|
Name |
Accession |
Description |
Interval |
E-value |
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
222-821 |
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: 821.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 222 GSAFRNGWRKLRTVFPYLWPKKNIALQIAVIVCIILLLAGRVIKLFLPIYRKKLVDSLTIAPivfrWDFVLIYVALSFLQ 301
Cdd:COG5265 9 APAAPPRLDLLLRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGA----AALLVVPVGLLLAY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 302 GGGTGSMGLFNNLRTFLWIRVQQYTTREIEIELFRHLHQLSLRWHLQRKTGEVLRVMDRGTDSINNLLNYIVFSIAPTIL 381
Cdd:COG5265 85 GLLRLLSVLFGELRDALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGGLSRDIERGTKGIEFLLRFLLFNILPTLL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 382 DLLVAVAYFVYAFNWWFGLIVFLTMFLYIASTIAITEWRTKYQRRMNLADNEQRARSVDSLLNFETVKYYGAEHYEVDCY 461
Cdd:COG5265 165 EIALVAGILLVKYDWWFALITLVTVVLYIAFTVVVTEWRTKFRREMNEADSEANTRAVDSLLNYETVKYFGNEAREARRY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 462 REAILKYQKEEFLSMLTLNMLNTAQNIILCLGLLAGSLLCVYLVVHHqTLTVGDFVLFSTYLMELYMPLNWFGTYYRAIQ 541
Cdd:COG5265 245 DEALARYERAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAG-TMTVGDFVLVNAYLIQLYIPLNFLGFVYREIR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 542 KNFVDMENMFDLLKEEEEIVDAPGCSPLLTAGGGIEFSNVTFGYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRL 621
Cdd:COG5265 324 QALADMERMFDLLDQPPEVADAPDAPPLVVGGGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 622 LFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGVVPQDTVLFNNTIFYNIEYAKLGASDEAVYEAARAADIHERILGFPEK 701
Cdd:COG5265 404 LFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDG 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 702 YETKVGERGLRLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVAHRLSTIIHADEIL 781
Cdd:COG5265 484 YDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEIL 563
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 19527665 782 VLQQGSIAERGRHEELvLREDGIYADMWQQQLKNLDAEQS 821
Cdd:COG5265 564 VLEAGRIVERGTHAEL-LAQGGLYAQMWARQQEEEEAEEA 602
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
226-815 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 563.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 226 RNGWRKLRTVFPYLWPKKnialqIAVIVCIILLLAGRVIKLFLPIYRKKLVDSLtIAPIVFR--WDFVLIYVALSFLQGg 303
Cdd:COG1132 3 KSPRKLLRRLLRYLRPYR-----GLLILALLLLLLSALLELLLPLLLGRIIDAL-LAGGDLSalLLLLLLLLGLALLRA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 304 gtgsmgLFNNLRTFLWIRVQQYTTREIEIELFRHLHQLSLRWHLQRKTGEVLRVMDRGTDSINNLLNYIVFSIAPTILDL 383
Cdd:COG1132 76 ------LLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 384 LVAVAYFVYaFNWWFGLIVFLTMFLYIASTIAITEWRTKYQRRMNLADNEQRARSVDSLLNFETVKYYGAEHYEVDCYRE 463
Cdd:COG1132 150 IGALVVLFV-IDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFRE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 464 AILKYQKEEFLSMLTLNMLNTAQNIILCLGLLAGSLLCVYLVVHHQtLTVGDFVLFSTYLMELYMPLNWFGTYYRAIQKN 543
Cdd:COG1132 229 ANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGS-LTVGDLVAFILYLLRLFGPLRQLANVLNQLQRA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 544 FVDMENMFDLLKEEEEIVDAPGCSPLLTAGGGIEFSNVTFGYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLF 623
Cdd:COG1132 308 LASAERIFELLDEPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 624 RFYDVQTGAILIDGQNIKLVQQQSLRKAIGVVPQDTVLFNNTIFYNIEYAKLGASDEAVYEAARAADIHERILGFPEKYE 703
Cdd:COG1132 388 RFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYD 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 704 TKVGERGLRLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVAHRLSTIIHADEILVL 783
Cdd:COG1132 468 TVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVL 547
|
570 580 590
....*....|....*....|....*....|..
gi 19527665 784 QQGSIAERGRHEELvLREDGIYADMWQQQLKN 815
Cdd:COG1132 548 DDGRIVEQGTHEEL-LARGGLYARLYRLQFGE 578
|
|
| ABC_6TM_ABCB6 |
cd18581 |
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, ... |
254-550 |
0e+00 |
|
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: 541.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 254 CIILLLAGRVIKLFLPIYRKKLVDSLT----IAPIVFRWDFVLIYVALSFLQGGGTGSMGLFNNLRTFLWIRVQQYTTRE 329
Cdd:cd18581 1 CLLLLAAGRVVNVLVPILYKKIVDSLTpdsaDSPLAFPWALILLYVFLKFLQGGGSGSVGLLSNLRSFLWIPVQQFTTRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 330 IEIELFRHLHQLSLRWHLQRKTGEVLRVMDRGTDSINNLLNYIVFSIAPTILDLLVAVAYFVYAFNWWFGLIVFLTMFLY 409
Cdd:cd18581 81 ISVKLFAHLHSLSLRWHLSRKTGEVLRVMDRGTSSINSLLSYVLFNIGPTIADIIIAIIYFAIAFNPWFGLIVFVTMALY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 410 IASTIAITEWRTKYQRRMNLADNEQRARSVDSLLNFETVKYYGAEHYEVDCYREAILKYQKEEFLSMLTLNMLNTAQNII 489
Cdd:cd18581 161 LILTIIITEWRTKFRREMNKLDNEKRAKAVDSLLNFETVKYYNAERFEVERYRRAIDDYQVAEWKSNASLNLLNTAQNLI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19527665 490 LCLGLLAGSLLCVYLVVHHqTLTVGDFVLFSTYLMELYMPLNWFGTYYRAIQKNFVDMENM 550
Cdd:cd18581 241 ITIGLLAGSLLCAYFVVEG-KLTVGDFVLFLTYIIQLYAPLNFFGTYYRMIQQSFIDMENM 300
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
576-812 |
6.52e-161 |
|
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: 468.25 E-value: 6.52e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGVV 655
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 656 PQDTVLFNNTIFYNIEYAKLGASDEAVYEAARAADIHERILGFPEKYETKVGERGLRLSGGEKQRVAIARTLLKAPIIVL 735
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19527665 736 LDEATSALDTHTERNIQAALARVCANRTTIIVAHRLSTIIHADEILVLQQGSIAERGRHEELvLREDGIYADMWQQQ 812
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEEL-LAKGGLYAEMWKAQ 236
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
230-813 |
2.16e-144 |
|
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: 443.51 E-value: 2.16e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 230 RKLRTVFPYLWPKKNIALQIAVIVCIILLLAgrvikLFLPIYRKKLVDSltiapIVFRWDFVLIYVaLSFLQGGGTGSMG 309
Cdd:COG2274 142 FGLRWFLRLLRRYRRLLLQVLLASLLINLLA-----LATPLFTQVVIDR-----VLPNQDLSTLWV-LAIGLLLALLFEG 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 310 LFNNLRTFLWIRVQQYTTREIEIELFRHLHQLSLRWHLQRKTGEVL-RVMDrgTDSINNLLNYIVFSiapTILDLLVAVA 388
Cdd:COG2274 211 LLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLAsRFRD--VESIREFLTGSLLT---ALLDLLFVLI 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 389 YFV--YAFNWWFGLIVFLTMFLYIASTIAITEWRTKYQRRMNLADNEQRARSVDSLLNFETVKYYGAEHYEVDCYREAIL 466
Cdd:COG2274 286 FLIvlFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 467 KYQKEEFLSMLTLNMLNTAQNIILCLGLLAGSLLCVYLVVHHQtLTVGDFVLFSTYLMELYMPLNWFGTYYRAIQKNFVD 546
Cdd:COG2274 366 KYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQ-LTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIA 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 547 MENMFDLLKEEEEIVDAPGCSPLLTAGGGIEFSNVTFGYSP-EKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRF 625
Cdd:COG2274 445 LERLDDILDLPPEREEGRSKLSLPRLKGDIELENVSFRYPGdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGL 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 626 YDVQTGAILIDGQNIKLVQQQSLRKAIGVVPQDTVLFNNTIFYNIEYAKLGASDEAVYEAARAADIHERILGFPEKYETK 705
Cdd:COG2274 525 YEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTV 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 706 VGERGLRLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVAHRLSTIIHADEILVLQQ 785
Cdd:COG2274 605 VGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDK 684
|
570 580
....*....|....*....|....*...
gi 19527665 786 GSIAERGRHEELvLREDGIYADMWQQQL 813
Cdd:COG2274 685 GRIVEDGTHEEL-LARKGLYAELVQQQL 711
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
576-809 |
6.33e-114 |
|
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: 346.91 E-value: 6.33e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSPEKI-VLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGV 654
Cdd:cd03251 1 VEFKNVTFRYPGDGPpVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 655 VPQDTVLFNNTIFYNIEYAKLGASDEAVYEAARAADIHERILGFPEKYETKVGERGLRLSGGEKQRVAIARTLLKAPIIV 734
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19527665 735 LLDEATSALDTHTERNIQAALARVCANRTTIIVAHRLSTIIHADEILVLQQGSIAERGRHEELvLREDGIYADMW 809
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEEL-LAQGGVYAKLH 234
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
254-550 |
1.43e-113 |
|
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: 348.44 E-value: 1.43e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 254 CIILLLAGRVIKLFLPIYRKKLVDSLTIAPivfRWDF------VLIYVALSFlqgggtgSMGLFNNLRTFLWIRVQQYTT 327
Cdd:cd18560 1 SLLLLILGKACNVLAPLFLGRAVNALTLAK---VKDLesavtlILLYALLRF-------SSKLLKELRSLLYRRVQQNAY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 328 REIEIELFRHLHQLSLRWHLQRKTGEVLRVMDRGTDSINNLLNYIVFSIAPTILDLLVAVAYFVYAFNWWFGLIVFLTMF 407
Cdd:cd18560 71 RELSLKTFAHLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLELIVVSVVFAFHFGAWLALIVFLSVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 408 LYIASTIAITEWRTKYQRRMNLADNEQRARSVDSLLNFETVKYYGAEHYEVDCYREAILKYQKEEFLSMLTLNMLNTAQN 487
Cdd:cd18560 151 LYGVFTIKVTEWRTKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQ 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19527665 488 IILCLGLLAGSLLCVYLVVHHQtLTVGDFVLFSTYLMELYMPLNWFGTYYRAIQKNFVDMENM 550
Cdd:cd18560 231 LIIQLGLTLGLLLAGYRVVDGG-LSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSLTDMENL 292
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
254-550 |
1.58e-111 |
|
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: 342.97 E-value: 1.58e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 254 CIILLLAGRVIKLFLPIYRKKLVDSLTIAPIVFRWDFVLIYVALSFLQgggtgSMGLFNNLRTFLWIRVQQYTTREIEIE 333
Cdd:cd18583 1 CFLCLLAERVLNVLVPRQLGIIVDSLSGGSGKSPWKEIGLYVLLRFLQ-----SGGGLGLLRSWLWIPVEQYSYRALSTA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 334 LFRHLHQLSLRWHLQRKTGEVLRVMDRGTdSINNLLNYIVFSIAPTILDLLVAVAYFVYAFNWWFGLIVFLTMFLYIAST 413
Cdd:cd18583 76 AFNHVMNLSMDFHDSKKSGEVLKAIEQGS-SINDLLEQILFQIVPMIIDLVIAIVYLYYLFDPYMGLIVAVVMVLYVWST 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 414 IAITEWRTKYQRRMNLADNEQRARSVDSLLNFETVKYYGAEHYEVDCYREAILKYQKEEFLSMLTLNMLNTAQNIILCLG 493
Cdd:cd18583 155 IKLTSWRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYREAVKNYQKAERKYLFSLNLLNAVQSLILTLG 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 19527665 494 LLAGSLLCVYLVVHHQtLTVGDFVLFSTYLMELYMPLNWFGTYYRAIQKNFVDMENM 550
Cdd:cd18583 235 LLAGCFLAAYQVSQGQ-ATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDLIDAERL 290
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
576-812 |
1.59e-111 |
|
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: 341.06 E-value: 1.59e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGY--SPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIG 653
Cdd:cd03249 1 IEFKNVSFRYpsRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 654 VVPQDTVLFNNTIFYNIEYAKLGASDEAVYEAARAADIHERILGFPEKYETKVGERGLRLSGGEKQRVAIARTLLKAPII 733
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19527665 734 VLLDEATSALDTHTERNIQAALARVCANRTTIIVAHRLSTIIHADEILVLQQGSIAERGRHEELvLREDGIYADMWQQQ 812
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDEL-MAQKGVYAKLVKAQ 238
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
333-803 |
1.53e-105 |
|
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: 337.12 E-value: 1.53e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 333 ELFRHLHQLSLRWHLQRKTGEVLRVMdrgTDSINNLLNYIVFSIAPTILDLLVAVAYFVYAF--NWWFGLIVFLTMFLYI 410
Cdd:COG4988 96 RLLEKLLALGPAWLRGKSTGELATLL---TEGVEALDGYFARYLPQLFLAALVPLLILVAVFplDWLSGLILLVTAPLIP 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 411 AStIAITEWRTK------YQRRMNLAdneqrARSVDSLLNFETVKYYGAEHYEV-------DCYREA---ILKYQkeeFL 474
Cdd:COG4988 173 LF-MILVGKGAAkasrrqWRALARLS-----GHFLDRLRGLTTLKLFGRAKAEAeriaeasEDFRKRtmkVLRVA---FL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 475 SMLTLNMLNT------AqnIILCLGLLAGSLlcvylvvhhqTLTVGDFVLFstyL-MELYMPLNWFGTYYRAIQKNFVDM 547
Cdd:COG4988 244 SSAVLEFFASlsialvA--VYIGFRLLGGSL----------TLFAALFVLL---LaPEFFLPLRDLGSFYHARANGIAAA 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 548 ENMFDLLKEEEEIVDAPGCSPLLTAGGGIEFSNVTFGYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYD 627
Cdd:COG4988 309 EKIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 628 VQTGAILIDGQNIKLVQQQSLRKAIGVVPQDTVLFNNTIFYNIEYAKLGASDEAVYEAARAADIHERILGFPEKYETKVG 707
Cdd:COG4988 389 PYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLG 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 708 ERGLRLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVAHRLSTIIHADEILVLQQGS 787
Cdd:COG4988 469 EGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGR 548
|
490
....*....|....*.
gi 19527665 788 IAERGRHEELvLREDG 803
Cdd:COG4988 549 IVEQGTHEEL-LAKNG 563
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
254-550 |
5.34e-104 |
|
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: 323.30 E-value: 5.34e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 254 CIILLLAGRVIKLFLPIYRKKLVDSLTIAPIVFRWDFVLIYVALSFLQGGGTgsmgLFNNLRTFLWIRVQQYTTREIEIE 333
Cdd:cd18582 1 ALLLLVLAKLLNVAVPFLLKYAVDALSAPASALLAVPLLLLLAYGLARILSS----LFNELRDALFARVSQRAVRRLALR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 334 LFRHLHQLSLRWHLQRKTGEVLRVMDRGTDSINNLLNYIVFSIAPTILDLLVAVAYFVYAFNWWFGLIVFLTMFLYIAST 413
Cdd:cd18582 77 VFRHLHSLSLRFHLSRKTGALSRAIERGTRGIEFLLRFLLFNILPTILELLLVCGILWYLYGWSYALITLVTVALYVAFT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 414 IAITEWRTKYQRRMNLADNEQRARSVDSLLNFETVKYYGAEHYEVDCYREAILKYQKEEFLSMLTLNMLNTAQNIILCLG 493
Cdd:cd18582 157 IKVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQALIISLG 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 19527665 494 LLAGSLLCVYLVVHHqTLTVGDFVLFSTYLMELYMPLNWFGTYYRAIQKNFVDMENM 550
Cdd:cd18582 237 LTAIMLLAAQGVVAG-TLTVGDFVLVNTYLLQLYQPLNFLGFVYREIRQSLIDMEKL 292
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
223-800 |
1.34e-103 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 332.70 E-value: 1.34e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 223 SAFRNGWRKLRtvfpYLWPKKNIALQIAVIVciiLLLAgrVIKLFLPIYRKKLVDSLT----IAPIVFRWdfvliyVALs 298
Cdd:PRK13657 2 SLFRLYARVLQ----YLGAEKRLGILLAVAN---VLLA--AATFAEPILFGRIIDAISgkgdIFPLLAAW------AGF- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 299 flqgggtgsmGLFNNLrTFLWI-----RVQQYTTREIEIELFRHLHQLSLRWHLQRKTGEVLRVMDRGTDSINNL-LNYI 372
Cdd:PRK13657 66 ----------GLFNII-AGVLVarhadRLAHRRRLAVLTEYFERIIQLPLAWHSQRGSGRALHTLLRGTDALFGLwLEFM 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 373 VFSIAPTI-LDLLVAVAYFVyafNWWFGLIVFLTMFLYIASTIAITEwRTKY-QRRMNLADNEQRARSVDSLLNFETVKY 450
Cdd:PRK13657 135 REHLATLVaLVVLLPLALFM---NWRLSLVLVVLGIVYTLITTLVMR-KTKDgQAAVEEHYHDLFAHVSDAIGNVSVVQS 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 451 YGAEHYEVDCYREAILKYQKEEF--LSMLTL-NMLNTAQNIILCLGLLagsLLCVYLVVHHQtLTVGD---FVLFSTYLm 524
Cdd:PRK13657 211 YNRIEAETQALRDIADNLLAAQMpvLSWWALaSVLNRAASTITMLAIL---VLGAALVQKGQ-LRVGEvvaFVGFATLL- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 525 elymplnwfgtyyraIQK-----NFVD--------MENMFDLLKEEEEIVDAPGCSPLLTAGGGIEFSNVTFGYSPEKIV 591
Cdd:PRK13657 286 ---------------IGRldqvvAFINqvfmaapkLEEFFEVEDAVPDVRDPPGAIDLGRVKGAVEFDDVSFSYDNSRQG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 592 LRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGVVPQDTVLFNNTIFYNIE 671
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIR 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 672 YAKLGASDEAVYEAARAADIHERILGFPEKYETKVGERGLRLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNI 751
Cdd:PRK13657 431 VGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKV 510
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 19527665 752 QAALARVCANRTTIIVAHRLSTIIHADEILVLQQGSIAERGRHEELVLR 800
Cdd:PRK13657 511 KAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVAR 559
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
230-814 |
2.68e-102 |
|
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: 328.98 E-value: 2.68e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 230 RKLRTVFPYLWpkknialqiAVIVCIILLLAGRVIKLFLPIYRKKLVD---SLTIAPIVfrWDFVLIYVALSFLQGggtg 306
Cdd:TIGR02203 4 RLWSYVRPYKA---------GLVLAGVAMILVAATESTLAALLKPLLDdgfGGRDRSVL--WWVPLVVIGLAVLRG---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 307 smgLFNNLRTFLWIRVQQYTTREIEIELFRHLHQLSLRWHLQRKTGEVLrvmDRGTDSINNLLNYIVFSIAPTILDLLVA 386
Cdd:TIGR02203 69 ---ICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLL---SRITFDSEQVASAATDAFIVLVRETLTV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 387 VAYFVYAF--NWWFGLIVFLtMFLYIASTIAITEWRTKYQRRMNLADNEQRARSVDSLL-NFETVKYYGAEHYEVDCYRE 463
Cdd:TIGR02203 143 IGLFIVLLyySWQLTLIVVV-MLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLqGYRVVKLFGGQAYETRRFDA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 464 A---ILKYQKEeflsMLTLNMLNTAqnIILCLGLLAgsLLCVYLVVHHQ----TLTVGDFVLFSTYLMELYMPLNWFGTY 536
Cdd:TIGR02203 222 VsnrNRRLAMK----MTSAGSISSP--ITQLIASLA--LAVVLFIALFQaqagSLTAGDFTAFITAMIALIRPLKSLTNV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 537 YRAIQKNFVDMENMFDLLKEEEEiVDApGCSPLLTAGGGIEFSNVTFGYSPEKI-VLRNVSFTVPAGKTVAIVGPSGAGK 615
Cdd:TIGR02203 294 NAPMQRGLAAAESLFTLLDSPPE-KDT-GTRAIERARGDVEFRNVTFRYPGRDRpALDSISLVIEPGETVALVGRSGSGK 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 616 STIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGVVPQDTVLFNNTIFYNIEYAKLG-ASDEAVYEAARAADIHER 694
Cdd:TIGR02203 372 STLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEqADRAEIERALAAAYAQDF 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 695 ILGFPEKYETKVGERGLRLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVAHRLSTI 774
Cdd:TIGR02203 452 VDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTI 531
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 19527665 775 IHADEILVLQQGSIAERGRHEELvLREDGIYADMWQQQLK 814
Cdd:TIGR02203 532 EKADRIVVMDDGRIVERGTHNEL-LARNGLYAQLHNMQFR 570
|
|
| MTABC_N |
pfam16185 |
Mitochondrial ABC-transporter N-terminal five TM region; MTABC_N is the N-terminal five ... |
3-241 |
2.65e-101 |
|
Mitochondrial ABC-transporter N-terminal five TM region; MTABC_N is the N-terminal five transmembrane helices of eukaryotic mitochondrial ABC-transporters.
Pssm-ID: 465049 Cd Length: 244 Bit Score: 314.60 E-value: 2.65e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 3 YCPPNVTLSEVWTQHGISHCFMDTVGPAVYGGFLLLFGSIQLLMYRKYATRItDPTQISKSRLFAMQLFLLLLLPVLALL 82
Cdd:pfam16185 2 YCEPNVSLTPVWVDHGLSPCFYDTLVPSVLLGFLLLFGTIQLIMYRKYGTPM-EPKFIPRSRLYVLQLFLALLLPLLALA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 83 RFLMNARIYPDSAVYGYMIFSTCVVCFSYPFSICLILKERYYQLPSMPTRGHGLVLLLFWTLAFINESLAFINLRHEDWW 162
Cdd:pfam16185 81 RFILRAALIGGGRLYGYMVLYACLSLLAWPFSLALLRLERRYALPSLPTRGHGLVLLLFWTLAFVAENLAFVSWNSPDWW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 163 FHLKTNKDQIEMGLFVTRFLCSLLIFVLGLKAPGIMA-PY----NPHQRLDNDTANESQGNVQTGSAFRNGWRKLRTVFP 237
Cdd:pfam16185 161 WGLETLSDQVEFGLFVVRYVCTLLLFVLGLKAPGLPRkPYmlliNEDERDVESSQPLLGDSEENGSTWRNFGKKLRLLWP 240
|
....
gi 19527665 238 YLWP 241
Cdd:pfam16185 241 YLWP 244
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
334-811 |
2.50e-100 |
|
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: 323.64 E-value: 2.50e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 334 LFRHLHQLSLRWHLQRKTGEVLrvmDRGTDSINNLLNYIVFSIAPTILDLLV--AVAYFVYAFNWWFGLIVFLTMFLYIA 411
Cdd:COG4987 94 LYRRLEPLAPAGLARLRSGDLL---NRLVADVDALDNLYLRVLLPLLVALLVilAAVAFLAFFSPALALVLALGLLLAGL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 412 STIAITEWRTK-YQRRMNLADNEQRARSVDSLLNFETVKYYGAEHYEVDCYREAILKYQKEEfLSMLTLNMLNTAQNIIL 490
Cdd:COG4987 171 LLPLLAARLGRrAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQ-RRLARLSALAQALLQLA 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 491 CLGLLAGSL-LCVYLVVHHQ---TLTVGdFVLFSTYLMELYMPL-----NWfGTYYRAIqknfvdmENMFDLLKEEEEIV 561
Cdd:COG4987 250 AGLAVVAVLwLAAPLVAAGAlsgPLLAL-LVLAALALFEALAPLpaaaqHL-GRVRAAA-------RRLNELLDAPPAVT 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 562 DaPGCSPLLTAGGGIEFSNVTFGYSPE-KIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNI 640
Cdd:COG4987 321 E-PAEPAPAPGGPSLELEDVSFRYPGAgRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDL 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 641 KLVQQQSLRKAIGVVPQDTVLFNNTIFYNIEYAKLGASDEAVYEAARAADIHERILGFPEKYETKVGERGLRLSGGEKQR 720
Cdd:COG4987 400 RDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRR 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 721 VAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVAHRLSTIIHADEILVLQQGSIAERGRHEELvLR 800
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEEL-LA 558
|
490
....*....|.
