cdd:cd03231 158 KAGVARFAEAMA 169
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
472-666 |
1.57e-14 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 71.80 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGqniqdvsleslRRAVGVV 551
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 552 PQDAvlfhntiYYNLlyGNinaspeevyavaklagLHDAILRmPHGydtqvgergLKLSGGEKQRVAIARAILKDPPVIL 631
Cdd:cd03223 70 PQRP-------YLPL--GT----------------LREQLIY-PWD---------DVLSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190
....*....|....*....|....*....|....*
gi 47058990 632 YDEATSSLDSITEETILGAMRDvvKHRTSIFIAHR 666
Cdd:cd03223 115 LDEATSALDEESEDRLYQLLKE--LGITVISVGHR 147
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
484-683 |
1.84e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 76.51 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 484 GQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYePQ---KGSIYLAGQNIQDVSL-ESLRRAVGVVPQDAVLFH 559
Cdd:PRK13549 17 GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIrDTERAGIAIIHQELALVK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 560 N-TIYYNLLYGN-------INAspEEVYAVAK--LAGLHDAIlrmphGYDTQVGErglkLSGGEKQRVAIARAILKDPPV 629
Cdd:PRK13549 96 ElSVLENIFLGNeitpggiMDY--DAMYLRAQklLAQLKLDI-----NPATPVGN----LGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 47058990 630 ILYDEATSSLDSITEETILGAMRDVVKHR-TSIFIAHRLSTVVD-ADEIIVLSQGK 683
Cdd:PRK13549 165 LILDEPTASLTESETAVLLDIIRDLKAHGiACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
484-687 |
1.98e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.58 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 484 GQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQ-DVSLESLRRAVGVVPQDAVLFHN-T 561
Cdd:PRK10762 16 GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEAGIGIIHQELNLIPQlT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 562 IYYNLLYGNINASP------EEVYAVAklaglhDAILR---MPHGYDTQVGErglkLSGGEKQRVAIARAILKDPPVILY 632
Cdd:PRK10762 96 IAENIFLGREFVNRfgridwKKMYAEA------DKLLArlnLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIM 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 47058990 633 DEATSSLDSITEETILGAMRDVVKHRTSI-FIAHRLSTVVD-ADEIIVLSQGK-VAER 687
Cdd:PRK10762 166 DEPTDALTDTETESLFRVIRELKSQGRGIvYISHRLKEIFEiCDDVTVFRDGQfIAER 223
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
484-685 |
2.33e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 76.24 E-value: 2.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 484 GQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSlESLRRAVGV--VPQDAVLFHN- 560
Cdd:PRK15439 23 GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT-PAKAHQLGIylVPQEPLLFPNl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 561 TIYYNLLYGNINASPEEVYAVAKLAGLHDAI-LRMPHGydtqvgerglKLSGGEKQRVAIARAILKDPPVILYDEATSSL 639
Cdd:PRK15439 102 SVKENILFGLPKRQASMQKMKQLLAALGCQLdLDSSAG----------SLEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 47058990 640 DSITEETILGAMRDVVKHRTSI-FIAHRLSTVVD-ADEIIVLSQGKVA 685
Cdd:PRK15439 172 TPAETERLFSRIRELLAQGVGIvFISHKLPEIRQlADRISVMRDGTIA 219
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
484-683 |
3.80e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 75.63 E-value: 3.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 484 GQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYePQ---KGSIYLAGQNIQDVSL-ESLRRAVGVVPQDAVLFH 559
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIrDTERAGIVIIHQELTLVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 560 N-TIYYNLLYGNINASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSS 638
Cdd:TIGR02633 92 ElSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSS 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 47058990 639 LDSITEETILGAMRDVVKHRTS-IFIAHRLSTV-VDADEIIVLSQGK 683
Cdd:TIGR02633 172 LTEKETEILLDIIRDLKAHGVAcVYISHKLNEVkAVCDTICVIRDGQ 218
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
144-438 |
3.96e-14 |
|
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: 73.75 E-value: 3.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 144 LGFLGGAKAMNIVVPFMFKYAVDSLNQMSGnmlnlSDAPNTVATMATAVLIGYGVsragaafFNEVRNAVFGKVAQNSIR 223
Cdd:cd18557 2 LLFLLISSAAQLLLPYLIGRLIDTIIKGGD-----LDVLNELALILLAIYLLQSV-------FTFVRYYLFNIAGERIVA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 224 RIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGT----RGISFVLSALVFNLLpivfeMTLVSSVLYYKCGAQFALVTLG 299
Cdd:cd18557 70 RLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTsvlqSAVTDNLSQLLRNIL-----QVIGGLIILFILSWKLTLVLLL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 300 TLGAYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNEKYEAQRYDGFLKTYETASLKSTSTLAMLNF 379
Cdd:cd18557 145 VIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQG 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 47058990 380 GQSAIFSVGLTAIMVLASQGIVAGALTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQAL 438
Cdd:cd18557 225 ITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKAL 283
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
486-684 |
4.58e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 73.12 E-value: 4.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 486 KVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGS---IYLAGQNIQDV-----SLESLRRAVGVVPQDAVL 557
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshIELLGRTVQREgrlarDIRKSRANTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 558 FHN-TIYYNLLYGNINASP-----EEVYAVAKLAGLHDAILRMphGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVIL 631
Cdd:PRK09984 98 VNRlSVLENVLIGALGSTPfwrtcFSWFTREQKQRALQALTRV--GMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 47058990 632 YDEATSSLDSITEETILGAMRDVVKHR--TSIFIAHRLSTVVD-ADEIIVLSQGKV 684
Cdd:PRK09984 176 ADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDYALRyCERIVALRQGHV 231
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
472-719 |
6.50e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 72.73 E-value: 6.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYiEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQ--NIQDVSLESLRRAVG 549
Cdd:PRK13638 2 LATSDLWFRY-QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 550 VVPQDAvlfHNTIYYNLLYGNInaspeeVYAVAKLAGLHDAILRMPHGYDTQVGERGLK------LSGGEKQRVAIARAI 623
Cdd:PRK13638 81 TVFQDP---EQQIFYTDIDSDI------AFSLRNLGVPEAEITRRVDEALTLVDAQHFRhqpiqcLSHGQKKRVAIAGAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 624 LKDPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIFI-AHRLSTVVD-ADEIIVLSQGKVAERGTHYGLLANSSSIy 701
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIsSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFACTEAM- 230
|
250
....*....|....*...
gi 47058990 702 SEMWHTQSTRIQNHDNLG 719
Cdd:PRK13638 231 EQAGLTQPWLVKLHTQLG 248
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
488-684 |
7.41e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.89 E-value: 7.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 488 LSGVSFEVPAGKKVAIVGGSGSGKSTivrLLFRF--YEPQKGSIYLAGQNIQDVSLESL--RRAVgVVPQDAVLFHNTIY 563
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKST---LLARMagLLPGSGSIQFAGQPLEAWSAAELarHRAY-LSQQQTPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 564 YNL-LYG----NINASPEEVYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVI-------L 631
Cdd:PRK03695 88 QYLtLHQpdktRTEAVASALNEVAEALGLDDKLGRSVN-----------QLSGGEWQRVRLAAVVLQVWPDInpagqllL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 47058990 632 YDEATSSLDsITEEtilGAMRDVVKH-----RTSIFIAHRLS-TVVDADEIIVLSQGKV 684
Cdd:PRK03695 157 LDEPMNSLD-VAQQ---AALDRLLSElcqqgIAVVMSSHDLNhTLRHADRVWLLKQGKL 211
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
476-689 |
7.51e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 75.28 E-value: 7.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 476 NVHFEYiEGQKV--LSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEP-----QKGSIYLAGQNIQDVSLESLRRA- 547
Cdd:PRK10261 19 NIAFMQ-EQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQagglvQCDKMLLRRRSRQVIELSEQSAAq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 548 --------VGVVPQDAVLFHNTIY------YNLLYGNINASPEEVYAVAK-------LAGLHDAILRMPHgydtqvgerg 606
Cdd:PRK10261 98 mrhvrgadMAMIFQEPMTSLNPVFtvgeqiAESIRLHQGASREEAMVEAKrmldqvrIPEAQTILSRYPH---------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 607 lKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRdVVKHRTS---IFIAHRLSTVVD-ADEIIVLSQG 682
Cdd:PRK10261 168 -QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIK-VLQKEMSmgvIFITHDMGVVAEiADRVLVMYQG 245
|
....*..
gi 47058990 683 KVAERGT 689
Cdd:PRK10261 246 EAVETGS 252
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
482-688 |
8.36e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 72.04 E-value: 8.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 482 IEGQKVL-SGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPqkGSIYLAGQNIQD---VSLESLR-RAVGVVPQDAV 556
Cdd:PRK10418 12 LQAAQPLvHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA--GVRQTAGRVLLDgkpVAPCALRgRKIATIMQNPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 557 LFHNTIYynllygNINASPEEVYAVAklaGLHDAILRMPHGYDtQVG----ERGLKL-----SGGEKQRVAIARAILKDP 627
Cdd:PRK10418 90 SAFNPLH------TMHTHARETCLAL---GKPADDATLTAALE-AVGlenaARVLKLypfemSGGMLQRMMIALALLCEA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47058990 628 PVILYDEATSSLDSITEETILGAMRDVVKHRTS--IFIAHRLSTVVD-ADEIIVLSQGKVAERG 688
Cdd:PRK10418 160 PFIIADEPTTDLDVVAQARILDLLESIVQKRALgmLLVTHDMGVVARlADDVAVMSHGRIVEQG 223
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
484-634 |
9.76e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 71.60 E-value: 9.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 484 GQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIvrllfrFY------EPQKGSIYLAGQNIQDVSLEslRRA---VGVVPQD 554
Cdd:COG1137 15 KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPMH--KRArlgIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 555 AVLFHN-TIYYNLLygninaspeevyAVAKLAGLH--------DAIL---RMPHGYDTqvgeRGLKLSGGEKQRVAIARA 622
Cdd:COG1137 87 ASIFRKlTVEDNIL------------AVLELRKLSkkereerlEELLeefGITHLRKS----KAYSLSGGERRRVEIARA 150
|
170
....*....|..