gi 19527665 801 EDGIYADMWQQ 811
Cdd:COG4987 559 QNGRYRQLYQR 569
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
574-800 |
1.30e-98 |
|
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: 306.84 E-value: 1.30e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 574 GGIEFSNVTFGYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIG 653
Cdd:cd03254 1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 654 VVPQDTVLFNNTIFYNIEYAKLGASDEAVYEAARAADIHERILGFPEKYETKVGERGLRLSGGEKQRVAIARTLLKAPII 733
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19527665 734 VLLDEATSALDTHTERNIQAALARVCANRTTIIVAHRLSTIIHADEILVLQQGSIAERGRHEELVLR 800
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
230-813 |
4.06e-96 |
|
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: 312.79 E-value: 4.06e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 230 RKLRTVFPYLWPKKNIalqiaVIVCIILLLAGRVIKLFLPIYRKKLVD-SLTIAPIVFRWDFVLIYVALSFLQGGGTGsm 308
Cdd:TIGR02204 4 RPLAALWPFVRPYRGR-----VLAALVALLITAAATLSLPYAVRLMIDhGFSKDSSGLLNRYFAFLLVVALVLALGTA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 309 glfnnLRTFLWIRVQQYTTREIEIELFRHLHQLSLRWHLQRKTGEVLRVMDrgTDSinNLLNYIV---FSIA-PTILDLL 384
Cdd:TIGR02204 77 -----ARFYLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLT--TDT--TLLQSVIgssLSMAlRNALMCI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 385 VAVAYFVYAfNWWFGLIVFLTMFLYIASTIAITEWRTKYQRRMN--LADNEQRARsvDSLLNFETVKYYGAEHYEVDCYR 462
Cdd:TIGR02204 148 GGLIMMFIT-SPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQdrIADAGSYAG--ETLGAIRTVQAFGHEDAERSRFG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 463 EAILKYQKEEFLSMLTLNMLnTAQNIILCLGLLAGSLLCVYLVVHHQTLTVGDFVLFSTYLMELYMPLNWFGTYYRAIQK 542
Cdd:TIGR02204 225 GAVEKAYEAARQRIRTRALL-TAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 543 NFVDMENMFDLLKEEEEIvDAPGCSPLLTA--GGGIEFSNVTFGY--SPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTI 618
Cdd:TIGR02204 304 AAGAAERLIELLQAEPDI-KAPAHPKTLPVplRGEIEFEQVNFAYpaRPDQPALDGLNLTVRPGETVALVGPSGAGKSTL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 619 MRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGVVPQDTVLFNNTIFYNIEYAKLGASDEAVYEAARAADIHERILGF 698
Cdd:TIGR02204 383 FQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISAL 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 699 PEKYETKVGERGLRLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVAHRLSTIIHAD 778
Cdd:TIGR02204 463 PEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKAD 542
|
570 580 590
....*....|....*....|....*....|....*
gi 19527665 779 EILVLQQGSIAERGRHEELVlREDGIYADMWQQQL 813
Cdd:TIGR02204 543 RIVVMDQGRIVAQGTHAELI-AKGGLYARLARLQF 576
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
509-813 |
1.17e-87 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 290.38 E-value: 1.17e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 509 QTLTVGDF-VLFSTyLMELYMPLNWFGTYYRAIQKNFVDMENMFDLLKEEEEIVDapGCSPLLTAGGGIEFSNVTFGY-S 586
Cdd:PRK11176 277 DTLTAGTItVVFSS-MIALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQEKDE--GKRVIERAKGDIEFRNVTFTYpG 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 587 PEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGVVPQDTVLFNNTI 666
Cdd:PRK11176 354 KEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTI 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 667 FYNIEYAKLGA-SDEAVYEAARAADIHERILGFPEKYETKVGERGLRLSGGEKQRVAIARTLLKAPIIVLLDEATSALDT 745
Cdd:PRK11176 434 ANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDT 513
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19527665 746 HTERNIQAALARVCANRTTIIVAHRLSTIIHADEILVLQQGSIAERGRHEELvLREDGIYADMWQQQL 813
Cdd:PRK11176 514 ESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAEL-LAQNGVYAQLHKMQF 580
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
576-812 |
2.11e-84 |
|
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: 269.74 E-value: 2.11e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSP-EKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGV 654
Cdd:cd03252 1 ITFEHVRFRYKPdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 655 VPQDTVLFNNTIFYNIEYAKLGASDEAVYEAARAADIHERILGFPEKYETKVGERGLRLSGGEKQRVAIARTLLKAPIIV 734
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19527665 735 LLDEATSALDTHTERNIQAALARVCANRTTIIVAHRLSTIIHADEILVLQQGSIAERGRHEELvLREDGIYADMWQQQ 812
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDEL-LAENGLYAYLYQLQ 237
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
333-806 |
1.65e-81 |
|
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: 273.69 E-value: 1.65e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 333 ELFRHLHQLSLRWHLQRKTGEVLRVMDRGTDSINNL-LNYIVFSIAPTI-LDLLVAVAYfvyAFNWWFGLIVFLTMFLYI 410
Cdd:TIGR01192 94 EAFGRIISMPLSWHQQRGTSNALHTLLRATETLFGLwLEFMRQHLATFVaLFLLIPTAF---AMDWRLSIVLMVLGILYI 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 411 AstiaITEW---RTKYQRrmnlADNEQRARSV-----DSLLNFETVKYYG---AEHYEVDCYREAILKYQKEEFLSMLTL 479
Cdd:TIGR01192 171 L----IAKLvmqRTKNGQ----AAVEHHYHNVfkhvsDSISNVSVVHSYNrieAETSALKQFTNNLLSAQYPVLDWWALA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 480 NMLN-TAQNIILCLGLLAGSLLcvylvVHHQTLTVGD---FVLFSTYLMELYMPLNWFGTYY---RAIQKNFVDMEnmfD 552
Cdd:TIGR01192 243 SGLNrMASTISMMCILVIGTVL-----VIKGELSVGEviaFIGFANLLIGRLDQMSGFITQIfeaRAKLEDFFDLE---D 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 553 LLKEEEEIVDAPgcsPLLTAGGGIEFSNVTFGYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGA 632
Cdd:TIGR01192 315 SVFQREEPADAP---ELPNVKGAVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQ 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 633 ILIDGQNIKLVQQQSLRKAIGVVPQDTVLFNNTIFYNIEYAKLGASDEAVYEAARAADIHERILGFPEKYETKVGERGLR 712
Cdd:TIGR01192 392 ILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNR 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 713 LSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVAHRLSTIIHADEILVLQQGSIAERG 792
Cdd:TIGR01192 472 LSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKG 551
|
490
....*....|....
gi 19527665 793 RHEELVLREDGIYA 806
Cdd:TIGR01192 552 SFQELIQKDGRFYK 565
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
222-808 |
3.64e-80 |
|
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: 273.36 E-value: 3.64e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 222 GSAFRNGWRKlRTVFPYLWPKKNiALQIAVIVCIILLLAGRVIKLFLPIYRKKLVDSLTIAPIVfRWDFVLIyvalsflq 301
Cdd:TIGR03796 129 GPEFQKGGRK-PSLLRALWRRLR-GSRGALLYLLLAGLLLVLPGLVIPAFSQIFVDEILVQGRQ-DWLRPLL-------- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 302 gggtGSMGLFNNLRTFL-WIrvQQYTTREIEIEL--------FRHLHQLSLRWHLQRKTGEVL-RVmdrgtDSINNLLNY 371
Cdd:TIGR03796 198 ----LGMGLTALLQGVLtWL--QLYYLRRLEIKLavgmsarfLWHILRLPVRFFAQRHAGDIAsRV-----QLNDQVAEF 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 372 IVFSIAPTILDLLVAVAYFV--YAFNWWFGLIVFLTMFLYIASTIAITEWRTKYQRRMNLADNEQRARSVDSLLNFETVK 449
Cdd:TIGR03796 267 LSGQLATTALDAVMLVFYALlmLLYDPVLTLIGIAFAAINVLALQLVSRRRVDANRRLQQDAGKLTGVAISGLQSIETLK 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 450 YYGAEHyevDCYREaILKYQKEEFLSMLTLNMLNTAQNII--LCLGLLAGSLLCV--YLVVHHQtLTVGDFVLFSTYLME 525
Cdd:TIGR03796 347 ASGLES---DFFSR-WAGYQAKLLNAQQELGVLTQILGVLptLLTSLNSALILVVggLRVMEGQ-LTIGMLVAFQSLMSS 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 526 LYMPLNWFGTYYRAIQKNFVDMENMFDLLK------EEEEIVDAPGCSPLLTAGGGIEFSNVTFGYSP-EKIVLRNVSFT 598
Cdd:TIGR03796 422 FLEPVNNLVGFGGTLQELEGDLNRLDDVLRnpvdplLEEPEGSAATSEPPRRLSGYVELRNITFGYSPlEPPLIENFSLT 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 599 VPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGVVPQDTVLFNNTIFYNIEYAKLGAS 678
Cdd:TIGR03796 502 LQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIP 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 679 DEAVYEAARAADIHERILGFPEKYETKVGERGLRLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALA-R 757
Cdd:TIGR03796 582 DADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRrR 661
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 19527665 758 VCanrTTIIVAHRLSTIIHADEILVLQQGSIAERGRHEELVLREdGIYADM 808
Cdd:TIGR03796 662 GC---TCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVG-GAYARL 708
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
326-783 |
5.07e-79 |
|
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: 265.30 E-value: 5.07e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 326 TTREIEIELFRHLHQLSLRWHLQRKTGEVLRVMDRGTDSINNLLN-YIVFSIAPTILDLLVAVAyfVYAFNWWFGLIVFL 404
Cdd:TIGR02857 75 VKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFArYLPQLVLAVIVPLAILAA--VFPQDWISGLILLL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 405 TMFLyIASTIAITEWRTKYQRRMNLADNEQRARSV-DSLLNFETVKYYGAEHYEV-------DCYREAILKYQKEEFLSM 476
Cdd:TIGR02857 153 TAPL-IPIFMILIGWAAQAAARKQWAALSRLSGHFlDRLRGLPTLKLFGRAKAQAaairrssEEYRERTMRVLRIAFLSS 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 477 LTLNMLNTaqniilclglLAGSLLCVYLVVHhqtLTVGDFVLFSTYLM-----ELYMPLNWFGTYYRAIQKNFVDMENMF 551
Cdd:TIGR02857 232 AVLELFAT----------LSVALVAVYIGFR---LLAGDLDLATGLFVlllapEFYLPLRQLGAQYHARADGVAAAEALF 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 552 DLLKEEEEIVdaPGCSPLLTA-GGGIEFSNVTFGYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQT 630
Cdd:TIGR02857 299 AVLDAAPRPL--AGKAPVTAApASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 631 GAILIDGQNIKLVQQQSLRKAIGVVPQDTVLFNNTIFYNIEYAKLGASDEAVYEAARAADIHERILGFPEKYETKVGERG 710
Cdd:TIGR02857 377 GSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGG 456
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19527665 711 LRLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVAHRLSTIIHADEILVL 783
Cdd:TIGR02857 457 AGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
576-786 |
5.26e-79 |
|
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: 252.69 E-value: 5.26e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSP-EKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGV 654
Cdd:cd03228 1 IEFKNVSFSYPGrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 655 VPQDTVLFNNTIFYNIeyaklgasdeavyeaaraadiherilgfpekyetkvgerglrLSGGEKQRVAIARTLLKAPIIV 734
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 19527665 735 LLDEATSALDTHTERNIQAALARVCANRTTIIVAHRLSTIIHADEILVLQQG 786
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
240-808 |
9.04e-79 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 269.67 E-value: 9.04e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 240 WPKKNIALQIAVIVCIILLL----AGRVIKLflpIYRKKLVDSLTIApiVFrwdFVLIYVALSFLQGGGTGsmGLFNnlr 315
Cdd:TIGR00958 160 WPWLISAFVFLTLSSLGEMFipfyTGRVIDT---LGGDKGPPALASA--IF---FMCLLSIASSVSAGLRG--GSFN--- 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 316 tFLWIRVQqyttREIEIELFRHLHQLSLRWHLQRKTGEVL-------RVMDRG-TDSINNLLNYIVfsiaptildLLVAV 387
Cdd:TIGR00958 227 -YTMARIN----LRIREDLFRSLLRQDLGFFDENKTGELTsrlssdtQTMSRSlSLNVNVLLRNLV---------MLLGL 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 388 AYFVYAFNWWFGLIVFLTMFLYIASTIAITEWRTKYQRRMN--LADNEQRARSVDSLLnfETVKYYGAEHYEVDCYREA- 464
Cdd:TIGR00958 293 LGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQeaVAKANQVAEEALSGM--RTVRSFAAEEGEASRFKEAl 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 465 --ILKYQKEEFLSmltlNMLNTAQNIILCLGLLAGSLLC-VYLVVHhQTLTVGDFVLFSTYLMELYMPLNWFGTYYRAIQ 541
Cdd:TIGR00958 371 eeTLQLNKRKALA----YAGYLWTTSVLGMLIQVLVLYYgGQLVLT-GKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMM 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 542 KNFVDMENMFDLLKEEEEIvDAPGCSPLLTAGGGIEFSNVTFGY--SPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIM 619
Cdd:TIGR00958 446 QAVGASEKVFEYLDRKPNI-PLTGTLAPLNLEGLIEFQDVSFSYpnRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVA 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 620 RLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGVVPQDTVLFNNTIFYNIEYAKLGASDEAVYEAARAADIHERILGFP 699
Cdd:TIGR00958 525 ALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFP 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 700 EKYETKVGERGLRLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARvcANRTTIIVAHRLSTIIHADE 779
Cdd:TIGR00958 605 NGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSR--ASRTVLLIAHRLSTVERADQ 682
|
570 580
....*....|....*....|....*....
gi 19527665 780 ILVLQQGSIAERGRHEELVLREDgIYADM 808
Cdd:TIGR00958 683 ILVLKKGSVVEMGTHKQLMEDQG-CYKHL 710
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
574-792 |
5.03e-70 |
|
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: 230.46 E-value: 5.03e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 574 GGIEFSNVTFGYSPE-KIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAI 652
Cdd:cd03244 1 GDIEFKNVSLRYRPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 653 GVVPQDTVLFNNTIFYNI----EYaklgaSDEAVYEAARAADIHERILGFPEKYETKVGERGLRLSGGEKQRVAIARTLL 728
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLdpfgEY-----SDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19527665 729 KAPIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVAHRLSTIIHADEILVLQQGSIAERG 792
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFD 219
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
574-788 |
6.05e-68 |
|
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: 225.04 E-value: 6.05e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 574 GGIEFSNVTFGY--SPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKA 651
Cdd:cd03248 10 GIVKFQNVTFAYptRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 652 IGVVPQDTVLFNNTIFYNIEYAKLGASDEAVYEAARAADIHERILGFPEKYETKVGERGLRLSGGEKQRVAIARTLLKAP 731
Cdd:cd03248 90 VSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 19527665 732 IIVLLDEATSALDTHTERNIQAALARVCANRTTIIVAHRLSTIIHADEILVLQQGSI 788
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
574-788 |
1.64e-66 |
|
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: 220.92 E-value: 1.64e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 574 GGIEFSNVTFGYSPEKI-VLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAI 652
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIpALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 653 GVVPQDTVLFNNTIFYNIEYAKLGASDEAVYEAARAADIHERILGFPEKYETKVGERGLRLSGGEKQRVAIARTLLKAPI 732
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 19527665 733 IVLLDEATSALDTHTERNIQAALARVCANRTTIIVAHRLSTIIHADEILVLQQGSI 788
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
503-813 |
1.77e-66 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 232.30 E-value: 1.77e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 503 YLVVHHqTLTVGDFVLFSTYLMELYMPLNWFGTYYRAIQKNFVDMENMFDLLKEEEEIVDapGCSPLLTAGGGIEFSNVT 582
Cdd:PRK10789 244 WMVVNG-SLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVKD--GSEPVPEGRGELDVNIRQ 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 583 FGY-SPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGVVPQDTVL 661
Cdd:PRK10789 321 FTYpQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFL 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 662 FNNTIFYNIEYAKLGASDEAVYEAARAADIHERILGFPEKYETKVGERGLRLSGGEKQRVAIARTLLKAPIIVLLDEATS 741
Cdd:PRK10789 401 FSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALS 480
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19527665 742 ALDTHTERNIQAALARVCANRTTIIVAHRLSTIIHADEILVLQQGSIAERGRHEELVlREDGIYADMWQ-QQL 813
Cdd:PRK10789 481 AVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLA-QQSGWYRDMYRyQQL 552
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
295-801 |
8.36e-66 |
|
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: 230.41 E-value: 8.36e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 295 VALSFLQGGGTGSMGLFNNLRTFLWIRVqqytTREIEIELFRHLHQLSLRWHLQRKTGEVLRVMDrgtDsINNLLNYIVF 374
Cdd:COG4618 60 LMLTLLALGLYAVMGLLDAVRSRILVRV----GARLDRRLGPRVFDAAFRAALRGGGGAAAQALR---D-LDTLRQFLTG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 375 SIAPTILDLLVAVAY--FVYAFNWWFGLIVFLTMFLYIASTIaITEWRT-KYQRRMNLADNeQRARSVDSLL-NFETVKY 450
Cdd:COG4618 132 PGLFALFDLPWAPIFlaVLFLFHPLLGLLALVGALVLVALAL-LNERLTrKPLKEANEAAI-RANAFAEAALrNAEVIEA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 451 YGAEHYEVDCYREAILKYQKEE--------FLSMLT--LNMLntAQNIILCLGllagsllcVYLVVHHQtLTVGdfVLF- 519
Cdd:COG4618 210 MGMLPALRRRWQRANARALALQarasdragGFSALSkfLRLL--LQSAVLGLG--------AYLVIQGE-ITPG--AMIa 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 520 STYLM-ELYMPL-----NWfgtyyraiqKNFVD-------MENMFDLLKEEEEIVdapgcsPLLTAGGGIEFSNVTFGYS 586
Cdd:COG4618 277 ASILMgRALAPIeqaigGW---------KQFVSarqayrrLNELLAAVPAEPERM------PLPRPKGRLSVENLTVVPP 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 587 P-EKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGVVPQDTVLFNNT 665
Cdd:COG4618 342 GsKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGT 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 666 IFYNIeyAKLG-ASDEAVYEAARAADIHERILGFPEKYETKVGERGLRLSGGEKQRVAIARTLLKAPIIVLLDEATSALD 744
Cdd:COG4618 422 IAENI--ARFGdADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLD 499
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 19527665 745 THTERNIQAALARVCA-NRTTIIVAHRLSTIIHADEILVLQQGSIAERGRHEElVLRE 801
Cdd:COG4618 500 DEGEAALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDE-VLAR 556
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
492-813 |
8.00e-65 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 228.45 E-value: 8.00e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 492 LGLLAGSLLCVYLVVH----HQTLTVGDFVLFSTYLMELYMPLNWFGTYYRAIQKNFVDMENMFDLLkeeeeivDAP--- 564
Cdd:PRK10790 256 LSLFSALILCGLLMLFgfsaSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELM-------DGPrqq 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 565 -GCSPLLTAGGGIEFSNVTFGYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLV 643
Cdd:PRK10790 329 yGNDDRPLQSGRIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSL 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 644 QQQSLRKAIGVVPQDTVLFNNTIFYNIeyaKLG--ASDEAVYEAARAADIHERILGFPEKYETKVGERGLRLSGGEKQRV 721
Cdd:PRK10790 409 SHSVLRQGVAMVQQDPVVLADTFLANV---TLGrdISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLL 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 722 AIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVAHRLSTIIHADEILVLQQGSIAERGRHEELvLRE 801
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQL-LAA 564
|
330
....*....|..
gi 19527665 802 DGIYADMWQQQL 813
Cdd:PRK10790 565 QGRYWQMYQLQL 576
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
230-808 |
4.13e-64 |
|
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: 228.86 E-value: 4.13e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 230 RKLRTVFPYLWPKKNIALQI---AVIVCIILLLAGRVIKLFLPIY-RKKLVDSLTIAPIvfrwDFVLIYValsfLQGggt 305
Cdd:TIGR01193 142 NSLLKFIPLITRQKKLIVNIviaAIIVTLISIAGSYYLQKIIDTYiPHKMMGTLGIISI----GLIIAYI----IQQ--- 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 306 gsmgLFNNLRTFLWIRVQQYTTREIEIELFRHLHQLSLRWHLQRKTGEVLrvmDRGTDSinnllNYIVFSIAPTILDL-- 383
Cdd:TIGR01193 211 ----ILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIV---SRFTDA-----SSIIDALASTILSLfl 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 384 ----LVAVAYFVYAFNWWFGLIVFLTMFLYIASTIAITEWRTKYQRRMNLADNEQRARSVDSLLNFETVKYYGAEH---- 455
Cdd:TIGR01193 279 dmwiLVIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAerys 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 456 ---YEVDCYREAILKYQKEEFLSMLTLNMLNTAQNIILclgLLAGSllcvYLVVHHQtLTVGDFVLFSTYLMELYMPLNW 532
Cdd:TIGR01193 359 kidSEFGDYLNKSFKYQKADQGQQAIKAVTKLILNVVI---LWTGA----YLVMRGK-LTLGQLITFNALLSYFLTPLEN 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 533 FGTYYRAIQKNFVDMENMFDLLKEEEEIVDAPGCSPLLTAGGGIEFSNVTFGYSPEKIVLRNVSFTVPAGKTVAIVGPSG 612
Cdd:TIGR01193 431 IINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTELNNLNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSG 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 613 AGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGVVPQDTVLFNNTIFYN-IEYAKLGASDEAVYEAARAADI 691
Cdd:TIGR01193 511 SGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENlLLGAKENVSQDEIWAACEIAEI 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 692 HERILGFPEKYETKVGERGLRLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVcANRTTIIVAHRL 771
Cdd:TIGR01193 591 KDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNL-QDKTIIFVAHRL 669
|
570 580 590
....*....|....*....|....*....|....*..
gi 19527665 772 STIIHADEILVLQQGSIAERGRHEELvLREDGIYADM 808
Cdd:TIGR01193 670 SVAKQSDKIIVLDHGKIIEQGSHDEL-LDRNGFYASL 705
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
334-771 |
1.83e-59 |
|
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: 211.84 E-value: 1.83e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 334 LFRHLHQLSLRWHLQRKTGEVLrvmDRGTDSINNLLNYIVFSIAPTILDLLVAVAY--FVYAFNWWFGLI--VFLTMFLY 409
Cdd:TIGR02868 92 VYERLARQALAGRRRLRRGDLL---GRLGADVDALQDLYVRVIVPAGVALVVGAAAvaAIAVLSVPAALIlaAGLLLAGF 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 410 IASTIAITEWRTKYQRRMNLAdNEQRARSVDSLLNFETVKYYGAEHYEVDCYREAILKYQKEEfLSMLTLNMLNTAQNII 489
Cdd:TIGR02868 169 VAPLVSLRAARAAEQALARLR-GELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAE-RRAAAATALGAALTLL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 490 LC-LGLLAGSLLCVYLVVHHQ----TLTVgdFVLFSTYLMELYMPL-NWFGTYYRAIQKnfvdMENMFDLL--KEEEEIV 561
Cdd:TIGR02868 247 AAgLAVLGALWAGGPAVADGRlapvTLAV--LVLLPLAAFEAFAALpAAAQQLTRVRAA----AERIVEVLdaAGPVAEG 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 562 DAPGCSPLLTAGGGIEFSNVTFGYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIK 641
Cdd:TIGR02868 321 SAPAAGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVS 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 642 LVQQQSLRKAIGVVPQDTVLFNNTIFYNIEYAKLGASDEAVYEAARAADIHERILGFPEKYETKVGERGLRLSGGEKQRV 721
Cdd:TIGR02868 401 SLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRL 480
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 19527665 722 AIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVAHRL 771
Cdd:TIGR02868 481 ALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
559-812 |
2.12e-56 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 204.29 E-value: 2.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 559 EIVDA------PGCSPLLTAGGGIEFSNVTFGYSP-EKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTG 631
Cdd:PRK11160 316 EITEQkpevtfPTTSTAAADQVSLTLNNVSFTYPDqPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 632 AILIDGQNIKLVQQQSLRKAIGVVPQDTVLFNNTIFYNIEYAKLGASDEAVYEAARAADIhERILGFPEKYETKVGERGL 711
Cdd:PRK11160 396 EILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGL-EKLLEDDKGLNAWLGEGGR 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 712 RLSGGEKQRVAIARTLLK-APiIVLLDEATSALDTHTERNIQAALARVCANRTTIIVAHRLSTIIHADEILVLQQGSIAE 790
Cdd:PRK11160 475 QLSGGEQRRLGIARALLHdAP-LLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIE 553
|
250 260
....*....|....*....|..