gi 47058990 623 ILKDPPVILYDE 634
Cdd:COG1137 151 LATNPKFILLDE 162
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
487-688 |
9.83e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 71.94 E-value: 9.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 487 VLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNL 566
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 567 L-YGNINASP-------EEVYAVAK---LAGLHDAILRmphGYDTqvgerglkLSGGEKQRVAIARAILKDPPVILYDEA 635
Cdd:PRK10253 102 VaRGRYPHQPlftrwrkEDEEAVTKamqATGITHLADQ---SVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 47058990 636 TSSLDSITEETILGAMRDVVKHR--TSIFIAHRLSTVVD-ADEIIVLSQGKVAERG 688
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELNREKgyTLAAVLHDLNQACRyASHLIALREGKIVAQG 226
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
483-679 |
1.54e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 69.57 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 483 EGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGqniqdvsleslRRAVGVVPQDAVLfhnti 562
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEV----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 563 yynllygnINASPEEVYAVAKLaGL--HDAILRMPHGYDTQVGERGLK--------------LSGGEKQRVAIARAILKD 626
Cdd:NF040873 67 --------PDSLPLTVRDLVAM-GRwaRRGLWRRLTRDDRAAVDDALErvgladlagrqlgeLSGGQRQRALLAQGLAQE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 47058990 627 PPVILYDEATSSLDSITEETILGAMRDVV-KHRTSIFIAHRLSTVVDADEIIVL 679
Cdd:NF040873 138 ADLLLLDEPTTGLDAESRERIIALLAEEHaRGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
476-658 |
2.14e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 69.59 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 476 NVHFEYiEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIqDVSLESLRRAV------- 548
Cdd:PRK13540 6 ELDFDY-HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI-KKDLCTYQKQLcfvghrs 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 549 GVVPQdaVLFHNTIYYNLLYGNINASPEEVYAVAKLAGLHDailrMPHGYdtqvgerglkLSGGEKQRVAIARAILKDPP 628
Cdd:PRK13540 84 GINPY--LTLRENCLYDIHFSPGAVGITELCRLFSLEHLID----YPCGL----------LSSGQKRQVALLRLWMSKAK 147
|
170 180 190
....*....|....*....|....*....|
gi 47058990 629 VILYDEATSSLDSITEETIlgaMRDVVKHR 658
Cdd:PRK13540 148 LWLLDEPLVALDELSLLTI---ITKIQEHR 174
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
484-684 |
2.27e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 73.14 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 484 GQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRA-VGVVPQD-----AVL 557
Cdd:COG3845 270 GVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPEDrlgrgLVP 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 558 fHNTIYYNLLYGNINASP---------EEVYAVAKlaglhDAILRM---PHGYDTQVGerglKLSGGEKQRVAIARAILK 625
Cdd:COG3845 350 -DMSVAENLILGRYRRPPfsrggfldrKAIRAFAE-----ELIEEFdvrTPGPDTPAR----SLSGGNQQKVILARELSR 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47058990 626 DPPVILYDEATSSLD--SIteETILGAMRDVVKHRTSIFIahrLSTVVD-----ADEIIVLSQGKV 684
Cdd:COG3845 420 DPKLLIAAQPTRGLDvgAI--EFIHQRLLELRDAGAAVLL---ISEDLDeilalSDRIAVMYEGRI 480
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
154-475 |
7.10e-13 |
|
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: 69.78 E-value: 7.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 154 NIVVPFMFKYAVDS-LNQMSGNMLNLsdapntvatMATAVLIGYGVSragaAFFNEVRNAVFGKVAQNSIRRIAKNVFLH 232
Cdd:cd18570 18 GIAGSFFFQILIDDiIPSGDINLLNI---------ISIGLILLYLFQ----SLLSYIRSYLLLKLSQKLDIRLILGYFKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 233 LHNLDLGFHLSRQTGA-LSKAIDrgTRGISFVLSALVFNLlPIVFEMTLVSSVLYYKCGAQFALVTLGTLGAYTAFTVA- 310
Cdd:cd18570 85 LLKLPLSFFETRKTGEiISRFND--ANKIREAISSTTISL-FLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILLf 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 311 VTRWRTRFRIEMNK-ADNDAgnAAIDSLLNYETVKYFNNEKYEAQRYDGFLKTYetasLKSTSTLAMLNFGQSAIF---- 385
Cdd:cd18570 162 NKPFKKKNREVMESnAELNS--YLIESLKGIETIKSLNAEEQFLKKIEKKFSKL----LKKSFKLGKLSNLQSSIKglis 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 386 SVGLTAIMVLASQGIVAGALTVGDLVMVNGLLfqlslpLNFLGTVyretrQALIDmntlftllkvdtrikdkamaspLQI 465
Cdd:cd18570 236 LIGSLLILWIGSYLVIKGQLSLGQLIAFNALL------GYFLGPI-----ENLIN----------------------LQP 282
|
330
....*....|
gi 47058990 466 TPQTATVAFD 475
Cdd:cd18570 283 KIQEAKVAAD 292
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
140-437 |
2.08e-12 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 68.28 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 140 VAISLGFLGGAKAMNIVVPFMFKYAVDSLnqmsgnmlnLSDAPNTVATMATAVLIGYGVSRAGAAFfneVRNAVFGKVA- 218
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGP---------IAHGDRSALWPLVLLLLALGVAEAVLSF---LRRYLAGRLSl 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 219 --QNSIRRiakNVFLHLHNLDLGFHLSRQTGAL-SKAI-DRGT--RGISFVLSALVfNLLPIVFEMT--LVSSVLyykcg 290
Cdd:cd18543 69 gvEHDLRT---DLFAHLQRLDGAFHDRWQSGQLlSRATsDLSLvqRFLAFGPFLLG-NLLTLVVGLVvmLVLSPP----- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 291 aqFALVTLGTLGAytaFTVAVTRWRTRFRIEMNKADNDAGNAAI---DSLLNYETVKYFNNEKYEAQRYDGFLKTYETAS 367
Cdd:cd18543 140 --LALVALASLPP---LVLVARRFRRRYFPASRRAQDQAGDLATvveESVTGIRVVKAFGRERRELDRFEAAARRLRATR 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 368 LKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGALTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQA 437
Cdd:cd18543 215 LRAARLRARFWPLLEALPELGLAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRA 284
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
491-689 |
2.65e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 68.61 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 491 VSFEVPAGKKVAIVGGSGSGKS----TIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVG----VVPQDAVLFHN-- 560
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLVGaevaMIFQDPMTSLNpc 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 561 -TIYYNLLY-------GNINASPEEVYAVAKLAGLHDAILRM---PHgydtqvgerglKLSGGEKQRVAIARAILKDPPV 629
Cdd:PRK11022 106 yTVGFQIMEaikvhqgGNKKTRRQRAIDLLNQVGIPDPASRLdvyPH-----------QLSGGMSQRVMIAMAIACRPKL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47058990 630 ILYDEATSSLDSITEETILGAMRDVVKHRTS--IFIAHRLSTVVD-ADEIIVLSQGKVAERGT 689
Cdd:PRK11022 175 LIADEPTTALDVTIQAQIIELLLELQQKENMalVLITHDLALVAEaAHKIIVMYAGQVVETGK 237
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
140-430 |
3.17e-12 |
|
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: 68.36 E-value: 3.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 140 VAISLGFLGGAKAMNIVVPFMFKYAVDS-LNQMSGNMLNLSDAPNTVATMATAVLIGY--GVSRAGAAFFNEVRNAVFGK 216
Cdd:cd18565 1 LVLGLLASILNRLFDLAPPLLIGVAIDAvFNGEASFLPLVPASLGPADPRGQLWLLGGltVAAFLLESLFQYLSGVLWRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 217 VAQNSIRRIAKNVFLHLHNLDLGFHLSRQTG----ALSKAIDRGTRgisfVLSALVFNLLPIVFEMTLVSSVLYYkCGAQ 292
Cdd:cd18565 81 FAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGdlmsVLNNDVNQLER----FLDDGANSIIRVVVTVLGIGAILFY-LNWQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 293 FALVTLGTLgaytAFTVAVTRWRTRfRIEMNKAD--NDAG--NAAI-DSLLNYETVKYFNNEKYEAQRYDGFLKTYETAS 367
Cdd:cd18565 156 LALVALLPV----PLIIAGTYWFQR-RIEPRYRAvrEAVGdlNARLeNNLSGIAVIKAFTAEDFERERVADASEEYRDAN 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47058990 368 LKSTSTLAMLNFGQSAIFSVGLTAI------MVLASQGIVAGALTVGDLVMVNGLLFQLSLPLNFLGTV 430
Cdd:cd18565 231 WRAIRLRAAFFPVIRLVAGAGFVATfvvggyWVLDGPPLFTGTLTVGTLVTFLFYTQRLLWPLTRLGDL 299
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
484-688 |
3.35e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 67.26 E-value: 3.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 484 GQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSL----ESLRRAV-----GVVPQD 554
Cdd:PRK11701 18 PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLyalsEAERRRLlrtewGFVHQH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 555 A-------VLFHNTIYYNLL------YGNINASpeevyAVAKLAGLHDAILRM---PHGYdtqvgerglklSGGEKQRVA 618
Cdd:PRK11701 98 PrdglrmqVSAGGNIGERLMavgarhYGDIRAT-----AGDWLERVEIDAARIddlPTTF-----------SGGMQQRLQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47058990 619 IARAILKDPPVILYDEATSSLDSITEETILGAMRDVVK--HRTSIFIAHRLSTV-VDADEIIVLSQGKVAERG 688
Cdd:PRK11701 162 IARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRelGLAVVIVTHDLAVArLLAHRLLVMKQGRVVESG 234
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
490-689 |
3.73e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 66.94 E-value: 3.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 490 GVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRaVGVVP--QDAVLFHN-TIYYNL 566
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIAR-MGVVRtfQHVRLFREmTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 567 LygninaspeevyaVAK--------LAGL----------HDAILRMPHGYDtQVGERGL------KLSGGEKQRVAIARA 622
Cdd:PRK11300 102 L-------------VAQhqqlktglFSGLlktpafrraeSEALDRAATWLE-RVGLLEHanrqagNLAYGQQRRLEIARC 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47058990 623 ILKDPPVILYDEATSSLDSitEETI-LGAMRDVVK--HRTSI-FIAHRLSTVVD-ADEIIVLSQGKVAERGT 689
Cdd:PRK11300 168 MVTQPEILMLDEPAAGLNP--KETKeLDELIAELRneHNVTVlLIEHDMKLVMGiSDRIYVVNQGTPLANGT 237
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
474-674 |
3.76e-12 |
|
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: 69.78 E-value: 3.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 474 FDNVHFEYIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLF--------RFYEPQKGSIYLAGQNIQdVSLESLR 545
Cdd:TIGR00954 454 FENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKLFYVPQRPY-MTLGTLR 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 546 ravgvvpqDAVLFHNTIYYNLLYGNINASPEEVYAVAKLaglhDAILRMPHGYDTqVGERGLKLSGGEKQRVAIARAILK 625
Cdd:TIGR00954 533 --------DQIIYPDSSEDMKRRGLSDKDLEQILDNVQL----THILEREGGWSA-VQDWMDVLSGGEKQRIAMARLFYH 599
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 47058990 626 DPPVILYDEATSSLDSITEETILGAMRDV------VKHRTSIFIAHRLSTVVDAD 674
Cdd:TIGR00954 600 KPQFAILDECTSAVSVDVEGYMYRLCREFgitlfsVSHRKSLWKYHEYLLYMDGR 654
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
140-412 |
3.91e-12 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 67.80 E-value: 3.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 140 VAISLGFLGGAKAMNIVVPFMFKYAVDS-LNQMSGNMLNLsdapntvatmaTAVLIGYGVSRAGAAFFNEVRNAVFGKVA 218
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDyIVPGQGDLQGL-----------LLLALLYLGLLLLSFLLQYLQTYLLQKLG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 219 QNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSkaidrgTR--------------GISFVLSALVFnLLPIVFEMTLVSsv 284
Cdd:cd18544 70 QRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLV------TRvtndtealnelftsGLVTLIGDLLL-LIGILIAMFLLN-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 285 lyykcgAQFALVTLGTLgaytAFTVAVTRWrtrFRIEMNKADND--AGNAAIDSLLNyE------TVKYFNNEKYEAQRY 356
Cdd:cd18544 141 ------WRLALISLLVL----PLLLLATYL---FRKKSRKAYREvrEKLSRLNAFLQ-EsisgmsVIQLFNREKREFEEF 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 47058990 357 DGFLKTYETASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGALTVGDLVM 412
Cdd:cd18544 207 DEINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSGAVTLGVLYA 262
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
469-640 |
9.38e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 65.91 E-value: 9.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 469 TATVAFDNVHFEYieGQ-KVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQniqdvslesLRra 547
Cdd:PRK09544 2 TSLVSLENVSVSF--GQrRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 548 VGVVPQ----DAVLFHNTIYYNLLY-----GNINASPEEVYAvaklAGLHDAILRmphgydtqvgerglKLSGGEKQRVA 618
Cdd:PRK09544 69 IGYVPQklylDTTLPLTVNRFLRLRpgtkkEDILPALKRVQA----GHLIDAPMQ--------------KLSGGETQRVL 130
|
170 180
....*....|....*....|..