gi 19527665 791 RGRHEELvLREDGIYADMWQQQ 812
Cdd:PRK11160 554 QGTHQEL-LAQQGRYYQLKQRL 574
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
510-812 |
6.98e-56 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 203.15 E-value: 6.98e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 510 TLTVGDFVLFstyLM-ELYMPLNWFGTYYRAIQKNFVDMENMFDLLKEEEEIVDAPGCSPLLTAGGGIEFSNVTFgYSPE 588
Cdd:PRK11174 286 TLFAGFFVLI---LApEFYQPLRDLGTFYHAKAQAVGAAESLVTFLETPLAHPQQGEKELASNDPVTIEAEDLEI-LSPD 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 589 -KIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQtGAILIDGQNIKLVQQQSLRKAIGVVPQDTVLFNNTIF 667
Cdd:PRK11174 362 gKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLR 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 668 YNIEYAKLGASDEAVYEAARAADIHERILGFPEKYETKVGERGLRLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHT 747
Cdd:PRK11174 441 DNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19527665 748 ERNIQAALARVCANRTTIIVAHRLSTIIHADEILVLQQGSIAERGRHEELVlREDGIYADMWQQQ 812
Cdd:PRK11174 521 EQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELS-QAGGLFATLLAHR 584
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
574-793 |
9.13e-56 |
|
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: 191.09 E-value: 9.13e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 574 GGIEFSNVTFGYSPE-KIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAI 652
Cdd:cd03369 5 GEIEVENLSVRYAPDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 653 GVVPQDTVLFNNTIFYNI----EYaklgaSDEAVYEAARaadiherilgfpekyetkVGERGLRLSGGEKQRVAIARTLL 728
Cdd:cd03369 85 TIIPQDPTLFSGTIRSNLdpfdEY-----SDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19527665 729 KAPIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVAHRLSTIIHADEILVLQQGSIAERGR 793
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
440-805 |
9.09e-49 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 187.93 E-value: 9.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 440 DSLLNFETVKYYGAEHYEVDCYREAILKYQKEEFLSMLTLNML----NTAQNIILCLGLLAGSLLcvylvVHHQTLTVGD 515
Cdd:PTZ00265 1027 EAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLwgfsQSAQLFINSFAYWFGSFL-----IRRGTILVDD 1101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 516 FV--LFSTYLMELY----MPLNW--------FGTYYRAI-QKNFVDMENMFDLLKEEEEIVDapgcsplltagGGIEFSN 580
Cdd:PTZ00265 1102 FMksLFTFLFTGSYagklMSLKGdsenaklsFEKYYPLIiRKSNIDVRDNGGIRIKNKNDIK-----------GKIEIMD 1170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 581 VTFGY--SPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQ----------------------------- 629
Cdd:PTZ00265 1171 VNFRYisRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKndhhivfknehtndmtneqdyqgdeeqnv 1250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 630 -------------------------TGAILIDGQNIKLVQQQSLRKAIGVVPQDTVLFNNTIFYNIEYAKLGASDEAVYE 684
Cdd:PTZ00265 1251 gmknvnefsltkeggsgedstvfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKR 1330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 685 AARAADIHERILGFPEKYETKVGERGLRLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARV--CANR 762
Cdd:PTZ00265 1331 ACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADK 1410
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 19527665 763 TTIIVAHRLSTIIHADEILVL----QQGSIAE-RGRHEELVLREDGIY 805
Cdd:PTZ00265 1411 TIITIAHRIASIKRSDKIVVFnnpdRTGSFVQaHGTHEELLSVQDGVY 1458
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
576-792 |
3.87e-47 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 165.95 E-value: 3.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSP-EKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQsLRKAIGV 654
Cdd:cd03247 1 LSINNVSFSYPEqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 655 VPQDTVLFNNTIFYNIeyaklgasdeavyeaaraadiherilgfpekyetkvgerGLRLSGGEKQRVAIARTLLKAPIIV 734
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 19527665 735 LLDEATSALDTHTERNIQAALARVCANRTTIIVAHRLSTIIHADEILVLQQGSIAERG 792
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
576-788 |
4.35e-47 |
|
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: 165.47 E-value: 4.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYS-PEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGV 654
Cdd:cd03246 1 LEVENVSFRYPgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 655 VPQDTVLFNNTIFYNIeyaklgasdeavyeaaraadiherilgfpekyetkvgerglrLSGGEKQRVAIARTLLKAPIIV 734
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 19527665 735 LLDEATSALDTHTERNIQAALARV-CANRTTIIVAHRLSTIIHADEILVLQQGSI 788
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
576-802 |
7.61e-46 |
|
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: 164.04 E-value: 7.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGVV 655
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 656 PQ--DTVLFNNTIFYNIEYA--KLGASDEAVYEAARAAdiheriLgfpekyeTKVGERGLR------LSGGEKQRVAIAR 725
Cdd:COG1122 81 FQnpDDQLFAPTVEEDVAFGpeNLGLPREEIRERVEEA------L-------ELVGLEHLAdrppheLSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19527665 726 TLLKAPIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVA-HRLSTII-HADEILVLQQGSIAERGRHEELVLRED 802
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVAeLADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
576-797 |
2.29e-45 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 162.74 E-value: 2.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSpEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQ-----TGAILIDGQNIKLVQQQ--SL 648
Cdd:cd03260 1 IELRDLNVYYG-DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDLDVDvlEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 649 RKAIGVVPQDTVLFNNTIFYNIEYA-KLGAS------DEAVYEAARAADIHERilgfpekyetkVGER--GLRLSGGEKQ 719
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGlRLHGIklkeelDERVEEALRKAALWDE-----------VKDRlhALGLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19527665 720 RVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVAHRLSTIIH-ADEILVLQQGSIAERGRHEEL 797
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
592-741 |
6.64e-45 |
|
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: 158.58 E-value: 6.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 592 LRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGVVPQDTVLFNN-TIFYNI 670
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19527665 671 EYAKLGASDEAVYEAARAADIHERiLGFPEKYETKVGERGLRLSGGEKQRVAIARTLLKAPIIVLLDEATS 741
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEK-LGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
577-786 |
7.00e-45 |
|
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: 160.71 E-value: 7.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 577 EFSNVTFGY-SPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGVV 655
Cdd:cd03225 1 ELKNLSFSYpDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 656 PQ--DTVLFNNTIFYNIEYA--KLGASDEavyeaaraaDIHERIlgfpEKYETKVGERGLR------LSGGEKQRVAIAR 725
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVAFGleNLGLPEE---------EIEERV----EEALELVGLEGLRdrspftLSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19527665 726 TLLKAPIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVA-HRLSTII-HADEILVLQQG 786
Cdd:cd03225 148 VLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLeLADRVIVLEDG 210
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
576-786 |
7.87e-45 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 160.37 E-value: 7.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSpEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGVV 655
Cdd:COG4619 1 LELEGLSFRVG-GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 656 PQDTVLFNNTIFYNIEYAKLGASDEavYEAARAADIHERiLGFPEKY-ETKVGerglRLSGGEKQRVAIARTLLKAPIIV 734
Cdd:COG4619 80 PQEPALWGGTVRDNLPFPFQLRERK--FDRERALELLER-LGLPPDIlDKPVE----RLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 735 LLDEATSALDTHTERNIQAALARVCA--NRTTIIVAH------RLstiihADEILVLQQG 786
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYLAeeGRAVLWVSHdpeqieRV-----ADRVLTLEAG 207
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
576-790 |
2.09e-43 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 156.75 E-value: 2.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLV---QQQSLRKAI 652
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 653 GVVPQDTVLFNN-TIFYNIEYAK--LGASDEAVyeAARAADIHERiLGFPEKYETKVGErglrLSGGEKQRVAIARTLLK 729
Cdd:COG2884 82 GVVFQDFRLLPDrTVYENVALPLrvTGKSRKEI--RRRVREVLDL-VGLSDKAKALPHE----LSGGEQQRVAIARALVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19527665 730 APIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVAhrlsTiiHADEI--------LVLQQGSIAE 790
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIA----T--HDLELvdrmpkrvLELEDGRLVR 217
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
576-802 |
5.86e-43 |
|
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: 156.74 E-value: 5.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYsPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGVV 655
Cdd:COG1120 2 LEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 656 PQDTVL-FNNTIFyniEYAKLG------------ASD-EAVYEAARAADIH---ERILGfpekyetkvgerglRLSGGEK 718
Cdd:COG1120 81 PQEPPApFGLTVR---ELVALGryphlglfgrpsAEDrEAVEEALERTGLEhlaDRPVD--------------ELSGGER 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 719 QRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCA--NRTTIIVAHRLSTII-HADEILVLQQGSIAERGRHE 795
Cdd:COG1120 144 QRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARerGRTVVMVLHDLNLAArYADRLVLLKDGRIVAQGPPE 223
|
....*..
gi 19527665 796 ElVLRED 802
Cdd:COG1120 224 E-VLTPE 229
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
576-835 |
6.71e-43 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 169.44 E-value: 6.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSPEKIV--LRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILI-DGQNIKLVQQQSLRKAI 652
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVeiYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 653 GVVPQDTVLFNNTIFYNIEYA-------------------------------------------KLGASDEAV-----YE 684
Cdd:PTZ00265 463 GVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsNTTDSNELIemrknYQ 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 685 AARAAD---------IHERILGFPEKYETKVGERGLRLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAAL 755
Cdd:PTZ00265 543 TIKDSEvvdvskkvlIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 756 ARVCA--NRTTIIVAHRLSTIIHADEILVLqqgSIAERG-RHEELVLREDGIYADMWQQQLKNLDAEQSGGSDNGDASAE 832
Cdd:PTZ00265 623 NNLKGneNRITIIIAHRLSTIRYANTIFVL---SNRERGsTVDVDIIGEDPTKDNKENNNKNNKDDNNNNNNNNNNKINN 699
|
...
gi 19527665 833 SGS 835
Cdd:PTZ00265 700 AGS 702
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
491-808 |
1.45e-42 |
|
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: 168.59 E-value: 1.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 491 CLGLLAGsllcVYLVVHHQTLTVGDFVLFSTYLMELYMPLNWFGTYYRAIQKNFVDMENMFDLLKEEEEivdAP----GC 566
Cdd:TIGR00957 1201 CIVLFAA----LFAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKE---APwqiqET 1273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 567 SPLLT--AGGGIEFSNVTFGYSPE-KIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLV 643
Cdd:TIGR00957 1274 APPSGwpPRGRVEFRNYCLRYREDlDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKI 1353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 644 QQQSLRKAIGVVPQDTVLFNNTIFYNIE-YAKLgaSDEAVYEAARAADIHERILGFPEKYETKVGERGLRLSGGEKQRVA 722
Cdd:TIGR00957 1354 GLHDLRFKITIIPQDPVLFSGSLRMNLDpFSQY--SDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVC 1431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 723 IARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVAHRLSTIIHADEILVLQQGSIAERGRHEELvLRED 802
Cdd:TIGR00957 1432 LARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNL-LQQR 1510
|
....*.
gi 19527665 803 GIYADM 808
Cdd:TIGR00957 1511 GIFYSM 1516
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
576-797 |
2.47e-42 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 154.45 E-value: 2.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSpEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKlVQQQSLRKAIGVV 655
Cdd:COG1131 1 IEVRGLTKRYG-DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA-RDPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 656 PQDTVLFNN-TIFYNIEY-AKL-GASDEAVyeAARAADIHERiLGFPEKYETKVGErglrLSGGEKQRVAIARTLLKAPI 732
Cdd:COG1131 79 PQEPALYPDlTVRENLRFfARLyGLPRKEA--RERIDELLEL-FGLTDAADRKVGT----LSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19527665 733 IVLLDEATSALDTHTERNIQAALARVCANRTTIIVA-HRLSTIIH-ADEILVLQQGSIAERGRHEEL 797
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAERlCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
577-786 |
5.73e-42 |
|
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: 150.47 E-value: 5.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 577 EFSNVTFGYsPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGVVP 656
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 657 QdtvlfnntifynieyaklgasdeavyeaaraadiherilgfpekyetkvgerglrLSGGEKQRVAIARTLLKAPIIVLL 736
Cdd:cd00267 80 Q-------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 19527665 737 DEATSALDTHTERNIQAALARVCA-NRTTIIVAHRLSTIIHA-DEILVLQQG 786
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
576-797 |
5.91e-42 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 153.47 E-value: 5.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSpEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKlVQQQSLRKAIGVV 655
Cdd:COG4555 2 IEVENLSKKYG-KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR-KEPREARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 656 PQDTVLF-NNTIFYNIEY-AKL-GASDEAVyeAARAADIHERiLGFPEKYETKVGErglrLSGGEKQRVAIARTLLKAPI 732
Cdd:COG4555 80 PDERGLYdRLTVRENIRYfAELyGLFDEEL--KKRIEELIEL-LGLEEFLDRRVGE----LSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19527665 733 IVLLDEATSALDTHTERNIQAALARVCANRTTIIVA-HRLSTIIH-ADEILVLQQGSIAERGRHEEL 797
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDEL 219
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
576-798 |
2.18e-41 |
|
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: 152.26 E-value: 2.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSP---EKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAI 652
Cdd:COG1124 2 LEVRNLSVSYGQggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 653 GVVPQD---------TVlfNNTIFYNIEYAKLGASDEAVYEAARAADIHERILG-FPEKyetkvgerglrLSGGEKQRVA 722
Cdd:COG1124 82 QMVFQDpyaslhprhTV--DRILAEPLRIHGLPDREERIAELLEQVGLPPSFLDrYPHQ-----------LSGGQRQRVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19527665 723 IARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANR--TTIIVAHRLSTIIH-ADEILVLQQGSIAERGRHEELV 798
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLL 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
576-788 |
3.28e-41 |
|
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: 150.33 E-value: 3.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGY---SPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNI---KLVQQQSLR 649
Cdd:cd03255 1 IELKNLSKTYgggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsklSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 650 -KAIGVVPQDTVLFNN-TIFYNIEYAKLGASDEAVYEAARAADIHERiLGFPEKYETKVGErglrLSGGEKQRVAIARTL 727
Cdd:cd03255 81 rRHIGFVFQSFNLLPDlTALENVELPLLLAGVPKKERRERAEELLER-VGLGDRLNHYPSE----LSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19527665 728 LKAPIIVLLDEATSALDTHTERNIQAALARVC--ANRTTIIVAHRLSTIIHADEILVLQQGSI 788
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLRELNkeAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
576-797 |
6.05e-41 |
|
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: 158.14 E-value: 6.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGY----SPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQS---L 648
Cdd:COG1123 261 LEVRNLSKRYpvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlreL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 649 RKAIGVVPQDTVL-FN--NTIFYNIEYA----KLGASDEAvyeAARAADIHERiLGFPEKYETKvgeRGLRLSGGEKQRV 721
Cdd:COG1123 341 RRRVQMVFQDPYSsLNprMTVGDIIAEPlrlhGLLSRAER---RERVAELLER-VGLPPDLADR---YPHELSGGQRQRV 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19527665 722 AIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCA--NRTTIIVAHRLSTIIH-ADEILVLQQGSIAERGRHEEL 797
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEV 492
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
576-800 |
7.63e-41 |
|
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: 150.04 E-value: 7.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVT--FGYSPEKI-VLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKA- 651
Cdd:cd03258 2 IELKNVSkvFGDTGGKVtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 652 --IGVVPQDTVLFNN-TIFYNIEYA-KLGASDEAvyeaARAADIHE--RILGFPEKYETKVGErglrLSGGEKQRVAIAR 725
Cdd:cd03258 82 rrIGMIFQHFNLLSSrTVFENVALPlEIAGVPKA----EIEERVLEllELVGLEDKADAYPAQ----LSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 726 TLLKAPIIVLLDEATSALDTHTERNIQAALARVcaNR----TTIIVAHRLSTI--IhADEILVLQQGSIAERGRHEELVL 799
Cdd:cd03258 154 ALANNPKVLLCDEATSALDPETTQSILALLRDI--NRelglTIVLITHEMEVVkrI-CDRVAVMEKGEVVEEGTVEEVFA 230
|
.
gi 19527665 800 R 800
Cdd:cd03258 231 N 231
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
576-786 |
1.22e-40 |
|
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: 147.33 E-value: 1.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYsPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQS--LRKAIG 653
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 654 VVPQDTVLFNN-TIFYNIEYAklgasdeavyeaaraadiherilgfpekyetkvgerglrLSGGEKQRVAIARTLLKAPI 732
Cdd:cd03229 80 MVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 19527665 733 IVLLDEATSALDTHTERNIQAALARVCAN--RTTIIVAHRLSTIIH-ADEILVLQQG 786
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
576-792 |
1.55e-40 |
|
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: 148.44 E-value: 1.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYsPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQslRKAIGVV 655
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 656 PQDTVLFNN-TIFYNIEYA-KLGASDEAVyEAARAADIHERiLGFPEKYETKVGErglrLSGGEKQRVAIARTLLKAPII 733
Cdd:cd03259 78 FQDYALFPHlTVAENIAFGlKLRGVPKAE-IRARVRELLEL-VGLEGLLNRYPHE----LSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19527665 734 VLLDEATSALDTHTERNIQAALARVCANR--TTIIVAHRLSTIIH-ADEILVLQQGSIAERG 792
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
576-792 |
4.48e-40 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 147.65 E-value: 4.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSPEKI---VLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNI---KLVQQQSLR 649
Cdd:cd03257 2 LEVKNLSVSFPTGGGsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 650 KAIGVVPQD--TVLfnN---TIFYNIEYAKLGASDEAVYEAARAADIHERI-LGFPEKYETKvgeRGLRLSGGEKQRVAI 723
Cdd:cd03257 82 KEIQMVFQDpmSSL--NprmTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVgVGLPEEVLNR---YPHELSGGQRQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19527665 724 ARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCA--NRTTIIVAHRLSTIIH-ADEILVLQQGSIAERG 792
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
576-791 |
4.79e-40 |
|
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: 147.23 E-value: 4.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGY---SPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIklvqqQSLRKAI 652
Cdd:cd03293 1 LEVRNVSKTYgggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV-----TGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 653 GVVPQDTVLFN-NTIFYNIEYA-KL-GASDEAVYEAARAAdIHE-RILGFPEKYETkvgerglRLSGGEKQRVAIARTLL 728
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGlELqGVPKAEARERAEEL-LELvGLSGFENAYPH-------QLSGGMRQRVALARALA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19527665 729 KAPIIVLLDEATSALDTHTERNIQAALARVCA--NRTTIIVAHRLSTIIH-ADEILVLQQ--GSIAER 791
Cdd:cd03293 148 VDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDIDEAVFlADRVVVLSArpGRIVAE 215
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
576-793 |
1.52e-39 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 145.96 E-value: 1.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGY---SPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNI-KLVQQQ--SLR 649
Cdd:COG1136 5 LELRNLTKSYgtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsSLSERElaRLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 650 -KAIGVVPQDTVLFNN-TIFYNIEYAKLGASDEAVYEAARAADIHERiLGFPEKYETKVGErglrLSGGEKQRVAIARTL 727
Cdd:COG1136 85 rRHIGFVFQFFNLLPElTALENVALPLLLAGVSRKERRERARELLER-VGLGDRLDHRPSQ----LSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19527665 728 LKAPIIVLLDEATSALDTHTERNIQAALARVCA--NRTTIIVAHRLSTIIHADEILVLQQGSIAERGR 793
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVSDER 227
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
577-792 |
1.70e-39 |
|
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: 144.12 E-value: 1.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 577 EFSNVTFGYsPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGVVP 656
Cdd:cd03214 1 EVENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 657 QdtVLfnntifynieyAKLGASDEAvyeaaraadihERILGfpekyetkvgerglRLSGGEKQRVAIARTLLKAPIIVLL 736
Cdd:cd03214 80 Q--AL-----------ELLGLAHLA-----------DRPFN--------------ELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 19527665 737 DEATSALDTHTERNIQAALARVCA--NRTTIIVAHRLS-TIIHADEILVLQQGSIAERG 792
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARerGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
574-810 |
2.40e-39 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 158.36 E-value: 2.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 574 GGIEFSNVTFGYSPE-KIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAI 652
Cdd:PLN03130 1236 GSIKFEDVVLRYRPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVL 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 653 GVVPQDTVLFNNTIFYNI----EYaklgaSDEAVYEAARAADIHERILGFPEKYETKVGERGLRLSGGEKQRVAIARTLL 728
Cdd:PLN03130 1316 GIIPQAPVLFSGTVRFNLdpfnEH-----NDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALL 1390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 729 KAPIIVLLDEATSALDTHTERNIQAALA---RVCanrTTIIVAHRLSTIIHADEILVLQQGSIAERGRHEELVLREDGIY 805
Cdd:PLN03130 1391 RRSKILVLDEATAAVDVRTDALIQKTIReefKSC---TMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAF 1467
|
....*
gi 19527665 806 ADMWQ 810
Cdd:PLN03130 1468 SKMVQ 1472
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
576-802 |
3.26e-39 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 145.62 E-value: 3.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSpEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVqqqslRKAIGVV 655
Cdd:COG1121 7 IELENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 656 PQ-------------DTVLFNNtifynieYAKLG-------ASDEAVYEAARAADIHERIlgfpekyETKVGErglrLSG 715
Cdd:COG1121 81 PQraevdwdfpitvrDVVLMGR-------YGRRGlfrrpsrADREAVDEALERVGLEDLA-------DRPIGE----LSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 716 GEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANRTTII-VAHRLSTII-HADEILVLQQGSIAErGR 793
Cdd:COG1121 143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILvVTHDLGAVReYFDRVLLLNRGLVAH-GP 221
|
....*....
gi 19527665 794 HEElVLRED 802
Cdd:COG1121 222 PEE-VLTPE 229
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
549-822 |
4.07e-39 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 157.83 E-value: 4.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 549 NMFDLLKEEEEIV--DAPGCS-PLltaGGGIEFSNVTFGYSPE-KIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFR 624
Cdd:PLN03232 1208 NYIDLPSEATAIIenNRPVSGwPS---RGSIKFEDVHLRYRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFR 1284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 625 FYDVQTGAILIDGQNIKLVQQQSLRKAIGVVPQDTVLFNNTIFYNIE-YAKlgASDEAVYEAARAADIHERILGFPEKYE 703
Cdd:PLN03232 1285 IVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDpFSE--HNDADLWEALERAHIKDVIDRNPFGLD 1362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 704 TKVGERGLRLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVAHRLSTIIHADEILVL 783
Cdd:PLN03232 1363 AEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVL 1442
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 19527665 784 QQGSIAERGRHEELVLREDGIYADMWQ-------QQLKNLDAEQSG 822
Cdd:PLN03232 1443 SSGQVLEYDSPQELLSRDTSAFFRMVHstgpanaQYLSNLVFERRE 1488
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
576-807 |
5.97e-39 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 145.20 E-value: 5.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKA---I 652
Cdd:COG3638 3 LELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrrrI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 653 GVVPQD-------TVLFN---------NT------IFYNIEYAklgasdeavyeaaRAADIHERiLGFPEKYETKVGErg 710
Cdd:COG3638 83 GMIFQQfnlvprlSVLTNvlagrlgrtSTwrsllgLFPPEDRE-------------RALEALER-VGLADKAYQRADQ-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 711 lrLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCA--NRTTIIVAHRLSTII-HADEILVLQQGS 787
Cdd:COG3638 147 --LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDLARrYADRIIGLRDGR 224
|
250 260
....*....|....*....|...
gi 19527665 788 IAERGRHEEL---VLREdgIYAD 807
Cdd:COG3638 225 VVFDGPPAELtdaVLRE--IYGG 245
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
576-797 |
1.26e-38 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 143.80 E-value: 1.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSpEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNI---KLVQQQSLRKAI 652
Cdd:cd03261 1 IELRGLTKSFG-GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglSEAELYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 653 GVVPQDTVLFNN-TIFYNI-----EYAKLGASdeavyeaaraaDIHERILgfpEKYETkVGERGLR------LSGGEKQR 720
Cdd:cd03261 80 GMLFQSGALFDSlTVFENVafplrEHTRLSEE-----------EIREIVL---EKLEA-VGLRGAEdlypaeLSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 721 VAIARTLLKAPIIVLLDEATSALD-------THTERNIQAALarvcaNRTTIIVAHRLSTIIH-ADEILVLQQGSIAERG 792
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDpiasgviDDLIRSLKKEL-----GLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEG 219
|
....*
gi 19527665 793 RHEEL 797
Cdd:cd03261 220 TPEEL 224
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
567-806 |
3.22e-38 |
|
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: 143.51 E-value: 3.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 567 SPLLTAGGGIEFSNVTFGY-SPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQ 645
Cdd:cd03288 11 SGLVGLGGEIKIHDLCVRYeNNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 646 QSLRKAIGVVPQDTVLFNNTIFYNIEYAKlGASDEAVYEAARAADIHERILGFPEKYETKVGERGLRLSGGEKQRVAIAR 725
Cdd:cd03288 91 HTLRSRLSIILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLAR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 726 TLLKAPIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVAHRLSTIIHADEILVLQQGSIAERGRHEELVLREDGIY 805
Cdd:cd03288 170 AFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVF 249
|
.
gi 19527665 806 A 806
Cdd:cd03288 250 A 250
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
576-797 |
4.07e-38 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 142.43 E-value: 4.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSpEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNI---KLVQQQSLRKAI 652
Cdd:COG1127 6 IEVRNLTKSFG-DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglSEKELYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 653 GVVPQDTVLFNN-TIFYNI-----EYAKLGasdeavyeaarAADIHERILgfpEKYEtKVGERGLR------LSGGEKQR 720
Cdd:COG1127 85 GMLFQGGALFDSlTVFENVafplrEHTDLS-----------EAEIRELVL---EKLE-LVGLPGAAdkmpseLSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 721 VAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANR--TTIIVAHRLSTIIH-ADEILVLQQGSIAERGRHEEL 797
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEEL 229
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
571-821 |
7.64e-38 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 142.15 E-value: 7.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 571 TAGGGIEFSNVTFGYSPEK---IVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKlvqqqS 647
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT-----G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 648 LRKAIGVVPQDTVLFN-NTIFYNIEYA--KLGASDEAVYEAARAAdiheriL------GFPEKY--EtkvgerglrLSGG 716
Cdd:COG1116 78 PGPDRGVVFQEPALLPwLTVLDNVALGleLRGVPKAERRERAREL------LelvglaGFEDAYphQ---------LSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 717 EKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCA--NRTTIIVAH------RLstiihADEILVLQQ--G 786
Cdd:COG1116 143 MRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQetGKTVLFVTHdvdeavFL-----ADRVVVLSArpG 217
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 19527665 787 SIAE-------RGRHEElvLREDGIYADMWQQQLKNLDAEQS 821
Cdd:COG1116 218 RIVEeidvdlpRPRDRE--LRTSPEFAALRAEILDLLREEAE 257
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
577-789 |
1.46e-37 |
|
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: 139.98 E-value: 1.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 577 EFSNVTFGYSpEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVqqqslRKAIGVVP 656
Cdd:cd03235 1 EVEDLTVSYG-GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 657 Q-------------DTVLFNNTIFYNIeYAKLGASDEAVYEAA----RAADIHERILGfpekyetkvgerglRLSGGEKQ 719
Cdd:cd03235 75 QrrsidrdfpisvrDVVLMGLYGHKGL-FRRLSKADKAKVDEAlervGLSELADRQIG--------------ELSGGQQQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19527665 720 RVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCA-NRTTIIVAHRLSTII-HADEILVLQQGSIA 789
Cdd:cd03235 140 RVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRReGMTILVVTHDLGLVLeYFDRVLLLNRTVVA 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
576-797 |
7.15e-37 |
|
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: 146.20 E-value: 7.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSPEKI-VLRNVSFTVPAGKTVAIVGPSGAGKST----IMRLLFRFYDVqTGAILIDGQNIKLVQQQSLRK 650
Cdd:COG1123 5 LEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTlalaLMGLLPHGGRI-SGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 651 AIGVVPQD--TVLFNNTIFYNIEYA--KLGASDEA----VYEAARAADIHERILGFPEkyetkvgerglRLSGGEKQRVA 722
Cdd:COG1123 84 RIGMVFQDpmTQLNPVTVGDQIAEAleNLGLSRAEararVLELLEAVGLERRLDRYPH-----------QLSGGQRQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19527665 723 IARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANR--TTIIVAHRLSTIIH-ADEILVLQQGSIAERGRHEEL 797
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
251-530 |
9.34e-37 |
|
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: 139.70 E-value: 9.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 251 VIVCIILLLAGRVIKLFLPIYRKKLVDSLTIAPIVFRWDFVLIYVALSFLqgggTGSMGLFNNLRTFLWIRVQQYTTREI 330
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLL----GLAQFILSFLQSYLLNHTGERLSRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 331 EIELFRHLHQLSLRWHLQRKTGEVLRVMDRGTDSINNLLNYIVFSIAPTILDLLVAVAYFVYaFNWWFGLIVFLTMFLYI 410
Cdd:pfam00664 77 RRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFY-YGWKLTLVLLAVLPLYI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 411 ASTIAITEWRTKYQRRMNLADNEQRARSVDSLLNFETVKYYGAEHYEVDCYREAILKYQKEEFLSMLTLNMLNTAQNIIL 490
Cdd:pfam00664 156 LVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIG 235
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 19527665 491 CLGLLAGSLLCVYLVVHHQtLTVGDFVLFSTYLMELYMPL 530
Cdd:pfam00664 236 YLSYALALWFGAYLVISGE-LSVGDLVAFLSLFAQLFGPL 274
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
576-787 |
1.97e-36 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 136.45 E-value: 1.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSPEKI----VLRNVSFTVPAGKTVAIVGPSGAGKSTimrLLfrfydvqtGAILidGQNIKLVQQQSLRKA 651
Cdd:cd03250 1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSS---LL--------SALL--GELEKLSGSVSVPGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 652 IGVVPQDTVLFNNTIFYNI----EYaklgasDEAVYEAA-RAADIHERILGFPEKYETKVGERGLRLSGGEKQRVAIART 726
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENIlfgkPF------DEERYEKViKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19527665 727 LLKAPIIVLLDEATSALDTHTERNI-----QAALARvcaNRTTIIVAHRLSTIIHADEILVLQQGS 787
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRHIfenciLGLLLN---NKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
559-808 |
2.68e-36 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 148.77 E-value: 2.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 559 EIVDAPGCSPLLTAGGGIEFSNVTFGYS---PekIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILI 635
Cdd:PTZ00243 1292 EPASPTSAAPHPVQAGSLVFEGVQMRYReglP--LVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRV 1369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 636 DGQNIKLVQQQSLRKAIGVVPQDTVLFNNTIFYNIEyAKLGASDEAVYEAARAADIHERILGFPEKYETKVGERGLRLSG 715
Cdd:PTZ00243 1370 NGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVD-PFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSV 1448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 716 GEKQRVAIARTLLK-APIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVAHRLSTIIHADEILVLQQGSIAERGRH 794
Cdd:PTZ00243 1449 GQRQLMCMARALLKkGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSP 1528
|
250
....*....|....