gi 47058990 619 IARAILKDPPVILYDEATSSLD 640
Cdd:PRK09544 131 LARALLNRPQLLVLDEPTQGVD 152
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
142-413 |
9.92e-12 |
|
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: 66.34 E-value: 9.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 142 ISLGFLG--GAKAMNIVVPFMFKYAVDSLNQMSGNMLNLSDAPNTVATMATA-VLIGygvsrAGAAFFNEVRNAVFGKVA 218
Cdd:cd18577 1 LIIGLLAaiAAGAALPLMTIVFGDLFDAFTDFGSGESSPDEFLDDVNKYALYfVYLG-----IGSFVLSYIQTACWTITG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 219 QNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTR----GISFVLSALVFNLlpivfeMTLVSSV---LYYkcGA 291
Cdd:cd18577 76 ERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNliqdGIGEKLGLLIQSL------STFIAGFiiaFIY--SW 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 292 QFALVTLGTLGAYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNEKYEAQRYDGFLKTYETASLKST 371
Cdd:cd18577 148 KLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKG 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 47058990 372 STLAMlnfgQSAIFSVGLTAIMVLA----SQGIVAGALTVGDLVMV 413
Cdd:cd18577 228 LVSGL----GLGLLFFIIFAMYALAfwygSRLVRDGEISPGDVLTV 269
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
484-685 |
1.54e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 67.35 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 484 GQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQ--NIQDVSlESLRRAVGVVPQD----AVL 557
Cdd:COG1129 264 VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvRIRSPR-DAIRAGIAYVPEDrkgeGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 558 FHNTIYYNLLYGNINA-------SPEEVYAVAKlaglhDAILRM---PHGYDTQVGErglkLSGGEKQRVAIARAILKDP 627
Cdd:COG1129 343 LDLSIRENITLASLDRlsrggllDRRRERALAE-----EYIKRLrikTPSPEQPVGN----LSGGNQQKVVLAKWLATDP 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47058990 628 PVILYDEATSSLD--SITEetILGAMRDVVKHRTSI-FIAHRLSTVVD-ADEIIVLSQGKVA 685
Cdd:COG1129 414 KVLILDEPTRGIDvgAKAE--IYRLIRELAAEGKAViVISSELPELLGlSDRILVMREGRIV 473
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
481-689 |
1.89e-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: 64.74 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 481 YIEGQKVLSGVSFEVPAG-----KKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIylagqniqdvslESLRRAVGVVPQDA 555
Cdd:cd03237 3 YPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI------------EIELDTVSYKPQYI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 556 VLFHNTIYYNLLYGNINASPEEVYAVAKLAGlhdaILRMPHGYDTQVGErglkLSGGEKQRVAIARAILKDPPVILYDEA 635
Cdd:cd03237 71 KADYEGTVRDLLSSITKDFYTHPYFKTEIAK----PLQIEQILDREVPE----LSGGELQRVAIAACLSKDADIYLLDEP 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47058990 636 TSSLDSitEETILGAmrDVVKHrtsiFIAHRLST--VVD---------ADEIIVLSqGKVAERGT 689
Cdd:cd03237 143 SAYLDV--EQRLMAS--KVIRR----FAENNEKTafVVEhdiimidylADRLIVFE-GEPSVNGV 198
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
477-689 |
1.95e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 65.88 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 477 VHFEYIEgQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRaVGVV----- 551
Cdd:COG4586 28 FRREYRE-VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARR-IGVVfgqrs 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 552 -------PQDAVLFHNTIYynllygNInasPEEVYA--VAKLAGLhdaiLRMPHGYDTQVgeRglKLSGGEKQRVAIARA 622
Cdd:COG4586 106 qlwwdlpAIDSFRLLKAIY------RI---PDAEYKkrLDELVEL----LDLGELLDTPV--R--QLSLGQRMRCELAAA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 623 ILKDPPVILYDEATSSLDSITEETILGAMRDVVK-HRTSIFIA-HRLSTVVD-ADEIIVLSQGKVAERGT 689
Cdd:COG4586 169 LLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNReRGTTILLTsHDMDDIEAlCDRVIVIDHGRIIYDGS 238
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
143-438 |
4.99e-11 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 64.10 E-value: 4.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 143 SLGFLGGAKAMNIVVPFMFKYAVDSLNQMSGnmlnlsdapntVATMATAVLIgYGVSRAGAAFFNEVRNAVFGKVAQNSI 222
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADGS-----------REAFYRAVLL-LLLLSVLSGLFSGLRGGCFSYAGTRLV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 223 RRIAKNVFLHLHNLDLGFHLSRQTGAL--------SKAIDRGTRGISFVLSALVfNLLPIVFEMTLVSsvlyykcgAQFA 294
Cdd:cd18572 69 RRLRRDLFRSLLRQDIAFFDATKTGELtsrltsdcQKVSDPLSTNLNVFLRNLV-QLVGGLAFMFSLS--------WRLT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 295 LVTLGTLGAytafTVAVTRWRTRFRIEMNKADND----AGNAAIDSLLNYETVKYFNNEKYEAQRYDGFLKTYETASLKS 370
Cdd:cd18572 140 LLAFITVPV----IALITKVYGRYYRKLSKEIQDalaeANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQ 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47058990 371 tstlAMLNFGQSAIFSVGLTAIMVLA----SQGIVAGALTVGDLVMVngLLFQLSL--PLNFLGTVYRETRQAL 438
Cdd:cd18572 216 ----ALAYAGYVAVNTLLQNGTQVLVlfygGHLVLSGRMSAGQLVTF--MLYQQQLgeAFQSLGDVFSSLMQAV 283
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
480-683 |
5.27e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.06 E-value: 5.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 480 EYIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLF-RFYEPQKGSIYLAgqNIQDVSLESLRRaVGVVPQDAVLF 558
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNFTGTILA--NNRKPTKQILKR-TGFVTQDDILY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 559 -HNTIYYNLLYGNINASPEEVYAVAKLAGLHDAI--LRMPHGYDTQVGERGLK-LSGGEKQRVAIARAILKDPPVILYDE 634
Cdd:PLN03211 153 pHLTVRETLVFCSLLRLPKSLTKQEKILVAESVIseLGLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 47058990 635 ATSSLDSITEETILGAMRDVV-KHRTSIFIAHRLSTVVDA--DEIIVLSQGK 683
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSLAqKGKTIVTSMHQPSSRVYQmfDSVLVLSEGR 284
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
459-682 |
7.66e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.19 E-value: 7.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 459 MASPLqITPQTATVAFDNVHfeyiegqkVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQD 538
Cdd:PRK09700 1 MATPY-ISMAGIGKSFGPVH--------ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 539 VSLE-SLRRAVGVVPQD-AVLFHNTIYYNLLYGNINASP---------EEVYAVAKLAGLHDAILRMPhgyDTQVGErgl 607
Cdd:PRK09700 72 LDHKlAAQLGIGIIYQElSVIDELTVLENLYIGRHLTKKvcgvniidwREMRVRAAMMLLRVGLKVDL---DEKVAN--- 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47058990 608 kLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHRTSI-FIAHRLSTVVD-ADEIIVLSQG 682
Cdd:PRK09700 146 -LSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIvYISHKLAEIRRiCDRYTVMKDG 221
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
498-680 |
1.03e-10 |
|
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: 60.46 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 498 GKKVAIVGGSGSGKSTIVRLLFRFYEPQKGS-IYLAGQNIQDVSLESLRravgvvpqdavlfhntiyynllygninaspe 576
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLL------------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 577 evyavaklaglhdailrmphgyDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVK 656
Cdd:smart00382 51 ----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLL 108
|
170 180 190
....*....|....*....|....*....|.
gi 47058990 657 HRTS-------IFIAHRLSTVVDADEIIVLS 680
Cdd:smart00382 109 LLLKseknltvILTTNDEKDLGPALLRRRFD 139
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
484-686 |
3.24e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 63.27 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 484 GQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLL-----FRFYEpqkGSIYLAGQ-----NIQDvsleSLRRAVGVVPQ 553
Cdd:NF040905 13 GVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLsgvypHGSYE---GEILFDGEvcrfkDIRD----SEALGIVIIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 554 D-AVLFHNTIYYNLLYGNINASP-----EEVYAVAK--LA--GLHDAilrmPhgyDTQVGERGLklsgGEKQRVAIARAI 623
Cdd:NF040905 86 ElALIPYLSIAENIFLGNERAKRgvidwNETNRRARelLAkvGLDES----P---DTLVTDIGV----GKQQLVEIAKAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47058990 624 LKDPPVILYDEATSSL---DSiteETILGAMRDVVKHR-TSIFIAHRLSTVVD-ADEIIVLSQGKVAE 686
Cdd:NF040905 155 SKDVKLLILDEPTAALneeDS---AALLDLLLELKAQGiTSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
488-677 |
4.13e-10 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 59.26 E-value: 4.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 488 LSGVSFEVPAGKKVAIVGGSGSGKSTIVrllfrfyepqKGSIYLAGQNIQDVSLEslrravgvvpqdavlfhntiyynll 567
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV----------NEGLYASGKARLISFLP------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 568 ygniNASPEEVYAVAKLAGLHDAILrmphGYDTqVGERGLKLSGGEKQRVAIARAILKDPPVILY--DEATSSLDSITEE 645
Cdd:cd03238 56 ----KFSRNKLIFIDQLQFLIDVGL----GYLT-LGQKLSTLSGGELQRVKLASELFSEPPGTLFilDEPSTGLHQQDIN 126
|
170 180 190
....*....|....*....|....*....|...
gi 47058990 646 TILGAMRDVV-KHRTSIFIAHRLSTVVDADEII 677
Cdd:cd03238 127 QLLEVIKGLIdLGNTVILIEHNLDVLSSADWII 159
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
143-421 |
4.26e-10 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 61.38 E-value: 4.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 143 SLGFLGGAKAMNIVVPFMFKYAVDSLNQMSGNMLNLSDAPNTVAT-MATAVLIGygvsragaAFFNEVRNAVFGKVAQNS 221
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDVASKESGDIEIFGLSLKTFALaLLGVFVVG--------AAANFGRVYLLRIAGERI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 222 IRRIAKNVFLHLHNLDLGFHLSRQTG---------------ALSKAIDRGTRGISFVLSALVFnllpivfeMTLVSSVLy 286
Cdd:cd18573 73 VARLRKRLFKSILRQDAAFFDKNKTGelvsrlssdtsvvgkSLTQNLSDGLRSLVSGVGGIGM--------MLYISPKL- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 287 ykcgaqfALVTLGTLGAYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNEKYEAQRYDGflKTYETA 366
Cdd:cd18573 144 -------TLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAK--KVDEVF 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47058990 367 SLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQG--IVAGALTVGDL-------VMVNGLLFQLS 421
Cdd:cd18573 215 DLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGslVASGELTVGDLtsflmyaVYVGSSVSGLS 278
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
453-689 |
1.34e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 61.34 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 453 RIKDKAMAspLQITPQTATVAFDNVhFEYIEGQKVLSGVSFEVPAGK-----KVAIVGGSGSGKSTIVRLLFRFYEPQKG 527
Cdd:COG1245 319 RIRDEPIE--FEVHAPRREKEEETL-VEYPDLTKSYGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 528 SI-----------YLagQNIQDVSLES-LRRAVGVVpqdavlFHNTIYYNLlygninaspeevyaVAKLAGLHdailRMp 595
Cdd:COG1245 396 EVdedlkisykpqYI--SPDYDGTVEEfLRSANTDD------FGSSYYKTE--------------IIKPLGLE----KL- 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 596 hgYDTQVGErglkLSGGEKQRVAIARAILKDPPVILYDEATSSLDSitEETILGA--MRDVV--KHRTSIFIAHRLsTVV 671
Cdd:COG1245 449 --LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDV--EQRLAVAkaIRRFAenRGKTAMVVDHDI-YLI 519
|
250 260
....*....|....*....|
gi 47058990 672 D--ADEIIVLSqGKVAERGT 689
Cdd:COG1245 520 DyiSDRLMVFE-GEPGVHGH 538
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
484-683 |
3.30e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.13 E-value: 3.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 484 GQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQ-DVSLESLRRAVGVVPQDAVLF-HNT 561
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQELNLVlQRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 562 IYYNLLYGNinaspeevYAVAKLAGLHDAILRMPH------GYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEA 635
Cdd:PRK10982 90 VMDNMWLGR--------YPTKGMFVDQDKMYRDTKaifdelDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 47058990 636 TSSLdsiTEE------TILGAMRDvvKHRTSIFIAHRLSTVVD-ADEIIVLSQGK 683
Cdd:PRK10982 162 TSSL---TEKevnhlfTIIRKLKE--RGCGIVYISHKMEEIFQlCDEITILRDGQ 211
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
484-640 |
3.44e-09 |
|
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: 59.95 E-value: 3.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 484 GQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLfrfyepqkgsiylAG--QNIQDVSLESLRRAVGVVPQDAVLFHN- 560
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------------AGvdKDFNGEARPQPGIKVGYLPQEPQLDPTk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 561 TIYYNLLYG-----NINASPEEVYA------------VAKLAGLHDAI------------------LRMPHGyDTQVGer 605
Cdd:TIGR03719 84 TVRENVEEGvaeikDALDRFNEISAkyaepdadfdklAAEQAELQEIIdaadawdldsqleiamdaLRCPPW-DADVT-- 160
|
170 180 190
....*....|....*....|....*....|....*
gi 47058990 606 glKLSGGEKQRVAIARAILKDPPVILYDEATSSLD 640
Cdd:TIGR03719 161 --KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
140-411 |
3.87e-09 |
|
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: 58.70 E-value: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 140 VAISLGFLGGAKAMNIVVPFMFKYAVDSLnqmsgnmlnlsdapnTVATMATAVLIGYGVSRAGA----AFFNEVRNAVFG 215
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLV---------------TIGSKSLGLLLGLALLLLGAyllrALLNFLRIYLNH 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 216 KVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGAL-SKAI---DRGTRGISFVLSALVFNLLPIVfemtLVSSVLYYKcGA 291
Cdd:cd18778 66 VAEQKVVADLRSDLYDKLQRLSLRYFDDRQTGDLmSRVIndvANVERLIADGIPQGITNVLTLV----GVAIILFSI-NP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 292 QFALVTLGTLGAYTAFTVAVTRW-RTRFRI------EMNKA--DNDAGNAAIdsllnyetvKYFNNEKYEAQRYDGFLKT 362
Cdd:cd18778 141 KLALLTLIPIPFLALGAWLYSKKvRPRYRKvrealgELNALlqDNLSGIREI---------QAFGREEEEAKRFEALSRR 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 47058990 363 YETASLKSTSTLAMlnFGQSAIFSVGLTAIMVLASQG--IVAGALTVGDLV 411
Cdd:cd18778 212 YRKAQLRAMKLWAI--FHPLMEFLTSLGTVLVLGFGGrlVLAGELTIGDLV 260
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
140-438 |
4.09e-09 |
|
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: 58.60 E-value: 4.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 140 VAISLGFLGGAkaMNIVVPFMFKYAVDSLNQMSGNMlnlsdapNTVATMATAVLIGygvsragaAFFNEVRNAVFGKVAQ 219
Cdd:cd18551 3 LALLLSLLGTA--ASLAQPLLVKNLIDALSAGGSSG-------GLLALLVALFLLQ--------AVLSALSSYLLGRTGE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 220 NSIRRIAKNVFLHLHNLDLGFHLSRQTG-----------ALSKAIDRGTrgISFVLSALVFnLLPIVFeMTLVSSVLyyk 288
Cdd:cd18551 66 RVVLDLRRRLWRRLLRLPVSFFDRRRSGdlvsrvtndttLLRELITSGL--PQLVTGVLTV-VGAVVL-MFLLDWVL--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 289 cgaqfALVTLGTLGAYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNEKYEAQRYDGFLKTYETASL 368
Cdd:cd18551 139 -----TLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGL 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47058990 369 KSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGALTVGDLV---MvngLLFQLSLPLNFLGTVYRETRQAL 438
Cdd:cd18551 214 KAAKIEALIGPLMGLAVQLALLVVLGVGGARVASGALTVGTLVaflL---YLFQLITPLSQLSSFFTQLQKAL 283
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
480-689 |
5.02e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.44 E-value: 5.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 480 EYIEGQKVLSGVSFEVPAGKK-----VAIVGGSGSGKSTIVRLLFRFYEPQKGSI-----------YLAGQniQDVSLES 543
Cdd:PRK13409 342 EYPDLTKKLGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVdpelkisykpqYIKPD--YDGTVED 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 544 LRRAVGVVpqdavlFHNTIYYNLLygninASPeevyavaklaglhdaiLRMPHGYDTQVGErglkLSGGEKQRVAIARAI 623
Cdd:PRK13409 420 LLRSITDD------LGSSYYKSEI-----IKP----------------LQLERLLDKNVKD----LSGGELQRVAIAACL 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47058990 624 LKDPPVILYDEATSSLDSitEETILGA--MRDVVKHR--TSIFIAHRLsTVVD--ADEIIVLSqGKVAERGT 689
Cdd:PRK13409 469 SRDADLYLLDEPSAHLDV--EQRLAVAkaIRRIAEEReaTALVVDHDI-YMIDyiSDRLMVFE-GEPGKHGH 536
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
576-683 |
5.39e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 59.74 E-value: 5.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 576 EEVYAvAKLAGLHDAILRMPHGYDTQVGE---RGLklSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMr 652
Cdd:TIGR00956 177 REEYA-KHIADVYMATYGLSHTRNTKVGNdfvRGV--SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRAL- 252
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 47058990 653 dvvkhRTSIFIAHRLSTVV------DA----DEIIVLSQGK 683
Cdd:TIGR00956 253 -----KTSANILDTTPLVAiyqcsqDAyelfDKVIVLYEGY 288
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
491-686 |
5.82e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.03 E-value: 5.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 491 VSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS-LESLRRAVGVVPQ---DAVLFHN-TIYYN 565
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpLDAVKKGMAYITEsrrDNGFFPNfSIAQN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 566 L-------------LYGNINASPEevyavAKLAGLHDAILRMP-HGYDTQVGErglkLSGGEKQRVAIARAILKDPPVIL 631
Cdd:PRK09700 362 MaisrslkdggykgAMGLFHEVDE-----QRTAENQRELLALKcHSVNQNITE----LSGGNQQKVLISKWLCCCPEVII 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 47058990 632 YDEATSSLDSITEETILGAMRDVVKH-RTSIFIAHRLSTVVDA-DEIIVLSQGKVAE 686
Cdd:PRK09700 433 FDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
140-430 |
6.77e-09 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 57.79 E-value: 6.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 140 VAISLGFLGGAKAMNIVVPFMFKYAVDS---------LNQMSGNMLNLsdapnTVATMATAVLIGYGVSRAGAAFFNEVR 210
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDEgiangdlsyILRTGLLMLLL-----ALLGLIAGILAGYFAAKASQGFGRDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 211 NAVFGKVAQNSirriaknvflhLHNLDlgfHLSrqTGALskaIDRGTRGISFVLSAlVFNLLPIVFE---MTLVSSVLYY 287
Cdd:cd18548 76 KDLFEKIQSFS-----------FAEID---KFG--TSSL---ITRLTNDVTQVQNF-VMMLLRMLVRapiMLIGAIIMAF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 288 KCGAQFALVTLGTLGAYTAFTVAVTRW-RTRFRIEMNKadNDAGNAAI-DSLLNYETVKYFNNEKYEAQRYDGFLKTYET 365
Cdd:cd18548 136 RINPKLALILLVAIPILALVVFLIMKKaIPLFKKVQKK--LDRLNRVVrENLTGIRVIRAFNREDYEEERFDKANDDLTD 213
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47058990 366 ASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGALTVGDLVMVNGLLFQLSLPLNFLGTV 430
Cdd:cd18548 214 TSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLSMV 278
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
139-431 |
8.77e-09 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 57.48 E-value: 8.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 139 RVAISLGFLGGAKAMNIVVPFMFKYAVDSlNQMSGNMLNLsdapntvatmaTAVLIGYGVSRAGAAFFNEVRNAVFGKVA 218
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLIKIAIDE-YIPNGDLSGL-----------LIIALLFLALNLVNWVASRLRIYLMAKVG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 219 QNSIRRIAKNVFLHLHNLDLGFHLSRQTGA-LSKAI-DRGTrgISFVLSALVFNLLPIVFEMTLVSSVLYYKcGAQFALV 296
Cdd:cd18545 69 QRILYDLRQDLFSHLQKLSFSFFDSRPVGKiLSRVInDVNS--LSDLLSNGLINLIPDLLTLVGIVIIMFSL-NVRLALV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 297 TLGTLgayTAFTVAVTRW----RTRFRIEMNKADNdaGNAAI-DSLLNYETVKYFNNEKYEAQRYDGFLKTYETASLKST 371
Cdd:cd18545 146 TLAVL---PLLVLVVFLLrrraRKAWQRVRKKISN--LNAYLhESISGIRVIQSFAREDENEEIFDELNRENRKANMRAV 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47058990 372 STLAMLNFGQSAIFSVGLTAIMVLASQGIVAGALTVGDLV-MVN--GLLFQlslPLNFLGTVY 431