gi 19527665 795 EELVLREDGIYADM 808
Cdd:PTZ00243 1529 RELVMNRQSIFHSM 1542
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
576-797 |
5.92e-36 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 136.28 E-value: 5.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVT--FGyspEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNI--KLVQQQSLRKA 651
Cdd:COG1126 2 IEIENLHksFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 652 IGVVPQDTVLFNN-TIFYNIEYAK---LGAS-DEAVyeaARAADIHERIlGFPEKYETKVGErglrLSGGEKQRVAIART 726
Cdd:COG1126 79 VGMVFQQFNLFPHlTVLENVTLAPikvKKMSkAEAE---ERAMELLERV-GLADKADAYPAQ----LSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19527665 727 LLKAPIIVLLDEATSALDthTER-----NIQAALARvcANRTTIIVAHRLS---TIihADEILVLQQGSIAERGRHEEL 797
Cdd:COG1126 151 LAMEPKVMLFDEPTSALD--PELvgevlDVMRDLAK--EGMTMVVVTHEMGfarEV--ADRVVFMDGGRIVEEGPPEEF 223
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
576-800 |
5.96e-36 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 139.06 E-value: 5.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNV--TFGYSPEKIV-LRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKA- 651
Cdd:COG1135 2 IELENLskTFPTKGGPVTaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 652 --IGVVPQDTVLFNN-TIFYNIEYAkLgasdeavyeaaraadiheRILGFPEKY-ETKVGER----GLR---------LS 714
Cdd:COG1135 82 rkIGMIFQHFNLLSSrTVAENVALP-L------------------EIAGVPKAEiRKRVAELlelvGLSdkadaypsqLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 715 GGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVcaNR----TTIIVAHRLSTI--IhADEILVLQQGSI 788
Cdd:COG1135 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDI--NRelglTIVLITHEMDVVrrI-CDRVAVLENGRI 219
|
250
....*....|..
gi 19527665 789 AERGRHEELVLR 800
Cdd:COG1135 220 VEQGPVLDVFAN 231
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
576-797 |
1.89e-35 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 138.31 E-value: 1.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSpEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNI-KLVQQQslRKaIGV 654
Cdd:COG3842 6 LELENVSKRYG-DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVtGLPPEK--RN-VGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 655 VPQDTVLFNN-TIFYNIEYaklGASDEAVYEAARAADIHE--RILGFPEKYETKVGErglrLSGGEKQRVAIARTLLKAP 731
Cdd:COG3842 82 VFQDYALFPHlTVAENVAF---GLRMRGVPKAEIRARVAEllELVGLEGLADRYPHQ----LSGGQQQRVALARALAPEP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19527665 732 IIVLLDEATSALDTHTERNIQAALARVCANR--TTIIVAHRLS---TIihADEILVLQQGSIAERGRHEEL 797
Cdd:COG3842 155 RVLLLDEPLSALDAKLREEMREELRRLQRELgiTFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
576-805 |
2.01e-34 |
|
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: 131.92 E-value: 2.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKA---I 652
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrqI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 653 GVVPQDTVLFNN-TIFYNIEYAKLGAS----------DEAVYEAARAAdiHERiLGFPEKYETKVGErglrLSGGEKQRV 721
Cdd:cd03256 81 GMIFQQFNLIERlSVLENVLSGRLGRRstwrslfglfPKEEKQRALAA--LER-VGLLDKAYQRADQ----LSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 722 AIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCA--NRTTIIVAHRLSTII-HADEILVLQQGSIAERGRHEEL- 797
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGPPAELt 233
|
250
....*....|
gi 19527665 798 --VLREdgIY 805
Cdd:cd03256 234 deVLDE--IY 241
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
576-800 |
2.19e-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: 130.99 E-value: 2.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQS---LRKAI 652
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 653 GVVPQDT-VLFNNTIFYNIEYAkLGASDEAVYEAARAADIHERILGFPEKYETKVGErglrLSGGEKQRVAIARTLLKAP 731
Cdd:cd03292 81 GVVFQDFrLLPDRNVYENVAFA-LEVTGVPPREIRKRVPAALELVGLSHKHRALPAE----LSGGEQQRVAIARAIVNSP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19527665 732 IIVLLDEATSALDTHTERNIQAALARVCANRTTIIVAhrlstiIHADEILvlqqgsiaERGRHEELVLR 800
Cdd:cd03292 156 TILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA------THAKELV--------DTTRHRVIALE 210
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
576-788 |
3.23e-34 |
|
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: 128.67 E-value: 3.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYsPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLvQQQSLRKAIGVV 655
Cdd:cd03230 1 IEVRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 656 PQDTVLFNNtiFYNIEYaklgasdeavyeaaraadiherilgfpekyetkvgergLRLSGGEKQRVAIARTLLKAPIIVL 735
Cdd:cd03230 79 PEEPSLYEN--LTVREN--------------------------------------LKLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 19527665 736 LDEATSALDTHTERNIQAALARVCANRTTIIVA-HRLSTIIH-ADEILVLQQGSI 788
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEGKTILLSsHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
251-548 |
6.18e-34 |
|
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: 131.90 E-value: 6.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 251 VIVCIILLLAGRVIKLFLPIYRKKLVDSLTIAPIVFrwdfVLIYVALSFLqgGGTGSMGLFNNLRTFLWIRVQQYTTREI 330
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLS----LLLWIALLLL--LLALLRALLSYLRRYLAARLGQRVVFDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 331 EIELFRHLHQLSLRWHLQRKTGEVLRVMDRGTDSINNLLNYIVFSIAPTILDLLVAVAYFVYaFNWWFGLIVFLTMFLYI 410
Cdd:cd07346 75 RRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFY-LNWKLTLVALLLLPLYV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 411 ASTIAITEWRTKYQRRMnladNEQRARS----VDSLLNFETVKYYGAEHYEVDCYREAILKYQKEEFLSMLTLNMLNTAQ 486
Cdd:cd07346 154 LILRYFRRRIRKASREV----RESLAELsaflQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLI 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19527665 487 NIILCLGLLAGSLLCVYLVVHHQtLTVGDFVLFSTYLMELYMPLNWFGTYYRAIQKNFVDME 548
Cdd:cd07346 230 GLLTALGTALVLLYGGYLVLQGS-LTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLE 290
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
576-797 |
9.54e-34 |
|
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: 129.09 E-value: 9.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGY--SPekiVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNI-KLVQQQSLRKAI 652
Cdd:cd03224 1 LEVENLNAGYgkSQ---ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItGLPPHERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 653 GVVPQDTVLFNN-TIFYNIEyakLGASdeAVYEAARAADIhERILG-FPEKYEtKVGERGLRLSGGEKQRVAIARTLLKA 730
Cdd:cd03224 78 GYVPEGRRIFPElTVEENLL---LGAY--ARRRAKRKARL-ERVYElFPRLKE-RRKQLAGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19527665 731 PIIVLLDEATSALDTHTERNIQAALARVCANRTTII-VAHRLSTII-HADEILVLQQGSIAERGRHEEL 797
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILlVEQNARFALeIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
576-800 |
1.12e-33 |
|
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: 129.73 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGVV 655
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 656 PQDTVLFNN-TIFYNIEYA-KLGASDEAVYEaARA----ADIHERILGFPEKYETKvgerglrLSGGEKQRVAIARTLLK 729
Cdd:cd03295 81 IQQIGLFPHmTVEENIALVpKLLKWPKEKIR-ERAdellALVGLDPAEFADRYPHE-------LSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19527665 730 APIIVLLDEATSALDTHTERNIQAALARV--CANRTTIIVAHRLSTIIH-ADEILVLQQGSIAERGRHEELVLR 800
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLqqELGKTIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
576-788 |
1.24e-33 |
|
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: 128.80 E-value: 1.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSPEKiVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQ--SLRKAIG 653
Cdd:cd03262 1 IEIKNLHKSFGDFH-VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 654 VVPQDTVLFNN-TIFYNIEYAK---LGASDEAVYEAARaaDIHERIlGFPEKYETKVGErglrLSGGEKQRVAIARTLLK 729
Cdd:cd03262 80 MVFQQFNLFPHlTVLENITLAPikvKGMSKAEAEERAL--ELLEKV-GLADKADAYPAQ----LSGGQQQRVAIARALAM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19527665 730 APIIVLLDEATSALDTHTER---NIQAALARvcANRTTIIVAHRLSTIIH-ADEILVLQQGSI 788
Cdd:cd03262 153 NPKVMLFDEPTSALDPELVGevlDVMKDLAE--EGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
576-798 |
2.63e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 129.73 E-value: 2.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSP-EKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGV 654
Cdd:PRK13632 8 IKVENVSFSYPNsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 655 vpqdtvlfnntIFYNIEYAKLGASDEAvyeaaraaDIH---ERILGFPEK-------YETKVGERGL------RLSGGEK 718
Cdd:PRK13632 88 -----------IFQNPDNQFIGATVED--------DIAfglENKKVPPKKmkdiiddLAKKVGMEDYldkepqNLSGGQK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 719 QRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALA--RVCANRTTIIVAHRLSTIIHADEILVLQQGSIAERGRHEE 796
Cdd:PRK13632 149 QRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVdlRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKE 228
|
..
gi 19527665 797 LV 798
Cdd:PRK13632 229 IL 230
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
576-792 |
4.25e-33 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 126.51 E-value: 4.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFG-----YSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLL--FRFYDVQTGAILIDGQNIKLvqqQSL 648
Cdd:cd03213 4 LSFRNLTVTvksspSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDK---RSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 649 RKAIGVVPQDTVLFNN-TIFYNIEY-AKLgasdeavyeaaraadiherilgfpekyetkvgeRGLrlSGGEKQRVAIART 726
Cdd:cd03213 81 RKIIGYVPQDDILHPTlTVRETLMFaAKL---------------------------------RGL--SGGERKRVSIALE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19527665 727 LLKAPIIVLLDEATSALDTHTERNIQAALARVC-ANRTTIIVAHRLSTIIHA--DEILVLQQGSIAERG 792
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAdTGRTIICSIHQPSSEIFElfDKLLLLSQGRVIYFG 194
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
591-796 |
9.93e-33 |
|
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: 126.68 E-value: 9.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 591 VLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQslRKAIGVVPQDTVLFNN-TIFYN 669
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPHmTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 670 IEYaklGASDEAVYEAARAADIHE--RILGFPEKYETKVGerglRLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHT 747
Cdd:cd03299 92 IAY---GLKKRKVDKKEIERKVLEiaEMLGIDHLLNRKPE----TLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 19527665 748 ERNIQAALARVC-ANRTTII-VAHRLSTI-IHADEILVLQQGSIAERGRHEE 796
Cdd:cd03299 165 KEKLREELKKIRkEFGVTVLhVTHDFEEAwALADKVAIMLNGKLIQVGKPEE 216
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
576-804 |
1.48e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 127.56 E-value: 1.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGY-SPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGV 654
Cdd:PRK13648 8 IVFKNVSFQYqSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 655 VPQ--DTVLFNNTIFYNIEYaklGASDEAV-YEaaraaDIHERIlgfPEKYE-----TKVGERGLRLSGGEKQRVAIART 726
Cdd:PRK13648 88 VFQnpDNQFVGSIVKYDVAF---GLENHAVpYD-----EMHRRV---SEALKqvdmlERADYEPNALSGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 727 LLKAPIIVLLDEATSALDTHTERNIQAALARVCANR--TTIIVAHRLSTIIHADEILVLQQGSIAERGRHEELVLREDGI 804
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEEL 236
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
576-771 |
6.74e-32 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 125.15 E-value: 6.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSpEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQ-----TGAILIDGQNI--KLVQQQSL 648
Cdd:COG1117 12 IEVRNLNVYYG-DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIpgarvEGEILLDGEDIydPDVDVVEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 649 RKAIGVVPQDTVLFNNTIFYNIEY----------AKLgasDEAVYEAARAADIHErilgfpekyETK--VGERGLRLSGG 716
Cdd:COG1117 91 RRRVGMVFQKPNPFPKSIYDNVAYglrlhgikskSEL---DEIVEESLRKAALWD---------EVKdrLKKSALGLSGG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 19527665 717 EKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVAHRL 771
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNM 213
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
352-837 |
9.86e-31 |
|
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: 130.84 E-value: 9.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 352 GEVLRVMDRGTDSINNLLNYI--VFSiAPtiLDLLVAVaYFVyafnwWFGL-------IVFLTMFLYIASTIAItEWRTK 422
Cdd:TIGR00957 415 GEIVNLMSVDAQRFMDLATYInmIWS-AP--LQVILAL-YFL-----WLNLgpsvlagVAVMVLMVPLNAVMAM-KTKTY 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 423 YQRRMNLADNeqRARSVDSLLN-FETVKYYGAEHyevdCYREAILKYQKEEFLSMLTLNMLNTAQNII-LCLG-LLAGSL 499
Cdd:TIGR00957 485 QVAHMKSKDN--RIKLMNEILNgIKVLKLYAWEL----AFLDKVEGIRQEELKVLKKSAYLHAVGTFTwVCTPfLVALIT 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 500 LCVYLVVHHQTLTVGDFVLFSTYLME-LYMPLNWFGTYYRAIQKNFVDMENMFDLLKEEEEIVDAPGCSPLLTAGG-GIE 577
Cdd:TIGR00957 559 FAVYVTVDENNILDAEKAFVSLALFNiLRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPGEGnSIT 638
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 578 FSNVTFGYS-PEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGqniklvqqqslrkAIGVVP 656
Cdd:TIGR00957 639 VHNATFTWArDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVP 705
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 657 QDTVLFNNTIFYNIEYAKlgASDEAVYEA-----ARAADIHerILgfPEKYETKVGERGLRLSGGEKQRVAIARTLLKAP 731
Cdd:TIGR00957 706 QQAWIQNDSLRENILFGK--ALNEKYYQQvleacALLPDLE--IL--PSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNA 779
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 732 IIVLLDEATSALDTHTERNIQAAL---ARVCANRTTIIVAHRLSTIIHADEILVLQQGSIAERGRHEELVLReDGIYADM 808
Cdd:TIGR00957 780 DIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQR-DGAFAEF 858
|
490 500 510
....*....|....*....|....*....|
gi 19527665 809 wqqqLKNL-DAEQSGGSDNGDASAESGSEK 837
Cdd:TIGR00957 859 ----LRTYaPDEQQGHLEDSWTALVSGEGK 884
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
576-800 |
1.39e-30 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 123.76 E-value: 1.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNV--TF-GYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKA- 651
Cdd:PRK11153 2 IELKNIskVFpQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 652 --IGVVPQDtvlFN----NTIFYNIEYAklgasdeavYEAA--RAADIHERIL------GFPEKYETKVGErglrLSGGE 717
Cdd:PRK11153 82 rqIGMIFQH---FNllssRTVFDNVALP---------LELAgtPKAEIKARVTellelvGLSDKADRYPAQ----LSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 718 KQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVcaNR----TTIIVAHRLSTIIH-ADEILVLQQGSIAERG 792
Cdd:PRK11153 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDI--NRelglTIVLITHEMDVVKRiCDRVAVIDAGRLVEQG 223
|
....*...
gi 19527665 793 RHEELVLR 800
Cdd:PRK11153 224 TVSEVFSH 231
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
576-792 |
2.75e-30 |
|
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: 119.13 E-value: 2.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSPEKIVLrnvSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQslRKAIGVV 655
Cdd:cd03298 1 VRLDKIRFSYGEQPMHF---DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 656 PQDTVLFNN-TIFYNIEYA-----KLGASD-EAVYEAARAADIHERILGFPEKyetkvgerglrLSGGEKQRVAIARTLL 728
Cdd:cd03298 76 FQENNLFAHlTVEQNVGLGlspglKLTAEDrQAIEVALARVGLAGLEKRLPGE-----------LSGGERQRVALARVLV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19527665 729 KAPIIVLLDEATSALDTHTERNIQAALARVCANR--TTIIVAHRLSTIIH-ADEILVLQQGSIAERG 792
Cdd:cd03298 145 RDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
350-788 |
4.62e-30 |
|
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: 128.49 E-value: 4.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 350 KTGEVLRVMDRGTDSINNLLNYIVFSIAPTILDLLVAVAyfvyafnwwfgLIVFLTMFLYIAS---TIAITEWRTKYQRR 426
Cdd:TIGR01271 980 KAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIF-----------VVSVLQPYIFIAAipvAVIFIMLRAYFLRT 1048
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 427 -MNLADNEQRARS------VDSLLNFETVKYYGAEHYEVDCYREAILKYQKEEFLSMLTLNMLNTAQNIILCLGLLAgsl 499
Cdd:TIGR01271 1049 sQQLKQLESEARSpifshlITSLKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDIIFVFFFIA--- 1125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 500 lCVYLVVHHQTLTVGDFVLFSTYLMELYMPLNW-------FGTYYRAIQKNFvdmeNMFDLLKEEEE------------- 559
Cdd:TIGR01271 1126 -VTFIAIGTNQDGEGEVGIILTLAMNILSTLQWavnssidVDGLMRSVSRVF----KFIDLPQEEPRpsggggkyqlstv 1200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 560 -IVDAPGCSPLLTAGGGIEFSNVTFGYSPE-KIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQtGAILIDG 637
Cdd:TIGR01271 1201 lVIENPHAQKCWPSGGQMDVQGLTAKYTEAgRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDG 1279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 638 QNIKLVQQQSLRKAIGVVPQDTVLFNNTIFYNIE-YAKLgaSDEAVYEAARAADIHERILGFPEKYETKVGERGLRLSGG 716
Cdd:TIGR01271 1280 VSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDpYEQW--SDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNG 1357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19527665 717 EKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVAHRLSTIIHADEILVLQQGSI 788
Cdd:TIGR01271 1358 HKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSV 1429
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
576-804 |
8.79e-30 |
|
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: 119.07 E-value: 8.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSP-EKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQ-QSLRKAIG 653
Cdd:TIGR04520 1 IEVENVSFSYPEsEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENlWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 654 VVPQ------------DTVLF---NNtifyNIEYAKLgasDEAVYEAARAADIheriLGFpEKYETKvgerglRLSGGEK 718
Cdd:TIGR04520 81 MVFQnpdnqfvgatveDDVAFgleNL----GVPREEM---RKRVDEALKLVGM----EDF-RDREPH------LLSGGQK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 719 QRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCA--NRTTIIVAHRLSTIIHADEILVLQQGSIAERGRHEE 796
Cdd:TIGR04520 143 QRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeeGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPRE 222
|
....*...
gi 19527665 797 LVLREDGI 804
Cdd:TIGR04520 223 IFSQVELL 230
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
576-792 |
9.74e-30 |
|
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: 117.29 E-value: 9.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYsPEKIVLRNVSFTVPAGKTvAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKlVQQQSLRKAIGVV 655
Cdd:cd03264 1 LQLENLTKRY-GKKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL-KQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 656 PQDTVLFNN-TIFYNIEYAklgasdeAVYEAARAADIHERI------LGFPEKYETKVGErglrLSGGEKQRVAIARTLL 728
Cdd:cd03264 78 PQEFGVYPNfTVREFLDYI-------AWLKGIPSKEVKARVdevlelVNLGDRAKKKIGS----LSGGMRRRVGIAQALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19527665 729 KAPIIVLLDEATSALDT---HTERNIqaaLARVCANRTTIIVAHRLSTI-IHADEILVLQQGSIAERG 792
Cdd:cd03264 147 GDPSILIVDEPTAGLDPeerIRFRNL---LSELGEDRIVILSTHIVEDVeSLCNQVAVLNKGKLVFEG 211
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
575-797 |
1.04e-29 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 121.41 E-value: 1.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 575 GIEFSNVTFGYSPEKiVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLL--FRFYDvqTGAILIDGQ--NIKL-VQQqslR 649
Cdd:COG1118 2 SIEVRNISKRFGSFT-LLDDVSLEIASGELVALLGPSGSGKTTLLRIIagLETPD--SGRIVLNGRdlFTNLpPRE---R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 650 KaIGVVPQDTVLFNN-TIFYNIEYaklGASDEAVYEAARAADIHE-----RILGFPEKYETKvgerglrLSGGEKQRVAI 723
Cdd:COG1118 76 R-VGFVFQHYALFPHmTVAENIAF---GLRVRPPSKAEIRARVEEllelvQLEGLADRYPSQ-------LSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 724 ARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCA--NRTTIIVAH------RLstiihADEILVLQQGSIAERGRHE 795
Cdd:COG1118 145 ARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDelGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPD 219
|
..
gi 19527665 796 EL 797
Cdd:COG1118 220 EV 221
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
576-802 |
1.33e-29 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 118.29 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSpEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGVV 655
Cdd:COG4559 2 LEAENLSVRLG-GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 656 PQDTVL-FNNTIfynIEYAKLGAS---------DEAVYEAARAADiherILGFPEK-YETkvgerglrLSGGEKQRVAIA 724
Cdd:COG4559 81 PQHSSLaFPFTV---EEVVALGRAphgssaaqdRQIVREALALVG----LAHLAGRsYQT--------LSGGEQQRVQLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 725 RTL--LKAPI-----IVLLDEATSALDTHTERNIQAALARVCANRTTII-VAHRLS-TIIHADEILVLQQGSIAERGRHE 795
Cdd:COG4559 146 RVLaqLWEPVdggprWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVaVLHDLNlAAQYADRILLLHQGRLVAQGTPE 225
|
....*..
gi 19527665 796 ElVLRED 802
Cdd:COG4559 226 E-VLTDE 231
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
576-801 |
1.56e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 119.00 E-value: 1.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSP----EKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNI--KLVQQQSLR 649
Cdd:PRK13637 3 IKIENLTHIYMEgtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 650 KAIGVVPQ--DTVLFNNTIFYNIEYA--KLGASDEAVYEAARAAdihERILGFPekYETKVGERGLRLSGGEKQRVAIAR 725
Cdd:PRK13637 83 KKVGLVFQypEYQLFEETIEKDIAFGpiNLGLSEEEIENRVKRA---MNIVGLD--YEDYKDKSPFELSGGQKRRVAIAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 726 TLLKAPIIVLLDEATSALDTHTERNIqaaLARVCA-----NRTTIIVAHRLSTIIH-ADEILVLQQGSIAERGRHEElVL 799
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPKGRDEI---LNKIKElhkeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE-VF 233
|
..