Cdd:cd18545 221 RLNALFWPLVELISALGTALVYWYGGKLVLGGAITVGVLVaFIGyvGRFWQ---PIRNLSNFY 280
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
482-690 |
1.06e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 56.72 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 482 IEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLF--RFYEPQKGSIYLAGQNIQDVSLESlRRAVGVV-----PQD 554
Cdd:PRK09580 11 VEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPED-RAGEGIFmafqyPVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 555 AVLFHNTIYynlLYGNINA-------SPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGlkLSGGEKQRVAIARAILKDP 627
Cdd:PRK09580 90 IPGVSNQFF---LQTALNAvrsyrgqEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47058990 628 PVILYDEATSSLD----SITEETIlGAMRDvvKHRTSIFIAH--RLSTVVDADEIIVLSQGKVAERGTH 690
Cdd:PRK09580 165 ELCILDESDSGLDidalKIVADGV-NSLRD--GKRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDF 230
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
469-684 |
1.35e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 55.73 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 469 TATVAFDNVHFEYIEGQ---KVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLL---FRFYEPQKGSIYLAGQNIQDVSlE 542
Cdd:cd03233 1 ASTLSWRNISFTTGKGRskiPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYKEFA-E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 543 SLRRAVGVVPQDAVLFHN-TIYynllygninaspEEVYAVAKLAGlhDAILRmphgydtqvgerglKLSGGEKQRVAIAR 621
Cdd:cd03233 80 KYPGEIIYVSEEDVHFPTlTVR------------ETLDFALRCKG--NEFVR--------------GISGGERKRVSIAE 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47058990 622 AILKDPPVILYDEATSSLDSITEETILGAMRDVVKhrtsifiAHRLSTVVDA-----------DEIIVLSQGKV 684
Cdd:cd03233 132 ALVSRASVLCWDNSTRGLDSSTALEILKCIRTMAD-------VLKTTTFVSLyqasdeiydlfDKVLVLYEGRQ 198
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
488-685 |
1.53e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.75 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 488 LSG-----VSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESlRRAVGVV--PQD------ 554
Cdd:PRK15439 274 LTGegfrnISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-RLARGLVylPEDrqssgl 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 555 ---AVLFHNTiyYNLLYGNINASPEEVYAVAKLAGLHDAI-LRMPHGyDTQVGerglKLSGGEKQRVAIARAILKDPPVI 630
Cdd:PRK15439 353 yldAPLAWNV--CALTHNRRGFWIKPARENAVLERYRRALnIKFNHA-EQAAR----TLSGGNQQKVLIAKCLEASPQLL 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 47058990 631 LYDEATSSLDSITEETILGAMRDVVKHRTSI-FIAHRLSTVVD-ADEIIVLSQGKVA 685
Cdd:PRK15439 426 IVDEPTRGVDVSARNDIYQLIRSIAAQNVAVlFISSDLEEIEQmADRVLVMHQGEIS 482
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
486-684 |
1.84e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 57.53 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 486 KVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ-KGSIYLAGQNIQDVS-LESLRRAVGVVPQD--------- 554
Cdd:TIGR02633 274 KRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNpAQAIRAGIAMVPEDrkrhgivpi 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 555 AVLFHNTIYYNL----LYGNINASPEEVYAVAKLAGLHdaiLRMPHGyDTQVGerglKLSGGEKQRVAIARAILKDPPVI 630
Cdd:TIGR02633 354 LGVGKNITLSVLksfcFKMRIDAAAELQIIGSAIQRLK---VKTASP-FLPIG----RLSGGNQQKAVLAKMLLTNPRVL 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 47058990 631 LYDEATSSLDSITEETILGAMRDVVKHRTS-IFIAHRLSTVVD-ADEIIVLSQGKV 684
Cdd:TIGR02633 426 ILDEPTRGVDVGAKYEIYKLINQLAQEGVAiIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
498-679 |
1.86e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.87 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 498 GKKVAIVGGSGSGKSTIVRLLfrfyepqkgsiylAGQ---NIQDVSLEslrravgvVPQDAVL--FHNTI---YYNLLY- 568
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKIL-------------SGElkpNLGDYDEE--------PSWDEVLkrFRGTElqdYFKKLAn 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 569 GNINAS--PEEVYAVAKL--------------AGLHDAI---LRMPHGYDTQVGErglkLSGGEKQRVAIARAILKDPPV 629
Cdd:COG1245 158 GEIKVAhkPQYVDLIPKVfkgtvrellekvdeRGKLDELaekLGLENILDRDISE----LSGGELQRVAIAAALLRDADF 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 47058990 630 ILYDEATSSLDsITEE-TILGAMRDVVKHRTSIFIA-HRLsTVVD--ADEIIVL 679
Cdd:COG1245 234 YFFDEPSSYLD-IYQRlNVARLIRELAEEGKYVLVVeHDL-AILDylADYVHIL 285
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
482-640 |
1.94e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.20 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 482 IEGQKVL-SGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQdvsleSLRRAvgvvpqdavlFHn 560
Cdd:PRK13538 10 ERDERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR-----RQRDE----------YH- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 561 tiyYNLLY-GNINA-----SPEE-VYAVAKLAGLHD-----AILRmphgydtQVGERGLK------LSGGEKQRVAIARA 622
Cdd:PRK13538 74 ---QDLLYlGHQPGiktelTALEnLRFYQRLHGPGDdealwEALA-------QVGLAGFEdvpvrqLSAGQQRRVALARL 143
|
170
....*....|....*...
gi 47058990 623 ILKDPPVILYDEATSSLD 640
Cdd:PRK13538 144 WLTRAPLWILDEPFTAID 161
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
229-444 |
1.99e-08 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 56.35 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 229 VFLHLHNLDLGFHLSRQTGALskaIDRgTRGIS----FVLSALVFNLLPIVFEMTLVSSVLYYKcgAQFALVTLGTLGAY 304
Cdd:cd18588 81 LFRHLLRLPLSYFESRQVGDT---VAR-VRELEsirqFLTGSALTLVLDLVFSVVFLAVMFYYS--PTLTLIVLASLPLY 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 305 TAFTVAVTRwRTRFRIEmNKADNDAGNAA--IDSLLNYETVKYFNNEKYEAQRYDGFLKTYETASLKsTSTLAmlNFGQS 382
Cdd:cd18588 155 ALLSLLVTP-ILRRRLE-EKFQRGAENQSflVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFK-TANLS--NLASQ 229
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47058990 383 AIFSVGLT---AIMVLASQGIVAGALTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 444
Cdd:cd18588 230 IVQLIQKLttlAILWFGAYLVMDGELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQAKVSVERL 294
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
498-679 |
2.33e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.51 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 498 GKKVAIVGGSGSGKSTIVRLLfrfyepqkgsiylAGQ---NIQDVSLES-----LRRAVGVVPQDavlfhntiYYNLLY- 568
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKIL-------------SGElipNLGDYEEEPswdevLKRFRGTELQN--------YFKKLYn 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 569 GNINAS--PEEVYAVAK-LAGLHDAILRmphgydtQVGERGL-------------------KLSGGEKQRVAIARAILKD 626
Cdd:PRK13409 158 GEIKVVhkPQYVDLIPKvFKGKVRELLK-------KVDERGKldevverlglenildrdisELSGGELQRVAIAAALLRD 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 47058990 627 PPVILYDEATSSLDsITEE-TILGAMRDVVKHRTSIFIAHRLsTVVD--ADEIIVL 679
Cdd:PRK13409 231 ADFYFFDEPTSYLD-IRQRlNVARLIRELAEGKYVLVVEHDL-AVLDylADNVHIA 284
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
467-685 |
2.69e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 57.18 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 467 PQTATVAFDNVHFEYIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYlagqniqdvslESLRR 546
Cdd:PLN03073 504 PGPPIISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF-----------RSAKV 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 547 AVGVVPQdavlfHNTIYYNLlygninASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLK----LSGGEKQRVAIARA 622
Cdd:PLN03073 573 RMAVFSQ-----HHVDGLDL------SSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQpmytLSGGQKSRVAFAKI 641
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47058990 623 ILKDPPVILYDEATSSLDSITEETILGAMrdVVKHRTSIFIAHRLSTVVDA-DEIIVLSQGKVA 685
Cdd:PLN03073 642 TFKKPHILLLDEPSNHLDLDAVEALIQGL--VLFQGGVLMVSHDEHLISGSvDELWVVSEGKVT 703
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
140-425 |
3.84e-08 |
|
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: 55.49 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 140 VAISLGFLGGAKAMNIVVPFMFKYAVDSLNQMSGNMLNlsDAPNTVATMATAVLIGYGVSragaAFFNEVRNAVFGKVAQ 219
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGG--VDFSGLLRILLLLLGLYLLS----ALFSYLQNRLMARVSQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 220 NSIRRIAKNVFLHLHNLDLGFHLSRQTGA-LSKA---IDRGTRGISFVLSALVFNLLPIV--FEMTLVSSVlyykcgaQF 293
Cdd:cd18547 75 RTVYDLRKDLFEKLQRLPLSYFDTHSHGDiMSRVtndVDNISQALSQSLTQLISSILTIVgtLIMMLYISP-------LL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 294 ALVTLGTLGAYTAFTVAVTRW-RTRFRIEMNKadndAG--NAAID-SLLNYETVKYFNNEKYEAQRYDGFLKTYETASLK 369
Cdd:cd18547 148 TLIVLVTVPLSLLVTKFIAKRsQKYFRKQQKA----LGelNGYIEeMISGQKVVKAFNREEEAIEEFDEINEELYKASFK 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47058990 370 STSTLAML--------NFGQSAIFSVGltAIMVLasqgivAGALTVGDLV----MVNgllfQLSLPLN 425
Cdd:cd18547 224 AQFYSGLLmpimnfinNLGYVLVAVVG--GLLVI------NGALTVGVIQaflqYSR----QFSQPIN 279
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
230-444 |
4.15e-08 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 55.26 E-value: 4.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 230 FLHLHNLDLGFHLSRQTGALskaIDR-----------GTRGISFVLSAL-VFNLLPIVFemtlvssvlYYKcgAQFALVT 297
Cdd:cd18568 82 YKHLLSLPLSFFASRKVGDI---ITRfqenqkirrflTRSALTTILDLLmVFIYLGLMF---------YYN--LQLTLIV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 298 LGTLGAYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNEKYEAQRYDGFLKTYETASLKSTSTLAML 377
Cdd:cd18568 148 LAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVL 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47058990 378 NFGQSAIFSVGLTAIMVLASQGIVAGALTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 444
Cdd:cd18568 228 QLISSLINHLGTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
484-648 |
9.22e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 55.33 E-value: 9.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 484 GQKVL-SGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLaGQNIQdvsleslrraVGVVPQ--DAVLFHN 560
Cdd:TIGR03719 333 GDKLLiDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK----------LAYVDQsrDALDPNK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 561 TIYynllygninaspEEVyavaklAGLHDAIL----RMP----------HGYDTQ--VGErglkLSGGEKQRVAIARAIL 624
Cdd:TIGR03719 402 TVW------------EEI------SGGLDIIKlgkrEIPsrayvgrfnfKGSDQQkkVGQ----LSGGERNRVHLAKTLK 459
|
170 180
....*....|....*....|....*...
gi 47058990 625 KDPPVILYDEATSSLDSIT----EETIL 648
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDVETlralEEALL 487
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
154-438 |
1.16e-07 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 54.18 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 154 NIVVPFMFKYAVDSLNQMSGNmlNLSDAPNTVATMATAVLIGYGVSragaAFFNEVRNAVFGKVAQNSIRRIAKNVFLHL 233
Cdd:cd18780 12 NLALPYFFGQVIDAVTNHSGS--GGEEALRALNQAVLILLGVVLIG----SIATFLRSWLFTLAGERVVARLRKRLFSAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 234 HNLDLGFHLSRQTGALskaIDR-----------GTRGISFVLSALVFNLLPIVFEMTLvssvlyykcGAQFALVTLGTLG 302
Cdd:cd18780 86 IAQEIAFFDVTRTGEL---LNRlssdtqvlqnaVTVNLSMLLRYLVQIIGGLVFMFTT---------SWKLTLVMLSVVP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 303 AYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNEKYEAQRYDGflKTYETASL--KSTSTLAMLNFG 380
Cdd:cd18780 154 PLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSE--KINESYLLgkKLARASGGFNGF 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 47058990 381 QSAIFSVGLTAIMVLASQGIVAGALTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQAL 438
Cdd:cd18780 232 MGAAAQLAIVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAV 289
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
485-685 |
1.30e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.74 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 485 QKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS-LESL----------RRAVGVVPQ 553
Cdd:PRK10982 261 QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaNEAInhgfalvteeRRSTGIYAY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 554 DAVLFhNTIYYNL--------LYGNINASPEEVYAVaklaglhDAILRMPHGYDTQVGErglkLSGGEKQRVAIARAILK 625
Cdd:PRK10982 341 LDIGF-NSLISNIrnyknkvgLLDNSRMKSDTQWVI-------DSMRVKTPGHRTQIGS----LSGGNQQKVIIGRWLLT 408
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47058990 626 DPPVILYDEATSSLDSITEETILGAMRDVVKH-RTSIFIAHRLSTVVD-ADEIIVLSQGKVA 685
Cdd:PRK10982 409 QPEILMLDEPTRGIDVGAKFEIYQLIAELAKKdKGIIIISSEMPELLGiTDRILVMSNGLVA 470
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
140-438 |
1.77e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 53.64 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 140 VAISLGFLGGAKAMNIVVPFMFKYAVDS---------LNQMSGNMLNLsdapnTVATMATAVLIGYGVSRAGAAFFNEVR 210
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDalpqgdlglLVLLALGMVAV-----AVASALLGVVQTYLSARIGQGVMYDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 211 NAVFGkvaqnsirriaknvflHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIVFemTLVSSVlyykcG 290
Cdd:cd18550 76 VQLYA----------------HLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVV--TLVATL-----V 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 291 AQFAL---VTLGTLGAYTAFtVAVTRW--RTRFRIEMNKADNdagNAAIDSLLNyET--------VKYFNNEKYEAQRYD 357
Cdd:cd18550 133 AMLALdwrLALLSLVLLPLF-VLPTRRvgRRRRKLTREQQEK---LAELNSIMQ-ETlsvsgallVKLFGREDDEAARFA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 358 GflKTYETASLKSTSTLAMLNFGQ--SAIFSVGLTAIMVLASQGIVAGALTVGDLVMVNGLLFQLSLPLNFLGTVYRETR 435
Cdd:cd18550 208 R--RSRELRDLGVRQALAGRWFFAalGLFTAIGPALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLM 285
|
...
gi 47058990 436 QAL 438
Cdd:cd18550 286 TSL 288
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
475-645 |
1.79e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.57 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 475 DNVHFEyIEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYlAGQNIQDVSLESLRRAVGvvPQd 554
Cdd:PRK11147 323 ENVNYQ-IDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH-CGTKLEVAYFDQHRAELD--PE- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 555 avlfhNTIYYNLLYGN----INASPEEVyavakLAGLHDaILRMPHGYDTQVGerglKLSGGEKQRVAIARAILKDPPVI 630
Cdd:PRK11147 398 -----KTVMDNLAEGKqevmVNGRPRHV-----LGYLQD-FLFHPKRAMTPVK----ALSGGERNRLLLARLFLKPSNLL 462
|
170
....*....|....*
gi 47058990 631 LYDEATSSLDSITEE 645
Cdd:PRK11147 463 ILDEPTNDLDVETLE 477
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
484-684 |
1.95e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.16 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 484 GQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQK-GSIYLAGQniqDVSLESLRRAV-------------- 548
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGK---PVKIRNPQQAIaqgiamvpedrkrd 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 549 GVVPQDAVLfHNTIYYNL----LYGNINASPEEVYAVAKLAGLHdaiLRMPHGyDTQVGerglKLSGGEKQRVAIARAIL 624
Cdd:PRK13549 351 GIVPVMGVG-KNITLAALdrftGGSRIDDAAELKTILESIQRLK---VKTASP-ELAIA----RLSGGNQQKAVLAKCLL 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47058990 625 KDPPVILYDEATSSLDSITEETILGAMRDVVKHRTS-IFIAHRLSTVVD-ADEIIVLSQGKV 684
Cdd:PRK13549 422 LNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAiIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
493-703 |
2.02e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 53.57 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 493 FEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ---KGSIYLAGQNIQDVSLESLRR----AVGVVPQDAVLFHNTiyyn 565
Cdd:PRK09473 37 FSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKELNKlraeQISMIFQDPMTSLNP---- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 566 llYGNINASPEEVYAVAKLAGLHDAI---LRM----------------PHgydtqvgerglKLSGGEKQRVAIARAILKD 626
Cdd:PRK09473 113 --YMRVGEQLMEVLMLHKGMSKAEAFeesVRMldavkmpearkrmkmyPH-----------EFSGGMRQRVMIAMALLCR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 627 PPVILYDEATSSLDSITEETILGAMRDVVKH-RTS-IFIAHRLSTVVD-ADEIIVLSQGKVAERGTHYGLLANSSSIYSE 703
Cdd:PRK09473 180 PKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAiIMITHDLGVVAGiCDKVLVMYAGRTMEYGNARDVFYQPSHPYSI 259
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
483-642 |
2.14e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.13 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 483 EGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAgQNIQdvsleslrraVGVVPQD-AVLFHNT 561
Cdd:PRK15064 330 DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS-ENAN----------IGYYAQDhAYDFEND 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 562 IyyNLLygninaspeEVYAVAKLAGlHD-----AIL-RMPHGYDtQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEA 635
Cdd:PRK15064 399 L--TLF---------DWMSQWRQEG-DDeqavrGTLgRLLFSQD-DIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEP 465
|
....*....
gi 47058990 636 TSSLD--SI 642
Cdd:PRK15064 466 TNHMDmeSI 474
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
486-682 |
4.94e-07 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 50.70 E-value: 4.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 486 KVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ--KGSIYLAGQNIQdvslESLRRAVGVVPQDAVLFHN-TI 562
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLD----KNFQRSTGYVEQQDVHSPNlTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 563 YYNLLYGninaspeevyavAKLaglhdailrmphgydtqvgeRGLKLSggEKQRVAIARAILKDPPVILYDEATSSLDSI 642
Cdd:cd03232 97 REALRFS------------ALL--------------------RGLSVE--QRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 47058990 643 TEETILGAMRDVVKH-RTSIFIAHRLSTVVDA--DEIIVLSQG 682
Cdd:cd03232 143 AAYNIVRFLKKLADSgQAILCTIHQPSASIFEkfDRLLLLKRG 185
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
484-640 |
5.92e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.81 E-value: 5.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 484 GQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLA-GQNI------------QDVsLESLRRAVGV 550
Cdd:PRK11819 19 KKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPApGIKVgylpqepqldpeKTV-RENVEEGVAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 551 VpQDAVLFHNTIYynLLYGNINASPEEVyaVAKLAGLHDAI------------------LRMPHGyDTQVGerglKLSGG 612
Cdd:PRK11819 98 V-KAALDRFNEIY--AAYAEPDADFDAL--AAEQGELQEIIdaadawdldsqleiamdaLRCPPW-DAKVT----KLSGG 167
|
170 180
....*....|....*....|....*...
gi 47058990 613 EKQRVAIARAILKDPPVILYDEATSSLD 640
Cdd:PRK11819 168 ERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
482-689 |
1.07e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.80 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 482 IEGQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRF--YEPQKGSIYLAGQNIQDvsLESLRRA------------ 547
Cdd:CHL00131 17 VNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILD--LEPEERAhlgiflafqypi 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 548 --VGVVPQDavlFHNTIYYNLL--YGNINASPEEVYAV----AKLAGLHdailrmPHGYDTQVGErglKLSGGEKQRVAI 619
Cdd:CHL00131 95 eiPGVSNAD---FLRLAYNSKRkfQGLPELDPLEFLEIinekLKLVGMD------PSFLSRNVNE---GFSGGEKKRNEI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47058990 620 ARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHRTSI-FIAH--RLSTVVDADEIIVLSQGKVAERGT 689
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIiLITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
201-387 |
1.57e-06 |
|
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: 50.91 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 201 AGAAFFNEVRNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFH--LSRQTGALSKAIDRGTRGISFVLSALVFNLLPIVFem 278
Cdd:cd18578 63 IVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFddPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIV-- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 279 TLVSSV---LYYkcGAQFALVTLGTLGAYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNEKYEAQR 355
Cdd:cd18578 141 TLVAGLiiaFVY--GWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEK 218
|
170 180 190
....*....|....*....|....*....|....
gi 47058990 356 YDGFLKTYETASLKStSTLAMLNFG--QSAIFSV 387
Cdd:cd18578 219 YEEALEEPLKKGLRR-ALISGLGFGlsQSLTFFA 251
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
142-442 |
2.00e-06 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 50.11 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 142 ISLGFLGGAKAMNI--VVPFMFKYAVDSLNQmsGNMLNLSDAPNTVATMATAVLIGYGVSRAGAAFfneVRNAVFGKVAQ 219
Cdd:cd18554 1 IIITIVIGLVRFGIplLLPLILKYIVDDVIQ--GSSLTLDEKVYKLFTIIGIMFFIFLILRPPVEY---YRQYFAQWIAN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 220 NSIRRIAKNVFLHLHNLDLGFHLSRQTGAL-SKAIDRGTRGISFVLSALVFNLLPIVFEMTLVSSVLYYKcgaqfALVTL 298
Cdd:cd18554 76 KILYDIRKDLFDHLQKLSLRYYANNRSGEIiSRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLN-----PKLTF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 299 GTLGAYTAFTVAVTRWRTRFRI---EMNKADNDAGNAAIDSLLNYETVKYFNNEKYEAQRYDGFLKTYETASLKSTS--- 372
Cdd:cd18554 151 VSLVIFPFYILAVKYFFGRLRKltkERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRwna 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47058990 373 -TLAMLNfgqsAIFSVGLTAIMVLASQGIVAGALTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMN 442
Cdd:cd18554 231 kTFSAVN----TITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMD 297
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
141-428 |
3.17e-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: 49.72 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 141 AISLGFLGGAKAMNIVVPFMFKYAVDSLNQMSGNMLNLsdapntvaTMATAVLIGYGVSRAGAAFFneVRNAVFGkvaqn 220
Cdd:cd18541 2 LLGILFLILVDLLQLLIPRIIGRAIDALTAGTLTASQL--------LRYALLILLLALLIGIFRFL--WRYLIFG----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 221 SIRRIAK----NVFLHLHNLDLGFHLSRQTGALskaIDRGT------R-----GISFVLSALVFNLLPIVFeMTLVSSVL 285
Cdd:cd18541 67 ASRRIEYdlrnDLFAHLLTLSPSFYQKNRTGDL---MARATndlnavRmalgpGILYLVDALFLGVLVLVM-MFTISPKL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 286 yykcgaqfalvTLGTLGAYTAFTVAVTRW----RTRFRI------EMNkadndagNAAIDSLLNYETVKYFNNEKYEAQR 355
Cdd:cd18541 143 -----------TLIALLPLPLLALLVYRLgkkiHKRFRKvqeafsDLS-------DRVQESFSGIRVIKAFVQEEAEIER 204
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47058990 356 YDGFLKTYETASLKststLAMLN--FGQSAIFSVGLTAIMVLA--SQGIVAGALTVGDLVMVNGLLFQLSLPLNFLG 428
Cdd:cd18541 205 FDKLNEEYVEKNLR----LARVDalFFPLIGLLIGLSFLIVLWygGRLVIRGTITLGDLVAFNSYLGMLIWPMMALG 277
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
484-694 |
3.47e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.44 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 484 GQKVLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLF-RFYEPQ-------KGSIYLAGQNIQDVSLESLRRAVGVVPQDA 555
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 556 V-LFHNTIYYNLLYGNINASPEEVYAVAKLAGLHDAILRMPhGYDTQVGERGLKLSGGEKQRVAIARAILK--------- 625
Cdd:PRK13547 93 QpAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALA-GATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaq 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47058990 626 DPPVILYDEATSSLDSITEETILGAMRDVVK--HRTSIFIAHRLSTVV-DADEIIVLSQGKVAERGTHYGLL 694
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNLAArHADRIAMLADGAIVAHGAPADVL 243
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
488-640 |
3.88e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.00 E-value: 3.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 488 LSG-----VSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSleslrravgvvPQDAVlfHNTI 562
Cdd:PRK10762 263 LSGpgvndVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRS-----------PQDGL--ANGI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 563 YY------------------NL----------LYGNINASpEEVYAVAKLAGLHDaiLRMPhGYDTQVGerglKLSGGEK 614
Cdd:PRK10762 330 VYisedrkrdglvlgmsvkeNMsltalryfsrAGGSLKHA-DEQQAVSDFIRLFN--IKTP-SMEQAIG----LLSGGNQ 401
|
170 180
....*....|....*....|....*.