gi 19527665 800 RE 801
Cdd:PRK13637 234 KE 235
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
576-797 |
1.70e-29 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 120.56 E-value: 1.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSpEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGqniKLVQQQSLRK-AIGV 654
Cdd:COG3839 4 LELENVSKSYG-GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG---RDVTDLPPKDrNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 655 VPQDTVLFNN-TIFYNIEY----AKLGAS--DEAVYEAAraadiheRILGFPEKYETKVGErglrLSGGEKQRVAIARTL 727
Cdd:COG3839 80 VFQSYALYPHmTVYENIAFplklRKVPKAeiDRRVREAA-------ELLGLEDLLDRKPKQ----LSGGQRQRVALGRAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 728 LKAPIIVLLDEATSALDTH------TE-RNIQAALarvcaNRTTIIVAHRLS---TIihADEILVLQQGSIAERGRHEEL 797
Cdd:COG3839 149 VREPKVFLLDEPLSNLDAKlrvemrAEiKRLHRRL-----GTTTIYVTHDQVeamTL--ADRIAVMNDGRIQQVGTPEEL 221
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
589-802 |
3.43e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 117.18 E-value: 3.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 589 KIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGVVPQDTVL-FNNTIf 667
Cdd:PRK13548 15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTV- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 668 ynIEYAKLGASDeavYEAARAADihERIlgfPEKYETKVGERGLR------LSGGEKQRVAIARTLL------KAPIIVL 735
Cdd:PRK13548 94 --EEVVAMGRAP---HGLSRAED--DAL---VAAALAQVDLAHLAgrdypqLSGGEQQRVQLARVLAqlwepdGPPRWLL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19527665 736 LDEATSALD-THTERNIQaaLARVCANR---TTIIVAHRLS-TIIHADEILVLQQGSIAERGRHEElVLRED 802
Cdd:PRK13548 164 LDEPTSALDlAHQHHVLR--LARQLAHErglAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAE-VLTPE 232
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
576-797 |
3.62e-29 |
|
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: 116.57 E-value: 3.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSpEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQslRKAIGVV 655
Cdd:cd03300 1 IELENVSKFYG-GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 656 PQDTVLFNN-TIFYNIEYA-KLGASDEAVYEAARAADIHE-RILGFPEKYETKvgerglrLSGGEKQRVAIARTLLKAPI 732
Cdd:cd03300 78 FQNYALFPHlTVFENIAFGlRLKKLPKAEIKERVAEALDLvQLEGYANRKPSQ-------LSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19527665 733 IVLLDEATSALDTHTERNIQAALARVCANR--TTIIVAHRLS-TIIHADEILVLQQGSIAERGRHEEL 797
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKELgiTFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
577-802 |
4.63e-29 |
|
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: 116.23 E-value: 4.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 577 EFSNVTFGYsPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNI-KLVQQQSLRKAIGVV 655
Cdd:COG0410 5 EVENLHAGY-GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDItGLPPHRIARLGIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 656 PQDTVLFNN-TIFYNIEyakLGASdeAVYEAARAADIHERILG-FPEKYEtKVGERGLRLSGGEKQRVAIARTLLKAPII 733
Cdd:COG0410 84 PEGRRIFPSlTVEENLL---LGAY--ARRDRAEVRADLERVYElFPRLKE-RRRQRAGTLSGGEQQMLAIGRALMSRPKL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19527665 734 VLLDEATSALDTHTERNIQAALARVCANRTTIIV----AHRLSTIihADEILVLQQGSIAERGRHEELVLRED 802
Cdd:COG0410 158 LLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
591-787 |
6.36e-29 |
|
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: 115.61 E-value: 6.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 591 VLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILI--DGQNIKLVQ---QQSL---RKAIGVVPQ----- 657
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQaspREILalrRRTIGYVSQflrvi 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 658 ------DTV---LFnntifynieyaKLGASDEavyEA-ARAADIHERiLGFPEkyetkvgerglRL--------SGGEKQ 719
Cdd:COG4778 106 prvsalDVVaepLL-----------ERGVDRE---EArARARELLAR-LNLPE-----------RLwdlppatfSGGEQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 720 RVAIARTLLKAPIIVLLDEATSALDTHTERN----IQAALARVCAnrttiIVAhrlstIIH--------ADEILVLQQGS 787
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRAVvvelIEEAKARGTA-----IIG-----IFHdeevreavADRVVDVTPFS 229
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
588-795 |
1.17e-28 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 114.81 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 588 EKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGVVPQDTVLFNNTIF 667
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 668 YNIEYAKLgASDEAVYEAARAADIHEriLGFPEKYETK-VGErglrLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTH 746
Cdd:PRK10247 99 DNLIFPWQ-IRNQQPDPAIFLDDLER--FALPDTILTKnIAE----LSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 19527665 747 TERNIQAALARVCANRTTII--VAHRLSTIIHADEILVLQ-QGSIAERGRHE 795
Cdd:PRK10247 172 NKHNVNEIIHRYVREQNIAVlwVTHDKDEINHADKVITLQpHAGEMQEARYE 223
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
574-788 |
2.31e-28 |
|
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: 115.34 E-value: 2.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 574 GGIEFSNVTFGYSPE-KIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQtGAILIDGQNIKLVQQQSLRKAI 652
Cdd:cd03289 1 GQMTVKDLTAKYTEGgNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 653 GVVPQDTVLFNNTIFYNIE-YAKLgaSDEAVYEAARAADIHERILGFPEKYETKVGERGLRLSGGEKQRVAIARTLLKAP 731
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDpYGKW--SDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 19527665 732 IIVLLDEATSALDTHTERNIQAALARVCANRTTIIVAHRLSTIIHADEILVLQQGSI 788
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
576-797 |
2.76e-28 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 113.70 E-value: 2.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSPEKIvlrNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIklvqqqsLRKAIGVV 655
Cdd:COG3840 2 LRLDDLTYRYGDFPL---RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL-------TALPPAER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 656 P-----QDTVLFNN-TIFYNIEYA-----KLGASD-EAVYEAARaadiherilgfpekyetKVGERGL------RLSGGE 717
Cdd:COG3840 72 PvsmlfQENNLFPHlTVAQNIGLGlrpglKLTAEQrAQVEQALE-----------------RVGLAGLldrlpgQLSGGQ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 718 KQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANR--TTIIVAHRLSTIIH-ADEILVLQQGSIAERGRH 794
Cdd:COG3840 135 RQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHDPEDAARiADRVLLVADGRIAADGPT 214
|
...
gi 19527665 795 EEL 797
Cdd:COG3840 215 AAL 217
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
592-798 |
2.81e-28 |
|
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: 115.05 E-value: 2.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 592 LRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSL----RKAIGVVPQDTVLF-NNTI 666
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 667 FYNIEYA-KLGASDEAVYEaARAADIHERI--LGFPEKYetkVGErglrLSGGEKQRVAIARTLLKAPIIVLLDEATSAL 743
Cdd:cd03294 120 LENVAFGlEVQGVPRAERE-ERAAEALELVglEGWEHKY---PDE----LSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 19527665 744 DTHTERNIQAALARVCAN--RTTIIVAHRLSTIIH-ADEILVLQQGSIAERGRHEELV 798
Cdd:cd03294 192 DPLIRREMQDELLRLQAElqKTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
580-767 |
5.54e-28 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 111.97 E-value: 5.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 580 NVTFGYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKlvqQQSLRKAIGVVPQDT 659
Cdd:cd03226 4 NISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK---AKERRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 660 --VLFNNTIfynieYAKLGASDEAVYEA-ARAADIHER--ILGFPEKYEtkvgergLRLSGGEKQRVAIARTLLKAPIIV 734
Cdd:cd03226 81 dyQLFTDSV-----REELLLGLKELDAGnEQAETVLKDldLYALKERHP-------LSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190
....*....|....*....|....*....|...
gi 19527665 735 LLDEATSALDTHTERNIqAALARVCANRTTIIV 767
Cdd:cd03226 149 IFDEPTSGLDYKNMERV-GELIRELAAQGKAVI 180
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
576-780 |
6.56e-28 |
|
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: 111.80 E-value: 6.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSpEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLvQQQSLRKAIGVV 655
Cdd:COG4133 3 LEAENLSCRRG-ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 656 PQDTVLFNN-TIFYNIE-YAKL---GASDEAVYEAARAADIHERIlgfpekyETKVGerglRLSGGEKQRVAIARTLLKA 730
Cdd:COG4133 81 GHADGLKPElTVRENLRfWAALyglRADREAIDEALEAVGLAGLA-------DLPVR----QLSAGQKRRVALARLLLSP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 19527665 731 PIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVA-HRLSTIIHADEI 780
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVL 200
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
576-788 |
6.95e-28 |
|
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: 112.21 E-value: 6.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGY-SPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIkLVQQQSLRKAIGV 654
Cdd:cd03263 1 LQIRNLTKTYkKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 655 VPQDTVLFNN-TIFYNIE-YAKL-GASDEavyEAARAADIHERILGFPEKYETKVGErglrLSGGEKQRVAIARTLLKAP 731
Cdd:cd03263 80 CPQFDALFDElTVREHLRfYARLkGLPKS---EIKEEVELLLRVLGLTDKANKRART----LSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 19527665 732 IIVLLDEATSALDTHTERNIQAALARVCANRTTIIVAHRLSTI-IHADEILVLQQGSI 788
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAeALCDRIAIMSDGKL 210
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
575-797 |
1.07e-27 |
|
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: 112.43 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 575 GIEFSNVT--FGYSPekiVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNiklVQQQSLRK-A 651
Cdd:cd03296 2 SIEVRNVSkrFGDFV---ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGED---ATDVPVQErN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 652 IGVVPQDTVLFNN-TIFYNIEYA-KLGASDEAVYEAARAADIHE-----RILGFPEKYETKvgerglrLSGGEKQRVAIA 724
Cdd:cd03296 76 VGFVFQHYALFRHmTVFDNVAFGlRVKPRSERPPEAEIRAKVHEllklvQLDWLADRYPAQ-------LSGGQRQRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19527665 725 RTLLKAPIIVLLDEATSALDTHTERNIQAALARVC--ANRTTIIVAHRLSTIIH-ADEILVLQQGSIAERGRHEEL 797
Cdd:cd03296 149 RALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHdeLHVTTVFVTHDQEEALEvADRVVVMNKGRIEQVGTPDEV 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
576-798 |
1.19e-27 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 112.11 E-value: 1.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVT--FGYSPekiVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIK--LVQQQSLRKA 651
Cdd:PRK09493 2 IEFKNVSkhFGPTQ---VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 652 IGVVPQDTVLFNN-TIFYNIEYAKL---GASDEAVYEAARAadiherILGfpekyetKVG--ERG----LRLSGGEKQRV 721
Cdd:PRK09493 79 AGMVFQQFYLFPHlTALENVMFGPLrvrGASKEEAEKQARE------LLA-------KVGlaERAhhypSELSGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 722 AIARTLLKAPIIVLLDEATSALDT---HTERNIQAALARvcANRTTIIVAHRLSTIIH-ADEILVLQQGSIAERGRHEEL 797
Cdd:PRK09493 146 AIARALAVKPKLMLFDEPTSALDPelrHEVLKVMQDLAE--EGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVL 223
|
.
gi 19527665 798 V 798
Cdd:PRK09493 224 I 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
580-797 |
4.15e-27 |
|
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: 112.84 E-value: 4.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 580 NVTFgYSPEKIV--LRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYD---VQTGAILIDGQNIKLVQQQSLRKA--- 651
Cdd:COG0444 8 KVYF-PTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELRKIrgr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 652 -IGVVPQD--TVLfnN---TIFYNIE---YAKLGASDEAVYEaaRAADIHERI-LGFPEKYetkvgergLR-----LSGG 716
Cdd:COG0444 87 eIQMIFQDpmTSL--NpvmTVGDQIAeplRIHGGLSKAEARE--RAIELLERVgLPDPERR--------LDrypheLSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 717 EKQRVAIARTLLKAPIIVLLDEATSALD-ThternIQAA----LARVCANR-TTII-VAHRLSTIIH-ADEILVLQQGSI 788
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDvT-----IQAQilnlLKDLQRELgLAILfITHDLGVVAEiADRVAVMYAGRI 229
|
....*....
gi 19527665 789 AERGRHEEL 797
Cdd:COG0444 230 VEEGPVEEL 238
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
576-789 |
1.33e-26 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 106.74 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSPEKiVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQ-QQSLRKAIGV 654
Cdd:cd03216 1 LELRGITKRFGGVK-ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 655 VPQdtvlfnntifynieyaklgasdeavyeaaraadiherilgfpekyetkvgerglrLSGGEKQRVAIARTLLKAPIIV 734
Cdd:cd03216 80 VYQ-------------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 19527665 735 LLDEATSALDTHTERNIQAALARVCANRTTII-VAHRLSTIIH-ADEILVLQQGSIA 789
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIfISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
594-792 |
1.45e-26 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 108.15 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 594 NVSFTVPAGkTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDG-------QNIKLVQQQslrKAIGVVPQDTVLFNN-T 665
Cdd:cd03297 16 KIDFDLNEE-VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKINLPPQQ---RKIGLVFQQYALFPHlN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 666 IFYNIEYAKLGASDEAvyEAARAADIHERiLGFpekyeTKVGERG-LRLSGGEKQRVAIARTLLKAPIIVLLDEATSALD 744
Cdd:cd03297 92 VRENLAFGLKRKRNRE--DRISVDELLDL-LGL-----DHLLNRYpAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 19527665 745 THTERNIQAALARVCA--NRTTIIVAHRLSTIIH-ADEILVLQQGSIAERG 792
Cdd:cd03297 164 RALRLQLLPELKQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
585-791 |
1.63e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 109.48 E-value: 1.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 585 YSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQ-----TGAILIDGQNI--KLVQQQSLRKAIGVVPQ 657
Cdd:PRK14239 14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysPRTDTVDLRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 658 DTVLFNNTIFYNIEY----------AKLgasDEAVYEAARAADIHERIlgfpekyETKVGERGLRLSGGEKQRVAIARTL 727
Cdd:PRK14239 94 QPNPFPMSIYENVVYglrlkgikdkQVL---DEAVEKSLKGASIWDEV-------KDRLHDSALGLSGGQQQRVCIARVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19527665 728 LKAPIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVAHRlstiihadeilvLQQGS-IAER 791
Cdd:PRK14239 164 ATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRS------------MQQASrISDR 216
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
576-792 |
1.76e-26 |
|
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: 108.22 E-value: 1.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSPEK---IVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGqnIKLVQQ-QSLRKA 651
Cdd:cd03266 2 ITADALTKRFRDVKktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEpAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 652 IGVVPQDTVLfnntifynieYAKLGASDEAVYEAA----RAADIHERI------LGFPEKYETKVGErglrLSGGEKQRV 721
Cdd:cd03266 80 LGFVSDSTGL----------YDRLTARENLEYFAGlyglKGDELTARLeeladrLGMEELLDRRVGG----FSTGMRQKV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19527665 722 AIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVA-HRLSTIIH-ADEILVLQQGSIAERG 792
Cdd:cd03266 146 AIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
576-797 |
2.53e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 113.96 E-value: 2.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSPEKiVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQ-QQSLRKAIGV 654
Cdd:COG1129 5 LEMRGISKSFGGVK-ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 655 VPQDTVLFNN-TIFYNI----EYAKLGASDEAvYEAARAADIHERiLGFPEKYETKVGErglrLSGGEKQRVAIARTLLK 729
Cdd:COG1129 84 IHQELNLVPNlSVAENIflgrEPRRGGLIDWR-AMRRRARELLAR-LGLDIDPDTPVGD----LSVAQQQLVEIARALSR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19527665 730 APIIVLLDEATSALdthTERNIQ---AALARVCANRTTII-VAHRLSTII-HADEILVLQQGSIAERGRHEEL 797
Cdd:COG1129 158 DARVLILDEPTASL---TEREVErlfRIIRRLKAQGVAIIyISHRLDEVFeIADRVTVLRDGRLVGTGPVAEL 227
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
576-802 |
2.55e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 109.44 E-value: 2.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGVV 655
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 656 PQ--DTVLFNNTIFYNIEYA----KLGAS--DEAVYEAARAADIHErilgFPEK--YEtkvgerglrLSGGEKQRVAIAR 725
Cdd:PRK13647 85 FQdpDDQVFSSTVWDDVAFGpvnmGLDKDevERRVEEALKAVRMWD----FRDKppYH---------LSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 726 TLLKAPIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVA-HRLSTIIH-ADEILVLQQG-SIAERGRheELVLRED 802
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGrVLAEGDK--SLLTDED 229
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
576-792 |
3.73e-26 |
|
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: 106.96 E-value: 3.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYsPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQslRKAIGVV 655
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 656 PQDTVLF-NNTIFYNIEYA-KLGAS-----DEAVYEAARAADIHERILGFPEkyetkvgerglRLSGGEKQRVAIARTLL 728
Cdd:cd03301 78 FQNYALYpHMTVYDNIAFGlKLRKVpkdeiDERVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRAIV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19527665 729 KAPIIVLLDEATSALDTHTERNIQAALARVCAN--RTTIIVAH-RLSTIIHADEILVLQQGSIAERG 792
Cdd:cd03301 147 REPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlgTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
577-797 |
1.20e-25 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 106.07 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 577 EFSNVTFGYSpEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNI-KLVQQQSLRKAIGVV 655
Cdd:TIGR03410 2 EVSNLNVYYG-QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDItKLPPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 656 PQDTVLFNN-TIFYNIEyakLGASDEAVYEAARAADIHERilgFPEKYETKvGERGLRLSGGEKQRVAIARTLLKAPIIV 734
Cdd:TIGR03410 81 PQGREIFPRlTVEENLL---TGLAALPRRSRKIPDEIYEL---FPVLKEML-GRRGGDLSGGQQQQLAIARALVTRPKLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19527665 735 LLDEATSALDTHTERNIQAALARVCANR--TTIIVAHRLSTIIH-ADEILVLQQGSIAERGRHEEL 797
Cdd:TIGR03410 154 LLDEPTEGIQPSIIKDIGRVIRRLRAEGgmAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
576-802 |
1.34e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 107.58 E-value: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGVV 655
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 656 PQ--DTVLFNNTIFYNIEYA--KLGASDEAVyeaARAADIHERILGFpEKYETKVGErglRLSGGEKQRVAIARTLLKAP 731
Cdd:PRK13652 84 FQnpDDQIFSPTVEQDIAFGpiNLGLDEETV---AHRVSSALHMLGL-EELRDRVPH---HLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19527665 732 IIVLLDEATSALDTHTERNIQAALARVCAN--RTTIIVAHRLSTIIH-ADEILVLQQGSIAERGRHEELVLRED 802
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQPD 230
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
575-795 |
1.49e-25 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 106.25 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 575 GIEFSNVTFGYSPEKiVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQ------QSL 648
Cdd:COG4161 2 SIQLKNINCFYGSHQ-ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKpsekaiRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 649 RKAIGVV-------PQDTVLfNNTIFYNIEYAKLgASDEAVYEAA------RAADIHERilgFPekyetkvgergLRLSG 715
Cdd:COG4161 81 RQKVGMVfqqynlwPHLTVM-ENLIEAPCKVLGL-SKEQAREKAMkllarlRLTDKADR---FP-----------LHLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 716 GEKQRVAIARTLLKAPIIVLLDEATSALD---THTERNIQAALARVcaNRTTIIVAHRLSTIIH-ADEILVLQQGSIAER 791
Cdd:COG4161 145 GQQQRVAIARALMMEPQVLLFDEPTAALDpeiTAQVVEIIRELSQT--GITQVIVTHEVEFARKvASQVVYMEKGRIIEQ 222
|
....
gi 19527665 792 GRHE 795
Cdd:COG4161 223 GDAS 226
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
591-790 |
1.61e-25 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 105.98 E-value: 1.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 591 VLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNI-KLVQQQSLRKAIGVVPQDTVLFNN-TIFY 668
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItGLPPHEIARLGIGRTFQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 669 NIE---YAKLGASDEAVYEAARAADIHERI------LGFPEKYETKVGErglrLSGGEKQRVAIARTLLKAPIIVLLDEA 739
Cdd:cd03219 95 NVMvaaQARTGSGLLLARARREEREARERAeellerVGLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 19527665 740 TSALdTHTERNIQAALAR--VCANRTTIIVAHRLSTII-HADEILVLQQGS-IAE 790
Cdd:cd03219 171 AAGL-NPEETEELAELIRelRERGITVLLVEHDMDVVMsLADRVTVLDQGRvIAE 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
576-786 |
1.74e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 107.22 E-value: 1.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSP----EKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQ----QS 647
Cdd:PRK13641 3 IKFENVDYIYSPgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnknlKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 648 LRKAIGVVPQ--DTVLFNNTIFYNIEYA--KLGASDEavyEAARAADIHERILGFPEKYETKvgeRGLRLSGGEKQRVAI 723
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGpkNFGFSED---EAKEKALKWLKKVGLSEDLISK---SPFELSGGQMRRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19527665 724 ARTLLKAPIIVLLDEATSALDTHTERNI-QAALARVCANRTTIIVAHRLSTII-HADEILVLQQG 786
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMmQLFKDYQKAGHTVILVTHNMDDVAeYADDVLVLEHG 221
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
595-802 |
2.39e-25 |
|
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: 108.66 E-value: 2.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 595 VSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNI----KLVQQQSLRKAIGVVPQDTVLFNN-TIFYN 669
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrKGIFLPPEKRRIGYVFQEARLFPHlSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 670 IEYaklGASDEAVYEAARAADIHERILGFpekyETKVGERGLRLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTER 749
Cdd:TIGR02142 96 LRY---GMKRARPSERRISFERVIELLGI----GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 19527665 750 NIQAALARVCA--NRTTIIVAHRLSTIIH-ADEILVLQQGSIAERGRHEELVLRED 802
Cdd:TIGR02142 169 EILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
575-797 |
3.13e-25 |
|
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: 106.48 E-value: 3.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 575 GIEFSNVTFGYSPekiVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQniklvqqqslrkaIGV 654
Cdd:cd03291 39 NLFFSNLCLVGAP---VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 655 VPQDTVLFNNTIFYNIEYaklGAS-DEAVYEAA-RAADIHERILGFPEKYETKVGERGLRLSGGEKQRVAIARTLLKAPI 732
Cdd:cd03291 103 SSQFSWIMPGTIKENIIF---GVSyDEYRYKSVvKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDAD 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19527665 733 IVLLDEATSALDTHTERNI-QAALARVCANRTTIIVAHRLSTIIHADEILVLQQGSIAERGRHEEL 797
Cdd:cd03291 180 LYLLDSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
580-771 |
3.54e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 105.63 E-value: 3.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 580 NVTFGYSpekIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGA-----ILIDGQNI--KLVQQQSLRKAI 652
Cdd:PRK14243 17 NVYYGSF---LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFrvegkVTFHGKNLyaPDVDPVEVRRRI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 653 GVVPQDTVLFNNTIFYNIEY-AKL----GASDEAVYEAARAADIHERIlgfpekyETKVGERGLRLSGGEKQRVAIARTL 727
Cdd:PRK14243 94 GMVFQKPNPFPKSIYDNIAYgARIngykGDMDELVERSLRQAALWDEV-------KDKLKQSGLSLSGGQQQRLCIARAI 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 19527665 728 LKAPIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVAHRL 771
Cdd:PRK14243 167 AVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
589-831 |
4.17e-25 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 112.56 E-value: 4.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 589 KIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDgqniklvqqqslrKAIGVVPQDTVLFNNTIFY 668
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 669 NIEYakLGASDEA-VYEAARAADIHERILGFPEKYETKVGERGLRLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHT 747
Cdd:PTZ00243 740 NILF--FDEEDAArLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHV 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 748 -ERNIQAALARVCANRTTIIVAHRLSTIIHADEILVLQQGSIAERGRHEELVlrEDGIYADMWQQQLKNLDAeqSGGSDN 826
Cdd:PTZ00243 818 gERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFM--RTSLYATLAAELKENKDS--KEGDAD 893
|
....*
gi 19527665 827 GDASA 831
Cdd:PTZ00243 894 AEVAE 898
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
576-808 |
4.85e-25 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 105.17 E-value: 4.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSpEKIVLRNVSFTVPAGKTVAIVGPSGAGKST----IMRLLfrfyDVQTGAILIDGQNIKLVQQQSLRKA 651
Cdd:COG4604 2 IEIKNVSKRYG-GKVVLDDVSLTIPKGGITALIGPNGAGKSTllsmISRLL----PPDSGEVLVDGLDVATTPSRELAKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 652 IGVVPQDtvlfnNTI-----------FYNIEYAK--LGASDEAVYEAARA----ADIHERILGfpekyetkvgerglRLS 714
Cdd:COG4604 77 LAILRQE-----NHInsrltvrelvaFGRFPYSKgrLTAEDREIIDEAIAyldlEDLADRYLD--------------ELS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 715 GGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVC--ANRTTIIVAHRLS-TIIHADEILVLQQGSIAER 791
Cdd:COG4604 138 GGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLAdeLGKTVVIVLHDINfASCYADHIVAMKDGRVVAQ 217
|
250 260
....*....|....*....|.