gi 47058990 615 QRVAIARAILKDPPVILYDEATSSLD 640
Cdd:PRK10762 402 QKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
140-437 |
4.01e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 49.41 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 140 VAISLGFLGGAKAMNIVVPFMFKYAVDS-LNQMSGNMLNLsdapnTVATMATAVLIGYGVSRAgaaffnevRNAVFGKVA 218
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDSgVRAGDLGVLLL-----AAAAYLAVVLAGWVAQRA--------QTRLTGRTG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 219 QNSIRRIAKNVFLHLHNLDLGFH--------LSRQTG---ALSKAIDRGtrgisfvLSALVFNLLPIVFeMTLVSSVLyy 287
Cdd:cd18546 68 ERLLYDLRLRVFAHLQRLSLDFHeretsgriMTRMTSdidALSELLQTG-------LVQLVVSLLTLVG-IAVVLLVL-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 288 kcGAQFALVTLGTLgaytAFTVAVTRWrtrFRIEMNKADNDAGNAAIDSLLNY-ET------VKYFNNEKYEAQRYDGFL 360
Cdd:cd18546 138 --DPRLALVALAAL----PPLALATRW---FRRRSSRAYRRARERIAAVNADLqETlagirvVQAFRRERRNAERFAELS 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 361 KTYETASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGALTVGDLV---MVNGLLFQlslPLNFLGTVYRETRQA 437
Cdd:cd18546 209 DDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAAGTLTVGVLVaflLYLRRFFA---PIQQLSQVFDSYQQA 285
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
495-679 |
5.02e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 48.52 E-value: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 495 VPA-GKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSI-----------YLAGQNIQDVsLESLRRA---VGVVPQDAVLFH 559
Cdd:cd03236 22 VPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildEFRGSELQNY-FTKLLEGdvkVIVKPQYVDLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 560 NTIYynllyGNINASPEEVYAVAKLAGLHDAiLRMPHGYDTQVGErglkLSGGEKQRVAIARAILKDPPVILYDEATSSL 639
Cdd:cd03236 101 KAVK-----GKVGELLKKKDERGKLDELVDQ-LELRHVLDRNIDQ----LSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 47058990 640 DSITEETILGAMRDVVKHRTSIFIA-HRLStVVD--ADEIIVL 679
Cdd:cd03236 171 DIKQRLNAARLIRELAEDDNYVLVVeHDLA-VLDylSDYIHCL 212
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
223-438 |
5.62e-06 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 49.01 E-value: 5.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 223 RRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSA-------LVFNLLPIVFEMTLVSSVLyykcgaqfAL 295
Cdd:cd18589 69 SRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSEnlsllmwYLARGLFLFIFMLWLSPKL--------AL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 296 VTLGTLGAYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNEKYEAQRYDGFL-KTYETASLKSTS-T 373
Cdd:cd18589 141 LTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLqKTYRLNKKEAAAyA 220
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47058990 374 LAMLNFGQSAIF-SVGltaIMVLASQGIVAGALTVGDLVMVngLLFQL--SLPLNFLGTVYRETRQAL 438
Cdd:cd18589 221 VSMWTSSFSGLAlKVG---ILYYGGQLVTAGTVSSGDLVTF--VLYELqfTSAVEVLLSYYPSVMKAV 283
|
|
| ABC_6TM_McjD_like |
cd18556 |
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ... |
220-438 |
6.00e-06 |
|
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter McjD and similar proteins; This group represents the 6-TM subunit of the ABC transporter McjD that exports the antibacterial peptide microcin J25, which is an antimicrobial peptide produced by Enterobacteriaceae against other microorganisms for survival under nutrient starvation. Thus, the ABC exporter McjD provides self-immunity of the producing bacteria through export of the toxic peptide out of the cell. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.
Pssm-ID: 350000 Cd Length: 298 Bit Score: 48.79 E-value: 6.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 220 NSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLP----IVFEMTLVSSVLYYKCGAQFAL 295
Cdd:cd18556 74 ELIISISSSYFRYLYEQPKTFFVKENSGDITQRLNQASNDLYTLVRNLSTNILPpllqLIIAIVVILSSGDYFVAALFLL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 296 VTLgtlgAYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNEKYEAQRYDGFLKTYETAS---LKSTS 372
Cdd:cd18556 154 YAV----LFVINNTIFTKKIVSLRNDLMDAGRKSYSLLTDSVKNIVAAKQNNAFDFLFKRYEATLTNDRNSQkryWKLTF 229
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47058990 373 TLAMLNFGQSAIFsVGLTAIMVLAsqGIVAGALTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQAL 438
Cdd:cd18556 230 KMLILNSLLNVIL-FGLSFFYSLY--GVVNGQVSIGHFVLITSYILLLSTPIESLGNMLSELRQSV 292
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
488-742 |
7.23e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.50 E-value: 7.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 488 LSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGqniqdvSLESLRRAVGVVPQDAVLfHNTIYYNLL 567
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG------SAALIAISSGLNGQLTGI-ENIELKGLM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 568 YGNINASPEEVY-AVAKLAGLHDAILRMPHGYdtqvgerglklSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEET 646
Cdd:PRK13545 113 MGLTKEKIKEIIpEIIEFADIGKFIYQPVKTY-----------SSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 647 ILGAMRDVVKH-RTSIFIAHRLSTVVD-ADEIIVLSQGKVAERG------THYGLLANSssiYSEMwhtqstriqnhdnl 718
Cdd:PRK13545 182 CLDKMNEFKEQgKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGdikevvDHYDEFLKK---YNQM-------------- 244
|
250 260
....*....|....*....|....
gi 47058990 719 gwdakkeslsKEEERKKLQEEIVN 742
Cdd:PRK13545 245 ----------SVEERKDFREEQIS 258
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
607-689 |
1.38e-05 |
|
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: 46.41 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 607 LKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKH--RTSIFIAHRLSTVVDADEIIVLSQGKV 684
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEgkKTALVVEHDLAVLDYLSDRIHVFEGEP 149
|
....*
gi 47058990 685 AERGT 689
Cdd:cd03222 150 GVYGI 154
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
182-425 |
2.41e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 46.81 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 182 PNTVATMATAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGIS 261
Cdd:cd18566 34 PNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERLNSLEQIRE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 262 FVLSALVFNL--LPIVFEMTLVSSVLyykcGAQFALVTLGTLGAYTAFTVAV-TRWRTRFRiEMNKADNDAGNAAIDSLL 338
Cdd:cd18566 114 FLTGQALLALldLPFVLIFLGLIWYL----GGKLVLVPLVLLGLFVLVAILLgPILRRALK-ERSRADERRQNFLIETLT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 339 NYETVKYFNNEKYEAQRYDGFLKTYETASLKSTSTLAMLNfGQSAIFSVgLTAIMVLA--SQGIVAGALTVGDLVMVNGL 416
Cdd:cd18566 189 GIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQ-TLGQLFSQ-VSMVAVVAfgALLVINGDLTVGALIACTML 266
|
....*....
gi 47058990 417 LFQLSLPLN 425
Cdd:cd18566 267 SGRVLQPLQ 275
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
483-667 |
4.72e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 47.32 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 483 EGQKVLSGVS--------FEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQdVSLESLRRAVGVVPQ- 553
Cdd:TIGR01257 1942 ELTKVYSGTSspavdrlcVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-TNISDVHQNMGYCPQf 2020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 554 DAVlfhntiyYNLLYGNinaspEEVYAVAKLAGLHDAILRMPHGYDTQvgERGLKL---------SGGEKQRVAIARAIL 624
Cdd:TIGR01257 2021 DAI-------DDLLTGR-----EHLYLYARLRGVPAEEIEKVANWSIQ--SLGLSLyadrlagtySGGNKRKLSTAIALI 2086
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 47058990 625 KDPPVILYDEATSSLDSITEETILGAMRDVVKH-RTSIFIAHRL 667
Cdd:TIGR01257 2087 GCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREgRAVVLTSHSM 2130
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
482-682 |
7.68e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.26 E-value: 7.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 482 IEGQK--VLSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLfrfyePQK--------GSIYLAGQNIQdvslESLRRAVGVV 551
Cdd:TIGR00956 771 IKKEKrvILNNVDGWVKPGTLTALMGASGAGKTTLLNVL-----AERvttgvitgGDRLVNGRPLD----SSFQRSIGYV 841
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 552 PQ-DAVLFHNTIYYNLLYGNINASPEEVYAVAKLAGLHDAI--LRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPP 628
Cdd:TIGR00956 842 QQqDLHLPTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIklLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPK 921
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 47058990 629 VILY-DEATSSLDSITEETILGAMRDVVKHRTSIFIA-HRLSTVVDA--DEIIVLSQG 682
Cdd:TIGR00956 922 LLLFlDEPTSGLDSQTAWSICKLMRKLADHGQAILCTiHQPSAILFEefDRLLLLQKG 979
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
496-677 |
1.15e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.12 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 496 PAGKKVAIVGGSGSGKSTIVR-----LLFRFYEPQKGSIYLAGQNIQDVSLEslrrAVGVVPQdavlfhntiyynllygn 570
Cdd:cd03227 19 GEGSLTIITGPNGSGKSTILDaiglaLGGAQSATRRRSGVKAGCIVAAVSAE----LIFTRLQ----------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 571 inaspeevyavaklaglhdailrmphgydtqvgerglkLSGGEKQRVAIARAI----LKDPPVILYDEATSSLDSITEET 646
Cdd:cd03227 78 --------------------------------------LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQA 119
|
170 180 190
....*....|....*....|....*....|..
gi 47058990 647 ILGAMRD-VVKHRTSIFIAHRLSTVVDADEII 677
Cdd:cd03227 120 LAEAILEhLVKGAQVIVITHLPELAELADKLI 151
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
472-640 |
1.37e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.11 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 472 VAFDNVHFEYieGQKVL-SGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLaGQNIQdvsleslrraVGV 550
Cdd:PRK11819 325 IEAENLSKSF--GDRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVK----------LAY 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 551 VPQ--DAVLFHNTIYynllygninaspEEVyavaklAGLHDAIL----RMP----------HGYDTQ--VGErglkLSGG 612
Cdd:PRK11819 392 VDQsrDALDPNKTVW------------EEI------SGGLDIIKvgnrEIPsrayvgrfnfKGGDQQkkVGV----LSGG 449
|
170 180
....*....|....*....|....*...
gi 47058990 613 EKQRVAIARAILKDPPVILYDEATSSLD 640
Cdd:PRK11819 450 ERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
328-411 |
1.42e-04 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 44.40 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 328 DAGNAAIDSLLNYETVKYFNNEKYEAQRYDGFLKTYETASLKSTSTLAMLNFgqSAIFSV--GLTAIMVLASQGIVAGAL 405
Cdd:cd18575 173 DLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTA--LVIFLVfgAIVFVLWLGAHDVLAGRM 250
|
....*.
gi 47058990 406 TVGDLV 411
Cdd:cd18575 251 SAGELS 256
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
457-682 |
2.18e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.84 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 457 KAMASPLqiTPqtATVAFDNVHF-----EYIEGQKV-------LSGVSFEVPAGKKVAIVGGSGSGKSTIVRLLfrfyEP 524
Cdd:PLN03140 857 RGMVLPF--TP--LAMSFDDVNYfvdmpAEMKEQGVtedrlqlLREVTGAFRPGVLTALMGVSGAGKTTLMDVL----AG 928
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 525 QKGSIYLAGqniqDVSL-------ESLRRAVGVVPQDAVlfHN---TIYYNLLYGNINASPEEVYAVAK----------- 583
Cdd:PLN03140 929 RKTGGYIEG----DIRIsgfpkkqETFARISGYCEQNDI--HSpqvTVRESLIYSAFLRLPKEVSKEEKmmfvdevmelv 1002
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 584 -LAGLHDAILRMPhgydtqvGERGlkLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKH-RTSI 661
Cdd:PLN03140 1003 eLDNLKDAIVGLP-------GVTG--LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTgRTVV 1073
|
250 260
....*....|....*....|...
gi 47058990 662 FIAHRLST-VVDA-DEIIVLSQG 682
Cdd:PLN03140 1074 CTIHQPSIdIFEAfDELLLMKRG 1096
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
503-640 |
2.34e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.94 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 503 IVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSleslrravgvVPQDAVLFHN-------TIYYNL-LYGNINAS 574
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA----------KPYCTYIGHNlglklemTVFENLkFWSEIYNS 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47058990 575 PEEVYAVAKLAGLHDAIlrmphgydtqvGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLD 640
Cdd:PRK13541 101 AETLYAAIHYFKLHDLL-----------DEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
603-692 |
2.63e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.96 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 603 GERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIF-----------IAHRLsTVV 671
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLlttqymeeaeqLAHEL-TVI 217
|
90 100
....*....|....*....|.
gi 47058990 672 DADEIIvlSQGKVAERGTHYG 692
Cdd:NF000106 218 DRGRVI--ADGKVDELKTKVG 236
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
599-688 |
2.88e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.45 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 599 DTQVGERGLK-LSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDVVKHRTSIFIAHRLSTVVDA---- 673
Cdd:PLN03140 326 DTIVGDEMIRgISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQPAPETfdlf 405
|
90
....*....|....*
gi 47058990 674 DEIIVLSQGKVAERG 688
Cdd:PLN03140 406 DDIILLSEGQIVYQG 420
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
152-411 |
3.12e-04 |
|
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: 43.59 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 152 AMNIVVPFMFKYAVDSLNQmSGNMlnlsdapNTVATMATAVLIGYGVsRAGAAFFNEVRNAVFGKVAQNSIRRiakNVFL 231
Cdd:cd18549 16 ALDLVFPLIVRYIIDDLLP-SKNL-------RLILIIGAILLALYIL-RTLLNYFVTYWGHVMGARIETDMRR---DLFE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 232 HLHNLDLGFHLSRQTGALSkaidrgTRGIS--FVLSALVF---NLLPIVFEMTLVSSVLYYKCGAQFALVTLGTLGAYTA 306
Cdd:cd18549 84 HLQKLSFSFFDNNKTGQLM------SRITNdlFDISELAHhgpEDLFISIITIIGSFIILLTINVPLTLIVFALLPLMII 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 307 FTVAVT-RWRTRFRieMNKADNDAGNAAI-DSLLNYETVKYFNNEKYEAQRYDGFLKTYETAslKSTSTLAMLNFGQSAI 384
Cdd:cd18549 158 FTIYFNkKMKKAFR--RVREKIGEINAQLeDSLSGIRVVKAFANEEYEIEKFDEGNDRFLES--KKKAYKAMAYFFSGMN 233
|
250 260
....*....|....*....|....*....
gi 47058990 385 FSVGLTAIMVLASQG--IVAGALTVGDLV 411
Cdd:cd18549 234 FFTNLLNLVVLVAGGyfIIKGEITLGDLV 262
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
152-433 |
3.23e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 43.27 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 152 AMNIVVPFMFKYAVDSLNqMSGNMLNLsdapNTVATMATAVLIGYGVsragaafFNEVRNAVFGKVaQNSI-RRIAKNVF 230
Cdd:cd18555 16 LLTLLIPILTQYVIDNVI-VPGNLNLL----NVLGIGILILFLLYGL-------FSFLRGYIIIKL-QTKLdKSLMSDFF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 231 LHLHNLDLGFHLSRQTGAL-----SKAIDRG---TRGISFVLSALvfnLLPIVFEMTLVSSVLYykcgaqfALVTLgTLG 302
Cdd:cd18555 83 EHLLKLPYSFFENRSSGDLlfranSNVYIRQilsNQVISLIIDLL---LLVIYLIYMLYYSPLL-------TLIVL-LLG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 303 AYTAFTVAVTRWRTRFRIEMNKADN-DAGNAAIDSLLNYETVKYFNNEKyeaQRYDGFLKTYET---ASLKSTSTLAMLN 378
Cdd:cd18555 152 LLIVLLLLLTRKKIKKLNQEEIVAQtKVQSYLTETLYGIETIKSLGSEK---NIYKKWENLFKKqlkAFKKKERLSNILN 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 47058990 379 FGQSAIFSVGLTAIMVLASQGIVAGALTVGDLVMVNGLLFQLSLPLNFLGTVYRE 433
Cdd:cd18555 229 SISSSIQFIAPLLILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQ 283
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
259-431 |
4.00e-04 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 43.07 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 259 GISFVLSALVFNLLPIVFemtLVSSVL--YYKcgaqfalvtlgtlgaytaftvavtrwrtRFRIEMNKADNDAGNAAIDS 336
Cdd:cd18784 133 KLSWQLSLVTLIGLPLIA---IVSKVYgdYYK----------------------------KLSKAVQDSLAKANEVAEET 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 337 LLNYETVKYFNNEKYEAQRYDGFLKtyETASLKSTSTLAMLNF-GQSAIFSVGLTAIMvLASQG--IVAGALTVGDLVMV 413
Cdd:cd18784 182 ISSIRTVRSFANEDGEANRYSEKLK--DTYKLKIKEALAYGGYvWSNELTELALTVST-LYYGGhlVITGQISGGNLISF 258
|
170 180
....*....|....*....|
gi 47058990 414 ngLLFQLSL--PLNFLGTVY 431
Cdd:cd18784 259 --ILYQLELgsCLESVGSVY 276
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
609-684 |
6.80e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.02 E-value: 6.80e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47058990 609 LSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMRDvvkHRTSI-FIAHRLSTVVD-ADEIIVLSQGKV 684
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKT---FQGSIiFISHDRSFIRNmATRIVDLDRGKL 231
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
194-431 |
5.59e-03 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 39.63 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 194 IGY-GVSRAGAAFFNEVRNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLsALVFNll 272
Cdd:cd18590 39 IGLmCLFSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSV-ALNAN-- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 273 piVFEMTLVSSVLYYkcGAQFAL---VTLGTLGAYTAFTVAVTRWRTRFR---IEMNKADNDAGNAAIDSLLNYETVKYF 346
Cdd:cd18590 116 --VLLRSLVKTLGML--GFMLSLswqLTLLTLIEMPLTAIAQKVYNTYHQklsQAVQDSIAKAGELAREAVSSIRTVRSF 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 347 NNEKYEAQRYDGFLK-TYETASLKSTSTLAMLNFGQsaIFSVGLTAIMV-LASQGIVAGALTVGDLVMVngLLFQLSLPL 424
Cdd:cd18590 192 KAEEEEACRYSEALErTYNLKDRRDTVRAVYLLVRR--VLQLGVQVLMLyCGRQLIQSGHLTTGSLVSF--ILYQKNLGS 267
|
....*..
gi 47058990 425 NFLGTVY 431
Cdd:cd18590 268 YVRTLVY 274
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
608-703 |
7.58e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 39.40 E-value: 7.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 608 KLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETI--LGAMRDVVKHRTSIFIAHRLSTVVD-ADEIIVLSQGKV 684
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIfrLLTRLNQNNNTTILLISHDLQMLSQwADKINVLYCGQT 237
|
90
....*....|....*....
gi 47058990 685 AERGTHYGLLANSSSIYSE 703
Cdd:PRK15093 238 VETAPSKELVTTPHHPYTQ 256
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
189-421 |
8.69e-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: 38.73 E-value: 8.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 189 ATAVLIGYGVSRAGAAFFNEV----RNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAID-----RG--- 256
Cdd:cd18782 37 DLATLYVIGVVMLVAALLEAVltalRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRISeldtiRGflt 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 257 TRGISFVLSAlVFNLLPIVFeMTLVSSVLyykcgaqfALVTLGTL---GAYTAFTVAVTRWRTRFRIEMNKADNdagNAA 333
Cdd:cd18782 117 GTALTTLLDV-LFSVIYIAV-LFSYSPLL--------TLVVLATVplqLLLTFLFGPILRRQIRRRAEASAKTQ---SYL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 334 IDSLLNYETVKYFNNEKYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGALTVGDLV-- 411
Cdd:cd18782 184 VESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLLVLWVGAYLVLRGELTLGQLIaf 263
|
250
....*....|....*
gi 47058990 412 -----MVNGLLFQLS 421
Cdd:cd18782 264 rilsgYVTGPILRLS 278
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
571-640 |
9.26e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.46 E-value: 9.26e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47058990 571 INASPEEVYAVAKLAGLhdailrmphGYDTQVGERGLK-LSGGEKQRVAIARAILKDPPVILYDEATSSLD 640
Cdd:PLN03073 315 IDAYTAEARAASILAGL---------SFTPEMQVKATKtFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
583-679 |
9.71e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 38.75 E-value: 9.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47058990 583 KLAGLHDAILrmphGYdTQVGERGLKLSGGEKQRVAIARAILK-DPPVILY--DEATSSLDSITEETILGAMRDVV-KHR 658
Cdd:cd03271 149 KLQTLCDVGL----GY-IKLGQPATTLSGGEAQRIKLAKELSKrSTGKTLYilDEPTTGLHFHDVKKLLEVLQRLVdKGN 223
|
90 100
....*....|....*....|.
gi 47058990 659 TSIFIAHRLSTVVDADEIIVL 679
Cdd:cd03271 224 TVVVIEHNLDVIKCADWIIDL 244
|
|
| |