gi 19527665 792 GRHEEL----VLREdgIYaDM 808
Cdd:COG4604 218 GTPEEIitpeVLSD--IY-DT 235
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
526-838 |
8.15e-25 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 111.75 E-value: 8.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 526 LYMPLNWFGTYYRAIQKNFVDMENMFDLLKEEEEIV-DAPGCSPLLTAgggIEFSNVTFGYSP--EKIVLRNVSFTVPAG 602
Cdd:PLN03130 567 LRFPLFMLPNLITQAVNANVSLKRLEELLLAEERVLlPNPPLEPGLPA---ISIKNGYFSWDSkaERPTLSNINLDVPVG 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 603 KTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIdgqniklvqqqsLRKAIGVVPQDTVLFNNTIFYNIEYaklGASDEAV 682
Cdd:PLN03130 644 SLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVAYVPQVSWIFNATVRDNILF---GSPFDPE 708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 683 --YEAARAADIHERILGFPEKYETKVGERGLRLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNI-QAALARVC 759
Cdd:PLN03130 709 ryERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVfDKCIKDEL 788
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19527665 760 ANRTTIIVAHRLSTIIHADEILVLQQGSIAERGRHEELVlrEDGiyaDMWQQQLKNLDAEQSGGSDNGDASAESGSEKR 838
Cdd:PLN03130 789 RGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELS--NNG---PLFQKLMENAGKMEEYVEENGEEEDDQTSSKP 862
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
591-797 |
8.24e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 104.45 E-value: 8.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 591 VLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYD-----VQTGAILIDGqNIKLVQQQS----LRKAIGVVPQDTVL 661
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQpeagtIRVGDITIDT-ARSLSQQKGlirqLRQHVGFVFQNFNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 662 F-NNTIFYNIEYAKLGASDEAVYEA-ARAadihERILGfpekyetKVGERG------LRLSGGEKQRVAIARTLLKAPII 733
Cdd:PRK11264 97 FpHRTVLENIIEGPVIVKGEPKEEAtARA----RELLA-------KVGLAGketsypRRLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19527665 734 VLLDEATSALDTHTERNIQA---ALARvcANRTTIIVAHRLSTIIH-ADEILVLQQGSIAERGRHEEL 797
Cdd:PRK11264 166 ILFDEPTSALDPELVGEVLNtirQLAQ--EKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
588-789 |
1.84e-24 |
|
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: 102.73 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 588 EKIVLRNVSFTVPAGKTVAIVGPSGAGKST----IMRLLfRFYDVQTGAILIDGQNIKlvqQQSLRKAIGVVPQDTVLFN 663
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTlldaISGRV-EGGGTTSGQILFNGQPRK---PDQFQKCVAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 664 N-TIFYNIEYA---KLGASDEAVYEAARAADIHERILGfpekyETKVGERGLR-LSGGEKQRVAIARTLLKAPIIVLLDE 738
Cdd:cd03234 95 GlTVRETLTYTailRLPRKSSDAIRKKRVEDVLLRDLA-----LTRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 19527665 739 ATSALDTHTERNIQAALARVCA-NRTTIIVAH--RLSTIIHADEILVLQQGSIA 789
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARrNRIVILTIHqpRSDLFRLFDRILLLSSGEIV 223
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
571-791 |
2.51e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 108.36 E-value: 2.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 571 TAGGGIEFSNVTFgYSPE-KIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILI-DGQNIKLVQQQ-- 646
Cdd:COG4178 358 SEDGALALEDLTL-RTPDgRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLPQRpy 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 647 ----SLRKAIgVVPQDTVLFnntifynieyaklgaSDEAVYEAARAADIHErilgFPEKYETkVGERGLRLSGGEKQRVA 722
Cdd:COG4178 437 lplgTLREAL-LYPATAEAF---------------SDAELREALEAVGLGH----LAERLDE-EADWDQVLSLGEQQRLA 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19527665 723 IARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVAHRLSTIIHADEILVLQQGSIAER 791
Cdd:COG4178 496 FARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGDGSWQL 564
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
576-802 |
2.75e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 103.95 E-value: 2.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSP----EKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNI----KLVQQQS 647
Cdd:PRK13634 3 ITFQKVEHRYQYktpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 648 LRKAIGVVPQ--DTVLFNNTIFYNIEYAKL--GASDEavyEAARAADIHERILGFPEKYETKvgeRGLRLSGGEKQRVAI 723
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMnfGVSEE---DAKQKAREMIELVGLPEELLAR---SPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 724 ARTLLKAPIIVLLDEATSALDTHTERNIQAALARVC--ANRTTIIVAHRLSTIIH-ADEILVLQQGSIAERGRHEELVLR 800
Cdd:PRK13634 157 AGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHkeKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFAD 236
|
..
gi 19527665 801 ED 802
Cdd:PRK13634 237 PD 238
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
594-797 |
2.82e-24 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 104.81 E-value: 2.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 594 NVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNI---KLVQQQSLRKAIGVVPQDTvlfnntifyni 670
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDItglSGRELRPLRRRMQMVFQDP----------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 671 eYAKL------GASDEAVYEAARAADIHERilgfpekyETKVGER----GLR----------LSGGEKQRVAIARTLLKA 730
Cdd:COG4608 105 -YASLnprmtvGDIIAEPLRIHGLASKAER--------RERVAELlelvGLRpehadrypheFSGGQRQRIGIARALALN 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19527665 731 PIIVLLDEATSALDThterNIQAA----LARVCA--NRTTIIVAHRLSTIIH-ADEILVLQQGSIAERGRHEEL 797
Cdd:COG4608 176 PKLIVCDEPVSALDV----SIQAQvlnlLEDLQDelGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
576-797 |
4.65e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 103.26 E-value: 4.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVT--FGyspEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIklvqQQSLRKAIG 653
Cdd:COG4152 2 LELKGLTkrFG---DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL----DPEDRRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 654 VVPqdtvlfnntifyniE----YAKLGASDEAVYEAAR----AADIHERI------LGFPEKYETKVGErglrLSGGEKQ 719
Cdd:COG4152 75 YLP--------------EerglYPKMKVGEQLVYLARLkglsKAEAKRRAdewlerLGLGDRANKKVEE----LSKGNQQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 720 RVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVA-HRLSTI-IHADEILVLQQGSIAERGRHEEL 797
Cdd:COG4152 137 KVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSsHQMELVeELCDRIVIINKGRKVLSGSVDEI 216
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
576-798 |
4.78e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 104.53 E-value: 4.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSpEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKlVQQQSLRKAIGVV 655
Cdd:PRK13536 42 IDLAGVSKSYG-DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP-ARARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 656 PQ-DTVLFNNTIFYNI----EYAKLGASD-EAVYEAaraadiherILGFPeKYETKVGERGLRLSGGEKQRVAIARTLLK 729
Cdd:PRK13536 120 PQfDNLDLEFTVRENLlvfgRYFGMSTREiEAVIPS---------LLEFA-RLESKADARVSDLSGGMKRRLTLARALIN 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19527665 730 APIIVLLDEATSALDTHTERNIQAALARVCANRTTIIV-------AHRLstiihADEILVLQQG-SIAErGRHEELV 798
Cdd:PRK13536 190 DPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVLEAGrKIAE-GRPHALI 260
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
576-802 |
5.75e-24 |
|
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: 101.70 E-value: 5.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSpEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRfYDVQTgailiDGQNIKLVQQQ-------SL 648
Cdd:COG1119 4 LELRNVTVRRG-GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITG-DLPPT-----YGNDVRLFGERrggedvwEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 649 RKAIGVV---------PQDTVL------FNNTIFYNIEYaklgaSDEavyEAARAADIHERiLGFPEKYETKVGErglrL 713
Cdd:COG1119 77 RKRIGLVspalqlrfpRDETVLdvvlsgFFDSIGLYREP-----TDE---QRERARELLEL-LGLAHLADRPFGT----L 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 714 SGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANR-TTII-VAHRLSTIIHA-DEILVLQQGSIAE 790
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVlVTHHVEEIPPGiTHVLLLKDGRVVA 223
|
250
....*....|..
gi 19527665 791 RGRHEElVLRED 802
Cdd:COG1119 224 AGPKEE-VLTSE 234
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
568-797 |
6.10e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 103.89 E-value: 6.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 568 PLLTAGGGIEFSNVTFG-YSPEKIV--LRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKL-- 642
Cdd:PRK11308 4 PLLQAIDLKKHYPVKRGlFKPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKad 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 643 -VQQQSLRKAIGVV---------PQDTV-------LFNNTifynieyaKLGASDEAvyeaARAADIHERILGFPEKYEtk 705
Cdd:PRK11308 84 pEAQKLLRQKIQIVfqnpygslnPRKKVgqileepLLINT--------SLSAAERR----EKALAMMAKVGLRPEHYD-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 706 vgerglR----LSGGEKQRVAIARTLLKAPIIVLLDEATSALDThterNIQAALARVCA------NRTTIIVAHRLSTII 775
Cdd:PRK11308 150 ------RyphmFSGGQRQRIAIARALMLDPDVVVADEPVSALDV----SVQAQVLNLMMdlqqelGLSYVFISHDLSVVE 219
|
250 260
....*....|....*....|...
gi 19527665 776 H-ADEILVLQQGSIAERGRHEEL 797
Cdd:PRK11308 220 HiADEVMVMYLGRCVEKGTKEQI 242
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
576-802 |
7.62e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 102.50 E-value: 7.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSP--EKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIG 653
Cdd:PRK13650 5 IEVKNLTFKYKEdqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 654 VVPQD--------TVlfNNTIFYNIEYAKLGASD--EAVYEAARAADIHErilgFPEKYETkvgerglRLSGGEKQRVAI 723
Cdd:PRK13650 85 MVFQNpdnqfvgaTV--EDDVAFGLENKGIPHEEmkERVNEALELVGMQD----FKEREPA-------RLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 724 ARTLLKAPIIVLLDEATSALD-------THTERNIqaalaRVCANRTTIIVAHRLSTIIHADEILVLQQGSIAERGRHEE 796
Cdd:PRK13650 152 AGAVAMRPKIIILDEATSMLDpegrlelIKTIKGI-----RDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRE 226
|
....*.
gi 19527665 797 LVLRED 802
Cdd:PRK13650 227 LFSRGN 232
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
576-806 |
8.09e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 104.92 E-value: 8.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSN--VTFGYSPekiVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIG 653
Cdd:PRK09536 4 IDVSDlsVEFGDTT---VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 654 VVPQDTVL-FNNTIFYNIE---------YAKLGASDEAVYEAARAAdihERILGFPEKYETKvgerglrLSGGEKQRVAI 723
Cdd:PRK09536 81 SVPQDTSLsFEFDVRQVVEmgrtphrsrFDTWTETDRAAVERAMER---TGVAQFADRPVTS-------LSGGERQRVLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 724 ARTLLKAPIIVLLDEATSALD-THTERNIQAALARVCANRTTIIVAHRLSTII-HADEILVLQQGSIAERGRHEElVLRE 801
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLDiNHQVRTLELVRRLVDDGKTAVAAIHDLDLAArYCDELVLLADGRVRAAGPPAD-VLTA 229
|
....*
gi 19527665 802 DGIYA 806
Cdd:PRK09536 230 DTLRA 234
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
576-792 |
8.20e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 101.24 E-value: 8.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSPEKiVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQ------QSLR 649
Cdd:PRK11124 3 IQLNGINCFYGAHQ-ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTpsdkaiRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 650 KAIGVVPQDTVLFNN-TIFYNIEYAK---LGASDEAVYEAA-------RAADIHERilgFPekyetkvgergLRLSGGEK 718
Cdd:PRK11124 82 RNVGMVFQQYNLWPHlTVQQNLIEAPcrvLGLSKDQALARAekllerlRLKPYADR---FP-----------LHLSGGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19527665 719 QRVAIARTLLKAPIIVLLDEATSALD---THTERNIQAALARVcaNRTTIIVAHRLSTIIH-ADEILVLQQGSIAERG 792
Cdd:PRK11124 148 QRVAIARALMMEPQVLLFDEPTAALDpeiTAQIVSIIRELAET--GITQVIVTHEVEVARKtASRVVYMENGHIVEQG 223
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
576-797 |
8.99e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 102.02 E-value: 8.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGY-SPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGV 654
Cdd:PRK13635 6 IRVEHISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 655 VPQ------------DTVLF---NNtifynieyaklGASDEAVYEAARAADIHERILGFPEkYETKvgerglRLSGGEKQ 719
Cdd:PRK13635 86 VFQnpdnqfvgatvqDDVAFgleNI-----------GVPREEMVERVDQALRQVGMEDFLN-REPH------RLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 720 RVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANR--TTIIVAHRLSTIIHADEILVLQQGSIAERGRHEEL 797
Cdd:PRK13635 148 RVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
591-793 |
1.19e-23 |
|
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: 100.59 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 591 VLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNI-KLVQQQ--SLRKA-IGVVPQD-------T 659
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfALDEDAraRLRARhVGFVFQSfqllptlT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 660 VLfnntifyniEY----AKLGASDEAvyeAARAADIHERIlGfpekyetkVGERgLR-----LSGGEKQRVAIARTLLKA 730
Cdd:COG4181 107 AL---------ENvmlpLELAGRRDA---RARARALLERV-G--------LGHR-LDhypaqLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19527665 731 PIIVLLDEATSALDTHTERNIQAALARVCANR-TT-IIVAHRLSTIIHADEILVLQQGSIAERGR 793
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIIDLLFELNRERgTTlVLVTHDPALAARCDRVLRLRAGRLVEDTA 229
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
576-792 |
1.24e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 103.87 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSpEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQslRKAIGVV 655
Cdd:PRK09452 15 VELRGISKSFD-GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 656 PQDTVLFNN-TIFYNIEYA----KLGASD--EAVYEAARAADIHERIlgfpekyetkvGERGLRLSGGEKQRVAIARTLL 728
Cdd:PRK09452 92 FQSYALFPHmTVFENVAFGlrmqKTPAAEitPRVMEALRMVQLEEFA-----------QRKPHQLSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19527665 729 KAPIIVLLDEATSALDTHTERNIQAALARVcaNR----TTIIVAH-RLSTIIHADEILVLQQGSIAERG 792
Cdd:PRK09452 161 NKPKVLLLDESLSALDYKLRKQMQNELKAL--QRklgiTFVFVTHdQEEALTMSDRIVVMRDGRIEQDG 227
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
526-797 |
2.20e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 106.98 E-value: 2.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 526 LYMPLNWFGTYYRAIQKNFVDMENMFDLLKEEEEIVdAPGcSPLLTAGGGIEFSNVTFGYSP--EKIVLRNVSFTVPAGK 603
Cdd:PLN03232 567 LRSPLNMLPNLLSQVVNANVSLQRIEELLLSEERIL-AQN-PPLQPGAPAISIKNGYFSWDSktSKPTLSDINLEIPVGS 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 604 TVAIVGPSGAGK-STIMRLLFRFYDVQTGAILIdgqniklvqqqslRKAIGVVPQDTVLFNNTIFYNIeyakLGASDEAV 682
Cdd:PLN03232 645 LVAIVGGTGEGKtSLISAMLGELSHAETSSVVI-------------RGSVAYVPQVSWIFNATVRENI----LFGSDFES 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 683 YEAARAADI----HERILgFPEKYETKVGERGLRLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNI-QAALAR 757
Cdd:PLN03232 708 ERYWRAIDVtalqHDLDL-LPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVfDSCMKD 786
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 19527665 758 VCANRTTIIVAHRLSTIIHADEILVLQQGSIAERGRHEEL 797
Cdd:PLN03232 787 ELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
576-787 |
3.06e-23 |
|
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: 98.94 E-value: 3.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTImrLLFRFYDVQT--GAILIDGQNIKLVQQQSL----R 649
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSL--LLAILGEMQTleGKVHWSNKNESEPSFEATrsrnR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 650 KAIGVVPQDTVLFNNTIFYNIEYAKlgASDEAVYEAA-RAADIHERILGFPEKYETKVGERGLRLSGGEKQRVAIARTLL 728
Cdd:cd03290 79 YSVAYAAQKPWLLNATVEENITFGS--PFNKQRYKAVtDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19527665 729 KAPIIVLLDEATSALDTH-TERNIQAALARVCAN--RTTIIVAHRLSTIIHADEILVLQQGS 787
Cdd:cd03290 157 QNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
578-744 |
3.63e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 104.38 E-value: 3.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 578 FSNVTFGYsPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLfrfydvqTGAILIDGQNIKLvqQQSLRkaIGVVPQ 657
Cdd:COG0488 1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKIL-------AGELEPDSGEVSI--PKGLR--IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 658 DTVLF-NNTIFYNI------------EYAKLGAS-DEAVYEAARAADIHERI------------------LGFPEK-YET 704
Cdd:COG0488 69 EPPLDdDLTVLDTVldgdaelraleaELEELEAKlAEPDEDLERLAELQEEFealggweaearaeeilsgLGFPEEdLDR 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 19527665 705 KVGErglrLSGGEKQRVAIARTLLKAPIIVLLDEATSALD 744
Cdd:COG0488 149 PVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
580-796 |
4.31e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 99.32 E-value: 4.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 580 NVTFGYSpEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGVVPQ-- 657
Cdd:PRK11231 7 NLTVGYG-TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQhh 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 658 ---------DTVLFNNTIFYNIeYAKLGASDEAVYEAARAAdihERILGFPEKYETKvgerglrLSGGEKQRVAIARTLL 728
Cdd:PRK11231 86 ltpegitvrELVAYGRSPWLSL-WGRLSAEDNARVNQAMEQ---TRINHLADRRLTD-------LSGGQRQRAFLAMVLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19527665 729 KAPIIVLLDEATSALDThterNIQAALARVC-----ANRTTIIVAHRLSTII-HADEILVLQQGSIAERGRHEE 796
Cdd:PRK11231 155 QDTPVVLLDEPTTYLDI----NHQVELMRLMrelntQGKTVVTVLHDLNQASrYCDHLVVLANGHVMAQGTPEE 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
592-797 |
4.51e-23 |
|
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: 104.00 E-value: 4.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 592 LRNVSFTVPAGKTVAIVGPSGAGKST----IMRLLfrfydVQTGAILIDGQNI-KLVQQQ--SLRKAIGVVPQD------ 658
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLdGLSRRAlrPLRRRMQVVFQDpfgsls 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 659 ---TVlfnntifynieyaklgasDEAVYEAARaadIHERILGFPEKYE------TKVG-ERGLR------LSGGEKQRVA 722
Cdd:COG4172 377 prmTV------------------GQIIAEGLR---VHGPGLSAAERRArvaealEEVGlDPAARhrypheFSGGQRQRIA 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 723 IARTLLKAPIIVLLDEATSALDthteRNIQAA----LARVCAnrttiivAHRLST--IIH--------ADEILVLQQGSI 788
Cdd:COG4172 436 IARALILEPKLLVLDEPTSALD----VSVQAQildlLRDLQR-------EHGLAYlfISHdlavvralAHRVMVMKDGKV 504
|
....*....
gi 19527665 789 AERGRHEEL 797
Cdd:COG4172 505 VEQGPTEQV 513
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
582-792 |
9.04e-23 |
|
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: 97.29 E-value: 9.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 582 TFGyspEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIklVQQQSLRKAIGVVPQDTVL 661
Cdd:cd03268 9 TYG---KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY--QKNIEALRRIGALIEAPGF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 662 FNN-TIFYNIEYAK--LGASDEAVYEAaraadihERILGFPEKYETKVGErglrLSGGEKQRVAIARTLLKAPIIVLLDE 738
Cdd:cd03268 84 YPNlTARENLRLLArlLGIRKKRIDEV-------LDVVGLKDSAKKKVKG----FSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 19527665 739 ATSALDTHTERNIQAALARVCANRTTIIVA-HRLSTI-IHADEILVLQQGSIAERG 792
Cdd:cd03268 153 PTNGLDPDGIKELRELILSLRDQGITVLISsHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
575-839 |
9.20e-23 |
|
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: 104.99 E-value: 9.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 575 GIEFSNVTFGYSPekiVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQniklvqqqslrkaIGV 654
Cdd:TIGR01271 428 GLFFSNFSLYVTP---VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISF 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 655 VPQDTVLFNNTIFYNIEYaklGAS-DEAVYEAA-RAADIHERILGFPEKYETKVGERGLRLSGGEKQRVAIARTLLKAPI 732
Cdd:TIGR01271 492 SPQTSWIMPGTIKDNIIF---GLSyDEYRYTSViKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDAD 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 733 IVLLDEATSALDTHTERNI-QAALARVCANRTTIIVAHRLSTIIHADEILVLQQGSIAERGRHEEL-VLREDGIYADMWQ 810
Cdd:TIGR01271 569 LYLLDSPFTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELqAKRPDFSSLLLGL 648
|
250 260 270
....*....|....*....|....*....|....*...
gi 19527665 811 QQLKNLDAEQSGG---------SDNGDASAESGSEKRR 839
Cdd:TIGR01271 649 EAFDNFSAERRNSiltetlrrvSIDGDSTVFSGPETIK 686
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
594-797 |
1.07e-22 |
|
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: 100.56 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 594 NVSFTVPAGKTVAIVGPSGAGKSTIMRL---LFRfydVQTGAILIDGQniklVQQQSLRK--------AIGVVPQDTVLF 662
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGE----VLQDSARGiflpphrrRIGYVFQEARLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 663 NN-TIFYNIEYaklGASDEAVyeAARAADIHERI--LGFpekyETKVGERGLRLSGGEKQRVAIARTLLKAPIIVLLDEA 739
Cdd:COG4148 90 PHlSVRGNLLY---GRKRAPR--AERRISFDEVVelLGI----GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19527665 740 TSALDTHTERNIQAALARVCAN-RTTII-VAHRLSTIIH-ADEILVLQQGSIAERGRHEEL 797
Cdd:COG4148 161 LAALDLARKAEILPYLERLRDElDIPILyVSHSLDEVARlADHVVLLEQGRVVASGPLAEV 221
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
591-790 |
1.16e-22 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 98.19 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 591 VLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNI------KLVQQ------QSLRkaigVVPQD 658
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItglpphRIARLgiartfQNPR----LFPEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 659 TVLFN----------NTIFYNIEYAKLGASDEAvyEA-ARAADIHERiLGFPEKYETKVGErglrLSGGEKQRVAIARTL 727
Cdd:COG0411 95 TVLENvlvaaharlgRGLLAALLRLPRARREER--EArERAEELLER-VGLADRADEPAGN----LSYGQQRRLEIARAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19527665 728 LKAPIIVLLDEATSALdTHTERN-IQAALARVCANR--TTIIVAHRLSTII-HADEILVLQQGS-IAE 790
Cdd:COG0411 168 ATEPKLLLLDEPAAGL-NPEETEeLAELIRRLRDERgiTILLIEHDMDLVMgLADRIVVLDFGRvIAE 234
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
576-786 |
1.22e-22 |
|
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: 96.97 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVT--FGyspEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIklvqQQSLRKAIG 653
Cdd:cd03269 1 LEVENVTkrFG---RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL----DIAARNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 654 VVPQDTVLfnntifynieYAKLGASDEAVY----------EAARAADIHERILGFPEKYETKVGErglrLSGGEKQRVAI 723
Cdd:cd03269 74 YLPEERGL----------YPKMKVIDQLVYlaqlkglkkeEARRRIDEWLERLELSEYANKRVEE----LSKGNQQKVQF 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19527665 724 ARTLLKAPIIVLLDEATSALD---THTERNIQAALARvcANRTTIIVAHRLSTIIH-ADEILVLQQG 786
Cdd:cd03269 140 IAAVIHDPELLILDEPFSGLDpvnVELLKDVIRELAR--AGKTVILSTHQMELVEElCDRVLLLNKG 204
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
576-800 |
1.37e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 100.18 E-value: 1.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVT--FGYSpekIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNI--KLVQQQSlrka 651
Cdd:PRK11432 7 VVLKNITkrFGSN---TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthRSIQQRD---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 652 IGVVPQDTVLFNN-TIFYNIEYA--KLGASDEA----VYEAARAADIHerilGFPEKYETKVgerglrlSGGEKQRVAIA 724
Cdd:PRK11432 80 ICMVFQSYALFPHmSLGENVGYGlkMLGVPKEErkqrVKEALELVDLA----GFEDRYVDQI-------SGGQQQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 725 RTLLKAPIIVLLDEATSALDTHTERN-------IQAALarvcaNRTTIIVAHRLSTIIH-ADEILVLQQGSIAERGRHEE 796
Cdd:PRK11432 149 RALILKPKVLLFDEPLSNLDANLRRSmrekireLQQQF-----NITSLYVTHDQSEAFAvSDTVIVMNKGKIMQIGSPQE 223
|
....
gi 19527665 797 LVLR 800
Cdd:PRK11432 224 LYRQ 227
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
585-797 |
1.39e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 98.20 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 585 YSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILID------GQNIKLVQQQSLRKAIGVVPQD 658
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDgkvlyfGKDIFQIDAIKLRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 659 TVLFNN-TIFYNIEYAKLGASDEAVYEAARAADIHERILGFPEKYETKVGERGLRLSGGEKQRVAIARTLLKAPIIVLLD 737
Cdd:PRK14246 99 PNPFPHlSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19527665 738 EATSALDTHTERNIQAALARVCANRTTIIVAHRLSTIIH-ADEILVLQQGSIAERGRHEEL 797
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
578-798 |
1.45e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 101.26 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 578 FSNVTFGYSPEKIV--------LRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLR 649
Cdd:PRK10070 22 FKYIEQGLSKEQILektglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 650 -----------KAIGVVPQDTVLfNNTIFyNIEYAKLGASD--EAVYEAARAADIHERILGFPEKyetkvgerglrLSGG 716
Cdd:PRK10070 102 evrrkkiamvfQSFALMPHMTVL-DNTAF-GMELAGINAEErrEKALDALRQVGLENYAHSYPDE-----------LSGG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 717 EKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCA--NRTTIIVAHRLSTIIH-ADEILVLQQGSIAERGR 793
Cdd:PRK10070 169 MRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAkhQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGT 248
|
....*
gi 19527665 794 HEELV 798
Cdd:PRK10070 249 PDEIL 253
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
576-797 |
1.58e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 98.23 E-value: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLvQQQSL---RKAI 652
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKY-DKKSLlevRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 653 GVVPQ--DTVLFNNTIFYNIEYA--KLGASDEAV----YEAARAADIherilgfpEKYETKVGERglrLSGGEKQRVAIA 724
Cdd:PRK13639 81 GIVFQnpDDQLFAPTVEEDVAFGplNLGLSKEEVekrvKEALKAVGM--------EGFENKPPHH---LSGGQKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19527665 725 RTLLKAPIIVLLDEATSALDTHTERNIQAALARVcaNR---TTIIVAHRLSTI-IHADEILVLQQGSIAERGRHEEL 797
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDL--NKegiTIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
588-797 |
2.43e-22 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 97.35 E-value: 2.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 588 EKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLV-------------QQQSLRKAIGV 654
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 655 VPQDTVLFNN-TIFYNIEYAK---LGASDEAVYEAAraadiherilgfpEKYETKVG--ERG-----LRLSGGEKQRVAI 723
Cdd:PRK10619 97 VFQHFNLWSHmTVLENVMEAPiqvLGLSKQEARERA-------------VKYLAKVGidERAqgkypVHLSGGQQQRVSI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19527665 724 ARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCAN-RTTIIVAHRLSTIIH-ADEILVLQQGSIAERGRHEEL 797
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQL 239
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
576-797 |
1.11e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 95.93 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSPEKIV--LRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIG 653
Cdd:PRK13642 5 LEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 654 VVPQ--DTVLFNNTIFYNIEYaklGASDEAVYEAARAADIHERILGFpEKYETKVGERGlRLSGGEKQRVAIARTLLKAP 731
Cdd:PRK13642 85 MVFQnpDNQFVGATVEDDVAF---GMENQGIPREEMIKRVDEALLAV-NMLDFKTREPA-RLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19527665 732 IIVLLDEATSALDTHTERNIQAALARV--CANRTTIIVAHRLSTIIHADEILVLQQGSIAERGRHEEL 797
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIHEIkeKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
251-534 |
1.73e-21 |
|
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: 95.65 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 251 VIVCIILLLAGRVIKLFLPIYRKKLVDSLTIAPIVFR--WDFVLIYVALSFLQGGGTgsmgLFNNLRTFLWIRVQQYTTR 328
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDVLIQLGPGGntSLLLLLVLGLAGAYVLSA----LLGILRGRLLARLGERITA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 329 EIEIELFRHLHQLSLRWHLQRKTGevlRVMDRGTDSINNLLNYIVFSIAPTILDLLVAVAYFVYAF--NWWFGLIVFLTM 406
Cdd:cd18563 77 DLRRDLYEHLQRLSLSFFDKRQTG---SLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFslNWKLALLVLIPV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 407 FLYIASTIAI-----TEWRTKYQRRMNLAdneqrARSVDSLLNFETVKYYGAEHYEVDCYREAILKYQKeeflSMLTLNM 481
Cdd:cd18563 154 PLVVWGSYFFwkkirRLFHRQWRRWSRLN-----SVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLD----ANIRAEK 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 19527665 482 LNTAQNIILCLGLLAGSLLCVYL---VVHHQTLTVGDFVLFSTYLMELYMPLNWFG 534
Cdd:cd18563 225 LWATFFPLLTFLTSLGTLIVWYFggrQVLSGTMTLGTLVAFLSYLGMFYGPLQWLS 280
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
588-800 |
2.55e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 93.98 E-value: 2.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 588 EKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLL--FRFYDVQTGAILIDGQNIKlvqqqSL------RKAIGVVPQDT 659
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDIL-----ELspderaRAGIFLAFQYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 660 VLF---NNTIFYNIEYAKLGASDEAVYEAARAADIHERILGFPEKYetkvGERGLR--LSGGEKQRVAIARTLLKAPIIV 734
Cdd:COG0396 87 VEIpgvSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLDEDF----LDRYVNegFSGGEKKRNEILQMLLLEPKLA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19527665 735 LLDEATSALDthternIQA--ALARVC-----ANRTTIIVAH--RLSTIIHADEILVLQQGSIAERGRhEELVLR 800
Cdd:COG0396 163 ILDETDSGLD------IDAlrIVAEGVnklrsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG-KELALE 230
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
575-774 |
2.57e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 94.33 E-value: 2.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 575 GIEFSNVTFGYSPEKIVlRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQT-----GAILIDGQNI--KLVQQQS 647
Cdd:PRK14258 7 AIKVNNLSFYYDTQKIL-EGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 648 LRKAIGVVPQDTVLFNNTIFYNIEYA--------KLgASDEAVYEAARAADIHERIlgfpekyETKVGERGLRLSGGEKQ 719
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwrpKL-EIDDIVESALKDADLWDEI-------KHKIHKSALDLSGGQQQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 19527665 720 RVAIARTLLKAPIIVLLDEATSALDTHTERNIQAAL--ARVCANRTTIIVAHRLSTI 774
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSELTMVIVSHNLHQV 214
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
575-797 |
3.09e-21 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 96.64 E-value: 3.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 575 GIEFSNVTFGYSpEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQslRKAIGV 654
Cdd:PRK11000 3 SVTLRNVTKAYG-DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 655 VPQDTVLFNN-TIFYNIEYA-KLGASDEAvyEAARAADIHERILGFPEKYETKVGErglrLSGGEKQRVAIARTLLKAPI 732
Cdd:PRK11000 80 VFQSYALYPHlSVAENMSFGlKLAGAKKE--EINQRVNQVAEVLQLAHLLDRKPKA----LSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19527665 733 IVLLDEATSALDTHTERNIQAALARVCA--NRTTIIVAH-RLSTIIHADEILVLQQGSIAERGRHEEL 797
Cdd:PRK11000 154 VFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
576-783 |
3.59e-21 |
|
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: 91.06 E-value: 3.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILI-DGQNIKLVQQQ------SL 648
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpEGEDLLFLPQRpylplgTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 649 RKAIgVVPQDTVLfnntifynieyaklgasdeavyeaaraadiherilgfpekyetkvgerglrlSGGEKQRVAIARTLL 728
Cdd:cd03223 81 REQL-IYPWDDVL----------------------------------------------------SGGEQQRLAFARLLL 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 19527665 729 KAPIIVLLDEATSALDTHTERniqaALARVCANR-TTII-VAHRLSTIIHADEILVL 783
Cdd:cd03223 108 HKPKFVFLDEATSALDEESED----RLYQLLKELgITVIsVGHRPSLWKFHDRVLDL 160
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
576-788 |
3.78e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 98.64 E-value: 3.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGY-SPEKI--VLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSL---- 648
Cdd:PRK10535 5 LELKDIRRSYpSGEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 649 RKAIGVVPQDTVLFNN-TIFYNIEYAKLGASDEAVYEAARAADIHERiLGFPEKyetkVGERGLRLSGGEKQRVAIARTL 727
Cdd:PRK10535 85 REHFGFIFQRYHLLSHlTAAQNVEVPAVYAGLERKQRLLRAQELLQR-LGLEDR----VEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19527665 728 LKAPIIVLLDEATSALDTHTERNIQAALARVCAN-RTTIIVAHRLSTIIHADEILVLQQGSI 788
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
567-797 |
5.01e-21 |
|
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: 97.83 E-value: 5.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 567 SPLLTagggIEFSNVTFG-YSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKS----TIMRLLFRFYDVQTGAILIDGQNIK 641
Cdd:COG4172 4 MPLLS----VEDLSVAFGqGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 642 LVQQQSLRK----AIGVVPQD--TVLfnNTIfYNIEyAKLGasdEA--VYEAARAADIHERIL------GFPEKyETKVG 707
Cdd:COG4172 80 GLSERELRRirgnRIAMIFQEpmTSL--NPL-HTIG-KQIA---EVlrLHRGLSGAAARARALellervGIPDP-ERRLD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 708 ERGLRLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANRTT----I-----IVAHrlstiiHAD 778
Cdd:COG4172 152 AYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMalllIthdlgVVRR------FAD 225
|
250
....*....|....*....
gi 19527665 779 EILVLQQGSIAERGRHEEL 797
Cdd:COG4172 226 RVAVMRQGEIVEQGPTAEL 244
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
576-797 |
5.73e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 94.08 E-value: 5.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGY---SP-EKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNI------KLVQQ 645
Cdd:PRK13646 3 IRFDNVSYTYqkgTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktkdKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 646 qsLRKAIGVVPQ--DTVLFNNTIFYNIEYA--KLGASDEAVYEAARAADIHeriLGFPEKYETKvgeRGLRLSGGEKQRV 721
Cdd:PRK13646 83 --VRKRIGMVFQfpESQLFEDTVEREIIFGpkNFKMNLDEVKNYAHRLLMD---LGFSRDVMSQ---SPFQMSGGQMRKI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19527665 722 AIARTLLKAPIIVLLDEATSALDTHTERNIQAALAR--VCANRTTIIVAHRLSTII-HADEILVLQQGSIAERGRHEEL 797
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVArYADEVIVMKEGSIVSQTSPKEL 233
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
592-802 |
7.19e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 92.60 E-value: 7.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 592 LRNVSFTVPAGKTVAIVGPSGAGKST-IMRL--LFRFydvqTGAILIDGQNIKLVQQQSLRKAIGVVPQDTV-LFNNTIF 667
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTlLARMagLLPG----QGEILLNGRPLSDWSAAELARHRAYLSQQQSpPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 668 yniEYAKLGASDEAVYEAARA--ADIHERiLGFPEKYETKVGerglRLSGGEKQRVAIARTLLK-------APIIVLLDE 738
Cdd:COG4138 88 ---QYLALHQPAGASSEAVEQllAQLAEA-LGLEDKLSRPLT----QLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 739 ATSALDTHTerniQAAL----ARVC-ANRTTIIVAHRLS-TIIHADEILVLQQGSIAERGRHEElVLRED 802
Cdd:COG4138 160 PMNSLDVAQ----QAALdrllRELCqQGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAE-VMTPE 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
576-786 |
1.06e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 96.63 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVT--FGyspeKIV-LRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQ-QQSLRKA 651
Cdd:COG3845 6 LELRGITkrFG----GVVaNDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSpRDAIALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 652 IGVVPQDTVLFNN-TIFYNI----EYAKLGASDEAVyEAARAADIHERiLGFPEKYETKVGErglrLSGGEKQRVAIART 726
Cdd:COG3845 82 IGMVHQHFMLVPNlTVAENIvlglEPTKGGRLDRKA-ARARIRELSER-YGLDVDPDAKVED----LSVGEQQRVEILKA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19527665 727 LLKAPIIVLLDEATSALdthTERNIQ---AALARVCANRTTII-VAHRLSTII-HADEILVLQQG 786
Cdd:COG3845 156 LYRGARILILDEPTAVL---TPQEADelfEILRRLAAEGKSIIfITHKLREVMaIADRVTVLRRG 217
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
576-790 |
1.23e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 96.67 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYsPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIdGQNIKlvqqqslrkaIGVV 655
Cdd:COG0488 316 LELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 656 PQDTVLF--NNTIFYNIEYAKLGASDEAVyeaaRAadiherILG---F-PEKYETKVGerglRLSGGEKQRVAIARTLLK 729
Cdd:COG0488 384 DQHQEELdpDKTVLDELRDGAPGGTEQEV----RG------YLGrflFsGDDAFKPVG----VLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19527665 730 APIIVLLDEATSALDTHTERNIQAALAR----VcanrttIIVAH-R--LSTIihADEILVLQQGSIAE 790
Cdd:COG0488 450 PPNVLLLDEPTNHLDIETLEALEEALDDfpgtV------LLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
567-797 |
1.53e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 94.52 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 567 SPLLtagggiEFSNVTFGYSPEKIVlRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVqqQ 646
Cdd:PRK11607 17 TPLL------EIRNLTKSFDGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV--P 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 647 SLRKAIGVVPQDTVLFNN-TIFYNIEYaklGASDEAVYEAARAADIHErILGFPEKYETkVGERGLRLSGGEKQRVAIAR 725
Cdd:PRK11607 88 PYQRPINMMFQSYALFPHmTVEQNIAF---GLKQDKLPKAEIASRVNE-MLGLVHMQEF-AKRKPHQLSGGQRQRVALAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19527665 726 TLLKAPIIVLLDEATSALDTHTERNIQAA----LARVCAnrTTIIVAH-RLSTIIHADEILVLQQGSIAERGRHEEL 797
Cdd:PRK11607 163 SLAKRPKLLLLDEPMGALDKKLRDRMQLEvvdiLERVGV--TCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
576-801 |
1.69e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 94.00 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVT--FGYSPekiVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRkaIG 653
Cdd:PRK10851 3 IEIANIKksFGRTQ---VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK--VG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 654 VVPQDTVLFNN-TIFYNIEYaklGASDEAVYEAARAADIHERILGFPEKYE-TKVGER-GLRLSGGEKQRVAIARTLLKA 730
Cdd:PRK10851 78 FVFQHYALFRHmTVFDNIAF---GLTVLPRRERPNAAAIKAKVTQLLEMVQlAHLADRyPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19527665 731 PIIVLLDEATSALDTHTERNIQAALARVCANR--TTIIVAHRLSTIIH-ADEILVLQQGSIAERGRHEElVLRE 801
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHDQEEAMEvADRVVVMSQGNIEQAGTPDQ-VWRE 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
576-797 |
1.70e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 92.56 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGY-SPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRL---LFRFYDVQTGAILIDGQNIKLVQQQSLRKA 651
Cdd:PRK13640 6 VEFKHVSFTYpDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLingLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 652 IGVVpqdtvlfnntiFYNIEYAKLGA--SDEAVYEAARAADIHERILGFPEKYETKVG------ERGLRLSGGEKQRVAI 723
Cdd:PRK13640 86 VGIV-----------FQNPDNQFVGAtvGDDVAFGLENRAVPRPEMIKIVRDVLADVGmldyidSEPANLSGGQKQRVAI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19527665 724 ARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCA--NRTTIIVAHRLSTIIHADEILVLQQGSIAERGRHEEL 797
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
249-521 |
2.17e-20 |
|
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: 92.51 E-value: 2.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 249 IAVIVCIILLLAgrVIKLFLPIYRKKLVDSLtiapIVFRWDFVLIYVALSFLqgggtgSMGLFNNL----RTFLWIRVQQ 324
Cdd:cd18570 4 LILILLLSLLIT--LLGIAGSFFFQILIDDI----IPSGDINLLNIISIGLI------LLYLFQSLlsyiRSYLLLKLSQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 325 YTTREIEIELFRHLHQLSLRWHLQRKTGEVL-RVMDrgTDSINNLLNYIVFSIaptILDLLVAVA--YFVYAFNWWFGLI 401
Cdd:cd18570 72 KLDIRLILGYFKHLLKLPLSFFETRKTGEIIsRFND--ANKIREAISSTTISL---FLDLLMVIIsgIILFFYNWKLFLI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 402 VFLTMFLYIASTIAITEWRTKYQRRMNLADNEQRARSVDSLLNFETVKYYGAEHYEVDCYREAILKYQKEEFLSMLTLNM 481
Cdd:cd18570 147 TLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNL 226
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 19527665 482 LNTAQNIILCLGLLAGSLLCVYLVVHHQtLTVGDFVLFST 521
Cdd:cd18570 227 QSSIKGLISLIGSLLILWIGSYLVIKGQ-LSLGQLIAFNA 265
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
592-808 |
2.61e-20 |
|
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: 90.60 E-value: 2.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 592 LRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKlvqqqslrkAIGvvPQDTVLFNN------- 664
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT---------EPG--PDRMVVFQNysllpwl 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 665 TIFYNIEYAKLGASDEAVYEAARA-ADIHERILGFPEKYETKVGErglrLSGGEKQRVAIARTLLKAPIIVLLDEATSAL 743
Cdd:TIGR01184 70 TVRENIALAVDRVLPDLSKSERRAiVEEHIALVGLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFGAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19527665 744 DTHTERNIQAALARVC--ANRTTIIVAHRL-STIIHADEILVLQQGSIA----------ERGRHEELVLrEDGIYADM 808
Cdd:TIGR01184 146 DALTRGNLQEELMQIWeeHRVTVLMVTHDVdEALLLSDRVVMLTNGPAAnigqilevpfPRPRDRLEVV-EDPSYYDL 222
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
576-798 |
3.23e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 90.41 E-value: 3.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYspEKIVLRnVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQslRKAIGVV 655
Cdd:PRK10771 2 LKLTDITWLY--HHLPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 656 PQDTVLFNN-TIFYNIEYA-----KLGASD-EAVYEAARAADIHERILGFPEKyetkvgerglrLSGGEKQRVAIARTLL 728
Cdd:PRK10771 77 FQENNLFSHlTVAQNIGLGlnpglKLNAAQrEKLHAIARQMGIEDLLARLPGQ-----------LSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19527665 729 KAPIIVLLDEATSALDTHTERNIQAALARVCANR--TTIIVAHRLSTIIH-ADEILVLQQGSIAERGRHEELV 798
Cdd:PRK10771 146 REQPILLLDEPFSALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELL 218
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
574-797 |
3.55e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 91.99 E-value: 3.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 574 GGIEFSNVTFGYSP----EKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNI-----KLVQ 644
Cdd:PRK13645 5 KDIILDNVSYTYAKktpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 645 QQSLRKAIGVVPQ--DTVLFNNTIFYNIEYA--KLGASDEAVYEaaraaDIHE--RILGFPEKYetkVGERGLRLSGGEK 718
Cdd:PRK13645 85 VKRLRKEIGLVFQfpEYQLFQETIEKDIAFGpvNLGENKQEAYK-----KVPEllKLVQLPEDY---VKRSPFELSGGQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 719 QRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCAN--RTTIIVAHRLSTIIH-ADEILVLQQGSIAERGRHE 795
Cdd:PRK13645 157 RRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPF 236
|
..
gi 19527665 796 EL 797
Cdd:PRK13645 237 EI 238
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
592-745 |
4.09e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 89.46 E-value: 4.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 592 LRNVSFTVPAGKTVAIVGPSGAGKSTIMRLL-------FRFydvqTGAILIDGQNIKLVQQQslRKAIGVVPQDTVLFNN 664
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIagtlspaFSA----SGEVLLNGRRLTALPAE--QRRIGILFQDDLLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 665 -TIFYNIEYA-----KLGASDEAVYEAARAADIHerilGFPEKYetkVGErglrLSGGEKQRVAIARTLLKAPIIVLLDE 738
Cdd:COG4136 91 lSVGENLAFAlpptiGRAQRRARVEQALEEAGLA----GFADRD---PAT----LSGGQRARVALLRALLAEPRALLLDE 159
|
....*..
gi 19527665 739 ATSALDT 745
Cdd:COG4136 160 PFSKLDA 166
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
576-788 |
4.66e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 90.92 E-value: 4.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNV--TF--GYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNI-KLVQQQslR- 649
Cdd:COG1101 2 LELKNLskTFnpGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtKLPEYK--Ra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 650 KAIGVVPQDTVL---FNNTIFYNIEYA---------KLGASdeavyeAARAADIHERI----LGFPEKYETKVGErglrL 713
Cdd:COG1101 80 KYIGRVFQDPMMgtaPSMTIEENLALAyrrgkrrglRRGLT------KKRRELFRELLatlgLGLENRLDTKVGL----L 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19527665 714 SGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCA--NRTTIIVAHRLSTII-HADEILVLQQGSI 788
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEenNLTTLMVTHNMEQALdYGNRLIMMHEGRI 227
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
568-807 |
5.56e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 91.41 E-value: 5.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 568 PLLTAGggIEFSNVTFGYSpEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQS 647
Cdd:PRK13537 2 PMSVAP--IDFRNVEKRYG-DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 648 lRKAIGVVPQ-D------TVLFNNTIFynieyaklgasdeAVYEAARAADIHERILGFPE------KYETKVGErglrLS 714
Cdd:PRK13537 79 -RQRVGVVPQfDnldpdfTVRENLLVF-------------GRYFGLSAAAARALVPPLLEfaklenKADAKVGE----LS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 715 GGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANRTTIIV-------AHRLstiihADEILVLQQG- 786
Cdd:PRK13537 141 GGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVIEEGr 215
|
250 260
....*....|....*....|....*.
gi 19527665 787 SIAErGRHEELVLREDG-----IYAD 807
Cdd:PRK13537 216 KIAE-GAPHALIESEIGcdvieIYGP 240
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
576-797 |
6.83e-20 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 89.35 E-value: 6.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSpEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIkLVQQQSLRKAIGVV 655
Cdd:cd03265 1 IEVENLVKKYG-DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV-VREPREVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 656 PQDTVLFNN-TIFYNIEyaklgasdeavyeaaraadIHERILGFPEKYETKVGERGLRL--------------SGGEKQR 720
Cdd:cd03265 79 FQDLSVDDElTGWENLY-------------------IHARLYGVPGAERRERIDELLDFvglleaadrlvktySGGMRRR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 721 VAIARTLLKAPIIVLLDEATSALDTHTE----RNIQAALARvcaNRTTIIvahrLSTiiH--------ADEILVLQQGSI 788
Cdd:cd03265 140 LEIARSLVHRPEVLFLDEPTIGLDPQTRahvwEYIEKLKEE---FGMTIL----LTT--HymeeaeqlCDRVAIIDHGRI 210
|
....*....
gi 19527665 789 AERGRHEEL 797
Cdd:cd03265 211 IAEGTPEEL 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
583-790 |
1.26e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 89.75 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 583 FGYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNI---KLVQQQSLRKAIGVVPQDT 659
Cdd:PRK10419 19 SGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklNRAQRKAFRRDIQMVFQDS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 660 V-LFN--NTIFYNIeyaklgasDE------AVYEAARAADIHE--RILGFPEKYETKvgeRGLRLSGGEKQRVAIARTLL 728
Cdd:PRK10419 99 IsAVNprKTVREII--------REplrhllSLDKAERLARASEmlRAVDLDDSVLDK---RPPQLSGGQLQRVCLARALA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19527665 729 KAPIIVLLDEATSALDTHTERNIQAALARVCANRTT--IIVAHRLSTIIH-ADEILVLQQGSIAE 790
Cdd:PRK10419 168 VEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
575-793 |
1.29e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 89.80 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 575 GIEFSNVTFGY---SP-EKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQ----Q 646
Cdd:PRK13649 2 GINLQNVSYTYqagTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 647 SLRKAIGVVPQ--DTVLFNNTIFYNIEYA--KLGASDEavyEAARAADIHERILGFPEKYETKvgeRGLRLSGGEKQRVA 722
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEETVLKDVAFGpqNFGVSQE---EAEALAREKLALVGISESLFEK---NPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19527665 723 IARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANRTTII-VAHRLSTII-HADEILVLQQGSIAERGR 793
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVAnYADFVYVLEKGKLVLSGK 228
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
588-802 |
2.37e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 89.91 E-value: 2.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 588 EKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMR-----LLFRFYDVQTGAILIdGQNIKLVQQ------------QSLRK 650
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglIKSKYGTIQVGDIYI-GDKKNNHELitnpyskkiknfKELRR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 651 AIGVVPQ--DTVLFNNTIFYNIEYA--KLGASDeavYEAARAADIHERILGFPEKYEtkvgERG-LRLSGGEKQRVAIAR 725
Cdd:PRK13631 117 RVSMVFQfpEYQLFKDTIEKDIMFGpvALGVKK---SEAKKLAKFYLNKMGLDDSYL----ERSpFGLSGGQKRRVAIAG 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19527665 726 TLLKAPIIVLLDEATSALDTHTERN-IQAALARVCANRTTIIVAHRLSTIIH-ADEILVLQQGSIAERGRHEELVLRED 802
Cdd:PRK13631 190 ILAIQPEILIFDEPTAGLDPKGEHEmMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
583-790 |
2.76e-19 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 88.71 E-value: 2.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 583 FGYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNI---KLVQQQSLRKAIGVVPQDT 659
Cdd:TIGR02769 18 FGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLyqlDRKQRRAFRRDVQLVFQDS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 660 V-LFN--NTIFYNIeyAKLGASDEAVYEAARAADIHE--RILGFPEKYETKvgeRGLRLSGGEKQRVAIARTLLKAPIIV 734
Cdd:TIGR02769 98 PsAVNprMTVRQII--GEPLRHLTSLDESEQKARIAEllDMVGLRSEDADK---LPRQLSGGQLQRINIARALAVKPKLI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 19527665 735 LLDEATSALDTHTERNIQAALARVCANRTT--IIVAHRLSTIIH-ADEILVLQQGSIAE 790
Cdd:TIGR02769 173 VLDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
588-788 |
3.29e-19 |
|
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: 87.77 E-value: 3.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 588 EKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGqNIKLVQQQSLRKAIGVV------------ 655
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-LVPWKRRKKFLRRIGVVfgqktqlwwdlp 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 656 PQDTVLFNNTIfYNIEYAKLGasdEAVYEAARAADIhERILGFPEKyetkvgerglRLSGGEKQRVAIARTLLKAPIIVL 735
Cdd:cd03267 112 VIDSFYLLAAI-YDLPPARFK---KRLDELSELLDL-EELLDTPVR----------QLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 19527665 736 LDEATSALDTHTERNIQAALARVCANR-TTIIV-AHRLSTIIH-ADEILVLQQGSI 788
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEYNRERgTTVLLtSHYMKDIEAlARRVLVIDKGRL 232
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
558-797 |
3.36e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 88.61 E-value: 3.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 558 EEIVDAPGCSPLLTAGGGIEFSNVTFGYSpEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDV-----QTGA 632
Cdd:PRK14271 4 ERLGGQSGAADVDAAAPAMAAVNLTLGFA-GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 633 ILIDGQNI-KLVQQQSLRKAIGVVPQDTVLFNNTIFYNI----EYAKLGASDEavYEAARAADIHEriLGFPEKYETKVG 707
Cdd:PRK14271 83 VLLGGRSIfNYRDVLEFRRRVGMLFQRPNPFPMSIMDNVlagvRAHKLVPRKE--FRGVAQARLTE--VGLWDAVKDRLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 708 ERGLRLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVAHRLSTIIH-ADEILVLQQG 786
Cdd:PRK14271 159 DSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDG 238
|
250
....*....|.
gi 19527665 787 SIAERGRHEEL 797
Cdd:PRK14271 239 RLVEEGPTEQL 249
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
568-788 |
4.12e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 87.81 E-value: 4.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 568 PLLTAGGGIEFSNVTFGYSpEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFyDVQTGAILIDGqNIKLVQqqs 647
Cdd:PRK11247 5 ARLNQGTPLLLNAVSKRYG-ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGL-ETPSAGELLAG-TAPLAE--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 648 LRKAIGVVPQDTVLFN-NTIFYNIEYAKLGASDEAVYEAARAADIHERILGFPEKyetkvgerglrLSGGEKQRVAIART 726
Cdd:PRK11247 79 AREDTRLMFQDARLLPwKKVIDNVGLGLKGQWRDAALQALAAVGLADRANEWPAA-----------LSGGQKQRVALARA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19527665 727 LLKAPIIVLLDEATSALDTHTERNIQAALARVCANR--TTIIVAHRLS-TIIHADEILVLQQGSI 788
Cdd:PRK11247 148 LIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
575-795 |
5.00e-19 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 88.02 E-value: 5.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 575 GIEFSNVTFGYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLrkaIGV 654
Cdd:PRK15056 6 GIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 655 VPQDT-------VLFNNTIFYNiEYAKLG------ASDEAVYEAARAAdiheriLGFPEKYETKVGErglrLSGGEKQRV 721
Cdd:PRK15056 83 VPQSEevdwsfpVLVEDVVMMG-RYGHMGwlrrakKRDRQIVTAALAR------VDMVEFRHRQIGE----LSGGQKKRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19527665 722 AIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCAN-RTTIIVAHRLSTIIHADEILVLQQGSIAERGRHE 795
Cdd:PRK15056 152 FLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
576-798 |
5.21e-19 |
|
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: 91.40 E-value: 5.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSpEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLL--FRFYDVQTGAIL------------------- 634
Cdd:TIGR03269 1 IEVKNLTKKFD-GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIyhvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 635 --------------IDGQNIKLVQQQSLRKAIGVVPQDT-VLF-NNTIFYNIeyakLGASDEAVYEAA----RAADIHER 694
Cdd:TIGR03269 80 epcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQRTfALYgDDTVLDNV----LEALEEIGYEGKeavgRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 695 IlgfpeKYETKVGERGLRLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAAL-ARVCANRTTIIVAHRLST 773
Cdd:TIGR03269 156 V-----QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALeEAVKASGISMVLTSHWPE 230
|
250 260
....*....|....*....|....*..
gi 19527665 774 IIH--ADEILVLQQGSIAERGRHEELV 798
Cdd:TIGR03269 231 VIEdlSDKAIWLENGEIKEEGTPDEVV 257
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
580-801 |
5.38e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 87.73 E-value: 5.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 580 NVTFGYSpEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGVVPQdt 659
Cdd:PRK10253 12 QLTLGYG-KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQ-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 660 vlfNNTIFYNIEYAKLGA----------------SDEAVYEAARAADIHERILgfpEKYETkvgerglrLSGGEKQRVAI 723
Cdd:PRK10253 89 ---NATTPGDITVQELVArgryphqplftrwrkeDEEAVTKAMQATGITHLAD---QSVDT--------LSGGQRQRAWI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 724 ARTLLKAPIIVLLDEATSALDTHTERNIQAALARVcaNRTTiivAHRLSTIIH--------ADEILVLQQGSIAERGRHE 795
Cdd:PRK10253 155 AMVLAQETAIMLLDEPTTWLDISHQIDLLELLSEL--NREK---GYTLAAVLHdlnqacryASHLIALREGKIVAQGAPK 229
|
....*.
gi 19527665 796 ELVLRE 801
Cdd:PRK10253 230 EIVTAE 235
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
591-800 |
5.81e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 87.28 E-value: 5.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 591 VLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQ-----TGAILIDGQNIKLVQQQSLRKAIGVVPQ-DTVLFNN 664
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRRVQMVFQiPNPIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 665 TIFYNIEYA----KLGASDEAVYEAARAADIHERILgfpEKYETKVGERGLRLSGGEKQRVAIARTLLKAPIIVLLDEAT 740
Cdd:PRK14247 98 SIFENVALGlklnRLVKSKKELQERVRWALEKAQLW---DEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPT 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19527665 741 SALDTHTERNIQAALARVCANRTTIIVAH------RLStiihaDEILVLQQGSIAERGRHEELVLR 800
Cdd:PRK14247 175 ANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWGPTREVFTN 235
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
591-783 |
7.70e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 85.36 E-value: 7.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 591 VLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILI-DGQNIKLVQQQS-LRKAIGVVPQDTVLFNntify 668
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRaGGARVAYVPQRSeVPDSLPLTVRDLVAMG----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 669 niEYAKLG------ASDEAVYEAARAAdiherilgfpekyetkVGERGLR------LSGGEKQRVAIARTLLKAPIIVLL 736
Cdd:NF040873 82 --RWARRGlwrrltRDDRAAVDDALER----------------VGLADLAgrqlgeLSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 19527665 737 DEATSALDTHTERNIQAALARVCA-NRTTIIVAHRLSTIIHADEILVL 783
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEEHArGATVVVVTHDLELVRRADPCVLL 191
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
588-792 |
1.30e-18 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 86.16 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 588 EKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLF--RFYDVQTGAILIDGQNI-KLVQQQSLRKAIGVVPQDTVLF-- 662
Cdd:TIGR01978 12 DKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAghPSYEVTSGTILFKGQDLlELEPDERARAGLFLAFQYPEEIpg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 663 -NNTIF----YNIEYAKLGASDEAVYEAARAADIHERILGFPEKYEtkvgERGLR--LSGGEKQRVAIARTLLKAPIIVL 735
Cdd:TIGR01978 92 vSNLEFlrsaLNARRSARGEEPLDLLDFEKLLKEKLALLDMDEEFL----NRSVNegFSGGEKKRNEILQMALLEPKLAI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 736 LDEATSALDTHTERNIQAALARVCA-NRTTIIVAH--RLSTIIHADEILVLQQGSIAERG 792
Cdd:TIGR01978 168 LDEIDSGLDIDALKIVAEGINRLREpDRSFLIITHyqRLLNYIKPDYVHVLLDGRIVKSG 227
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
588-800 |
3.36e-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: 83.73 E-value: 3.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 588 EKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRF--YDVQTGAILIDGQNIKlvqqqslrkaigvvpqdtvlfnnt 665
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDIT------------------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 666 ifynieyaklgasDEAVYEAARAAdiherI-LGF--PEKYE-TKVGE--RGLR--LSGGEKQRVAIARTLLKAPIIVLLD 737
Cdd:cd03217 68 -------------DLPPEERARLG-----IfLAFqyPPEIPgVKNADflRYVNegFSGGEKKRNEILQLLLLEPDLAILD 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19527665 738 EATSALDTHTERNIQAALAR-VCANRTTIIVAH--RLSTIIHADEILVLQQGSIAERGRhEELVLR 800
Cdd:cd03217 130 EPDSGLDIDALRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD-KELALE 194
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
586-798 |
3.77e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 89.34 E-value: 3.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 586 SPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLL-FRFY-DVQ-TGAILIDGQNIKLVQQqslRKAIGVVPQDTVLF 662
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALaFRSPkGVKgSGSVLLNGMPIDAKEM---RAISAYVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 663 NN-TIFYNIEYA---KLGASDEAVYEAARAADIHERiLGFPEKYETKVGERGLR--LSGGEKQRVAIARTLLKAPIIVLL 736
Cdd:TIGR00955 112 PTlTVREHLMFQahlRMPRRVTKKEKRERVDEVLQA-LGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFC 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19527665 737 DEATSALDTHTERNIQAALARVCANRTTIIVA-HRLSTIIHA--DEILVLQQGSIAERGRHEELV 798
Cdd:TIGR00955 191 DEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTiHQPSSELFElfDKIILMAEGRVAYLGSPDQAV 255
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
589-802 |
4.90e-18 |
|
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: 84.13 E-value: 4.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 589 KIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNI-KLVQQQSLRKAIGVVPQDTVLFNN-TI 666
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDItKLPMHKRARLGIGYLPQEASIFRKlTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 667 FYNIeyaklgasdEAVYEAAR--AADIHERILGFPEKYE-TKVGER-GLRLSGGEKQRVAIARTLLKAPIIVLLDEATSA 742
Cdd:cd03218 93 EENI---------LAVLEIRGlsKKEREEKLEELLEEFHiTHLRKSkASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19527665 743 LDTHTERNIQAALARVCANRTTI-IVAHRLS-TIIHADEILVLQQGSIAERGRHEELVLRED 802
Cdd:cd03218 164 VDPIAVQDIQKIIKILKDRGIGVlITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
591-772 |
5.31e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 84.10 E-value: 5.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 591 VLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNikLVQQQSLRKA------IGVV-------PQ 657
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQP--MSKLSSAAKAelrnqkLGFIyqfhhllPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 658 DTVLFNNTIFYNIEYAKLGASDEAVYEAARAADIHERilgfpekyetkVGERGLRLSGGEKQRVAIARTLLKAPIIVLLD 737
Cdd:PRK11629 102 FTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHR-----------ANHRPSELSGGERQRVAIARALVNNPRLVLAD 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 19527665 738 EATSALDTHTERNIQAALARVCANRTT--IIVAHRLS 772
Cdd:PRK11629 171 EPTGNLDARNADSIFQLLGELNRLQGTafLVVTHDLQ 207
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
584-792 |
6.23e-18 |
|
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: 83.74 E-value: 6.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 584 GYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLvqqqsLRKAIGVVPQDTVLfN 663
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSL-----LGLGGGFNPELTGR-E 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 664 NTIFYNIEYAKLGASDEAVYeaaraadihERILGF---PEKYETKVGErglrLSGGEKQRVAIARTLLKAPIIVLLDEAT 740
Cdd:cd03220 104 NIYLNGRLLGLSRKEIDEKI---------DEIIEFselGDFIDLPVKT----YSSGMKARLAFAIATALEPDILLIDEVL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 19527665 741 SALDTHTERNIQAALARVCAN-RTTIIVAHRLSTII-HADEILVLQQGSIAERG 792
Cdd:cd03220 171 AVGDAAFQEKCQRRLRELLKQgKTVILVSHDPSSIKrLCDRALVLEKGKIRFDG 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
585-798 |
7.74e-18 |
|
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: 87.55 E-value: 7.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 585 YSPEKIVLR---NVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRF-------YDVQTGAILIDGQNIKLVQQQSLRKAIGV 654
Cdd:TIGR03269 290 ISVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVleptsgeVNVRVGDEWVDMTKPGPDGRGRAKRYIGI 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 655 VPQDTVLF-NNTIFYNI-EYAKLGASDEAvyeAARAADIHERILGFPEKYETKVGER-GLRLSGGEKQRVAIARTLLKAP 731
Cdd:TIGR03269 370 LHQEYDLYpHRTVLDNLtEAIGLELPDEL---ARMKAVITLKMVGFDEEKAEEILDKyPDELSEGERHRVALAQVLIKEP 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 732 IIVLLDEATSALDTHTERNIQAAL--ARVCANRTTIIVAHRLSTIIH-ADEILVLQQGSIAERGRHEELV 798
Cdd:TIGR03269 447 RIVILDEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIV 516
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
576-792 |
9.99e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 84.75 E-value: 9.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSP----EKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLL------------FRFYD--VQTGAILIDG 637
Cdd:PRK13651 3 IKVKNIVKIFNKklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLnalllpdtgtieWIFKDekNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 638 QNIKLVQQQS----------LRKAIGVVPQ--DTVLFNNTIFYNIEYA--KLGASDEAVYEaaRAADIHErILGFPEKYE 703
Cdd:PRK13651 83 VLEKLVIQKTrfkkikkikeIRRRVGVVFQfaEYQLFEQTIEKDIIFGpvSMGVSKEEAKK--RAAKYIE-LVGLDESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 704 TKvgeRGLRLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCAN-RTTIIVAHRLSTIIH-ADEIL 781
Cdd:PRK13651 160 QR---SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVLEwTKRTI 236
|
250
....*....|.
gi 19527665 782 VLQQGSIAERG 792
Cdd:PRK13651 237 FFKDGKIIKDG 247
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
588-797 |
1.10e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.45 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 588 EKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQtGAILIDGQNIKLVQQQSL---RKAIGVVPQDTvlfnn 664
Cdd:PRK15134 298 HNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDP----- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 665 tifynieYAKLGASDEAVYEAARAADIHERILGfPEKYETKV----GERGL----------RLSGGEKQRVAIARTLLKA 730
Cdd:PRK15134 372 -------NSSLNPRLNVLQIIEEGLRVHQPTLS-AAQREQQViavmEEVGLdpetrhrypaEFSGGQRQRIAIARALILK 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 731 PIIVLLDEATSALDthteRNIQA---ALARVCANRttiivaHRLSTI-IHAD---------EILVLQQGSIAERGRHEEL 797
Cdd:PRK15134 444 PSLIILDEPTSSLD----KTVQAqilALLKSLQQK------HQLAYLfISHDlhvvralchQVIVLRQGEVVEQGDCERV 513
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
589-788 |
1.16e-17 |
|
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: 81.71 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 589 KIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIK-LVQQQSLRKAIGVVPQD---TVLF-N 663
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTrRSPRDAIRAGIAYVPEDrkrEGLVlD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 664 NTIFYNIeyaklgasdeavyeaaraadiherILGFpekyetkvgerglRLSGGEKQRVAIARTLLKAPIIVLLDEATSAL 743
Cdd:cd03215 93 LSVAENI------------------------ALSS-------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 19527665 744 DTHTERNIQAALARVCANRTTIIVahrLST----IIH-ADEILVLQQGSI 788
Cdd:cd03215 136 DVGAKAEIYRLIRELADAGKAVLL---ISSeldeLLGlCDRILVMYEGRI 182
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
309-548 |
1.44e-17 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 84.49 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 309 GLFNNLRTFLWIRVQQYTTREIEIELFRHLHQLSLRWHLQRKTGEVL-RVmdrgTDSINNLLNYIVFSIAPTILDLLVAV 387
Cdd:cd18564 68 GLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLsRL----TGDVGAIQDLLVSGVLPLLTNLLTLV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 388 AYFVYAF--NWWFGLIVFLTM-FLYIAStiaitewrTKYQRRMNLADNEQRARSVD-------SLLNFETVKYYGAEHYE 457
Cdd:cd18564 144 GMLGVMFwlDWQLALIALAVApLLLLAA--------RRFSRRIKEASREQRRREGAlasvaqeSLSAIRVVQAFGREEHE 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 458 VDCYREAILKYQKEEFLSMLTLNMLNTAQNIILCLGLLAGSLLCVYLVVHHqTLTVGDFVLFSTYLMELYMPLNWFGTYY 537
Cdd:cd18564 216 ERRFARENRKSLRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAG-RLTPGDLLVFLAYLKNLYKPVRDLAKLT 294
|
250
....*....|.
gi 19527665 538 RAIQKNFVDME 548
Cdd:cd18564 295 GRIAKASASAE 305
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
594-744 |
1.79e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 87.22 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 594 NVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLV---QQQSLRKAIGVVPQD---TVLFNNTIF 667
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLspgKLQALRRDIQFIFQDpyaSLDPRQTVG 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 668 YNI----EYAKLGASDEAvyeAARAADIHERILGFPE---KYETKvgerglrLSGGEKQRVAIARTLLKAPIIVLLDEAT 740
Cdd:PRK10261 422 DSImeplRVHGLLPGKAA---AARVAWLLERVGLLPEhawRYPHE-------FSGGQRQRICIARALALNPKVIIADEAV 491
|
....
gi 19527665 741 SALD 744
Cdd:PRK10261 492 SALD 495
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
588-768 |
2.06e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.46 E-value: 2.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 588 EKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGvvPQDTVLFNNTIF 667
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 668 YNIEY--AKLGASDEAVYEAARAADIHeRILGFPEKYetkvgerglrLSGGEKQRVAIARTLL-KAPIIvLLDEATSALD 744
Cdd:PRK13539 92 ENLEFwaAFLGGEELDIAAALEAVGLA-PLAHLPFGY----------LSAGQKRRVALARLLVsNRPIW-ILDEPTAALD 159
|
170 180
....*....|....*....|....
gi 19527665 745 THTERNIQAALARVCANRTTIIVA 768
Cdd:PRK13539 160 AAAVALFAELIRAHLAQGGIVIAA 183
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
584-758 |
3.30e-17 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 82.22 E-value: 3.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 584 GYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNiklVQQQSLRKaiGVVPQDTVLF- 662
Cdd:COG4525 15 GGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVP---VTGPGADR--GVVFQKDALLp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 663 -----NNTIFynieyaklGASDEAVYEAARAAdIHERILgfpekyeTKVGERGL------RLSGGEKQRVAIARTLLKAP 731
Cdd:COG4525 90 wlnvlDNVAF--------GLRLRGVPKAERRA-RAEELL-------ALVGLADFarrriwQLSGGMRQRVGIARALAADP 153
|
170 180
....*....|....*....|....*..
gi 19527665 732 IIVLLDEATSALDTHTERNIQAALARV 758
Cdd:COG4525 154 RFLLMDEPFGALDALTREQMQELLLDV 180
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
576-796 |
3.40e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 81.46 E-value: 3.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQS---LRKAI 652
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 653 GVVPQDT-VLFNNTIFYNIEYAKL--GASDEavyeaaraaDIHERILGFPEKYE--TKVGERGLRLSGGEKQRVAIARTL 727
Cdd:PRK10908 82 GMIFQDHhLLMDRTVYDNVAIPLIiaGASGD---------DIRRRVSAALDKVGllDKAKNFPIQLSGGEQQRVGIARAV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19527665 728 LKAPIIVLLDEATSALDTHTERNIQAALARVcaNR---TTIIVAHRLSTIIHAD-EILVLQQGSIAErGRHEE 796
Cdd:PRK10908 153 VNKPAVLLADEPTGNLDDALSEGILRLFEEF--NRvgvTVLMATHDIGLISRRSyRMLTLSDGHLHG-GVGGE 222
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
588-770 |
3.77e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 81.16 E-value: 3.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 588 EKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGvvpqdtvlfnntif 667
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLIDAIG-------------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 668 ynieyaKLGASDEAVYEAARAAdiheriLGFPEKYETKVGErglrLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHT 747
Cdd:COG2401 108 ------RKGDFKDAVELLNAVG------LSDAVLWLRRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180
....*....|....*....|....*
gi 19527665 748 ERNIQAALARVC--ANRTTIIVAHR 770
Cdd:COG2401 172 AKRVARNLQKLArrAGITLVVATHH 196
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
576-797 |
5.81e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 82.20 E-value: 5.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQ--QSLRKAIG 653
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKglMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 654 VVPQ--DTVLFNNTIFYNIEYaklGASDEAVYEaaraADIHERIlgfpEKYETKVGERGLR------LSGGEKQRVAIAR 725
Cdd:PRK13636 86 MVFQdpDNQLFSASVYQDVSF---GAVNLKLPE----DEVRKRV----DNALKRTGIEHLKdkpthcLSFGQKKRVAIAG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19527665 726 TLLKAPIIVLLDEATSALDTHTERNIQAALARVCA--NRTTIIVAHRLSTI-IHADEILVLQQGSIAERGRHEEL 797
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
287-539 |
1.06e-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: 350009 [Multi-domain] Cd Length: 313 Bit Score: 81.84 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 287 RWDFVLIYVALSFLQGGGTGsmgLFNNLRTFLWIRVQQYTTREIEIELFRHLHQLSLRWHLQRKTGEVLRVMdrgTDSIN 366
Cdd:cd18565 49 PRGQLWLLGGLTVAAFLLES---LFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVL---NNDVN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 367 NL---LNYIVFSIAPTILDLLVAVAYFVYaFNWWFGLIVFLTMFLYIASTIaitewrtKYQRRMNLADNEQR-------A 436
Cdd:cd18565 123 QLerfLDDGANSIIRVVVTVLGIGAILFY-LNWQLALVALLPVPLIIAGTY-------WFQRRIEPRYRAVReavgdlnA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 437 RSVDSLLNFETVKYYGAEHYEVDCYREAILKYQKEEFLSMLTLNMLNTAQNIILCLGLLAGSLLCVYLVVH-----HQTL 511
Cdd:cd18565 195 RLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVLDgpplfTGTL 274
|
250 260 270
....*....|....*....|....*....|..
gi 19527665 512 TVGDFVLFSTYLMELYMPLNWFG----TYYRA 539
Cdd:cd18565 275 TVGTLVTFLFYTQRLLWPLTRLGdlidQYQRA 306
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
592-816 |
1.58e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 83.44 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 592 LRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQT--GAILIDGQ-----NIKlvqqQSLRKAIGV-------VPQ 657
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEelqasNIR----DTERAGIAIihqelalVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 658 DTVLFNntIFYNIEYAKLGASD-EAVYeaARAADIHERiLGFPEKYETKVGErglrLSGGEKQRVAIARTLLKAPIIVLL 736
Cdd:PRK13549 97 LSVLEN--IFLGNEITPGGIMDyDAMY--LRAQKLLAQ-LKLDINPATPVGN----LGLGQQQLVEIAKALNKQARLLIL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 737 DEATSALdthTERNIQAALARVCANR----TTIIVAHRLSTIIH-ADEILVLQQGS-IAERGRHEelvLREDGIYADMWQ 810
Cdd:PRK13549 168 DEPTASL---TESETAVLLDIIRDLKahgiACIYISHKLNEVKAiSDTICVIRDGRhIGTRPAAG---MTEDDIITMMVG 241
|
....*.
gi 19527665 811 QQLKNL 816
Cdd:PRK13549 242 RELTAL 247
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
594-796 |
1.65e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 81.84 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 594 NVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDG-------QNIKLVQQQslRKaIGVVPQDTVLFNN-T 665
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaeKGICLPPEK--RR-IGYVFQDARLFPHyK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 666 IFYNIEYAkLGASDEAVYEaaraaDIHErILG-------FPekyetkvgergLRLSGGEKQRVAIARTLLKAPIIVLLDE 738
Cdd:PRK11144 93 VRGNLRYG-MAKSMVAQFD-----KIVA-LLGieplldrYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19527665 739 ATSALDTHTERNIQAALARVCAN-RTTII-VAHRLSTIIH-ADEILVLQQGSIAERGRHEE 796
Cdd:PRK11144 155 PLASLDLPRKRELLPYLERLAREiNIPILyVSHSLDEILRlADRVVVLEQGKVKAFGPLEE 215
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
580-744 |
1.70e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 79.94 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 580 NVTFGYSPEKIVlRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQ-QQSLRKAIGVVPQD 658
Cdd:PRK10895 8 NLAKAYKGRRVV-EDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 659 TVLFNNTIFYNIEYAKLGASDEAVYE--AARAADIHERIlgfpeKYETKVGERGLRLSGGEKQRVAIARTLLKAPIIVLL 736
Cdd:PRK10895 87 ASIFRRLSVYDNLMAVLQIRDDLSAEqrEDRANELMEEF-----HIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL 161
|
....*...
gi 19527665 737 DEATSALD 744
Cdd:PRK10895 162 DEPFAGVD 169
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
556-779 |
1.71e-16 |
|
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: 83.45 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 556 EEEEIVDAPGcsPLLtagGG--IEFSNVTFGYSpEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAI 633
Cdd:TIGR03719 306 ETAEIYIPPG--PRL---GDkvIEAENLTKAFG-DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 634 LIdGQNIKL--VQQQslrkaigvvpQDTVLFNNTIFYNI----EYAKLGAsdeavYE-AARAadiheRILGFPEK---YE 703
Cdd:TIGR03719 380 EI-GETVKLayVDQS----------RDALDPNKTVWEEIsgglDIIKLGK-----REiPSRA-----YVGRFNFKgsdQQ 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 704 TKVGErglrLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARV--CAnrttIIVAH------RLSTII 775
Cdd:TIGR03719 439 KKVGQ----LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFagCA----VVISHdrwfldRIATHI 510
|
....
gi 19527665 776 HADE 779
Cdd:TIGR03719 511 LAFE 514
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
587-758 |
2.61e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 79.74 E-value: 2.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 587 PEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIK-------LVQQQSlrkaiGVVPQDT 659
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpgaergVVFQNE-----GLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 660 VLFNntIFYNIEYAklGASDEAVYEAARAADIHERILGFPEKYEtkvgergLRLSGGEKQRVAIARTLLKAPIIVLLDEA 739
Cdd:PRK11248 87 VQDN--VAFGLQLA--GVEKMQRLEIAHQMLKKVGLEGAEKRYI-------WQLSGGQRQRVGIARALAANPQLLLLDEP 155
|
170
....*....|....*....
gi 19527665 740 TSALDTHTERNIQAALARV 758
Cdd:PRK11248 156 FGALDAFTREQMQTLLLKL 174
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
576-801 |
4.69e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 82.33 E-value: 4.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGVV 655
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 656 PQDTVLFNNTifynieyakLGASDEAVyEAARAADIHERiLGFPEKYETKVGE-RGLRLSGGEKQRVAIARTLLKAPIIV 734
Cdd:PRK10522 403 FTDFHLFDQL---------LGPEGKPA-NPALVEKWLER-LKMAHKLELEDGRiSNLKLSKGQKKRLALLLALAEERDIL 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 735 LLDEATSALDTHTERNI-QAALARVCANRTTII-VAHRLSTIIHADEILVLQQGSIAE-RGRHEELVLRE 801
Cdd:PRK10522 472 LLDEWAADQDPHFRREFyQVLLPLLQEMGKTIFaISHDDHYFIHADRLLEMRNGQLSElTGEERDAASRD 541
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
591-789 |
5.46e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 81.60 E-value: 5.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 591 VLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQ-QQSLRKAIGVVPQD----TVLFNNT 665
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSpRDAIRAGIAYVPEDrkgeGLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 666 IFYNI------EYAKLGASDEAVyEAARAADIHERiLGFpeKY---ETKVGErglrLSGGEKQRVAIARTLLKAPIIVLL 736
Cdd:COG1129 347 IRENItlasldRLSRGGLLDRRR-ERALAEEYIKR-LRI--KTpspEQPVGN----LSGGNQQKVVLAKWLATDPKVLIL 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 19527665 737 DEATSALDTHTERNIQAALARVCANRTTIIVAhrlST----IIH-ADEILVLQQGSIA 789
Cdd:COG1129 419 DEPTRGIDVGAKAEIYRLIRELAAEGKAVIVI---SSelpeLLGlSDRILVMREGRIV 473
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
588-822 |
6.20e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 81.68 E-value: 6.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 588 EKIVLRNVSFTVPAGKTVAIVGPSGAGKS----TIMRLLFRFYDVQT-GAILIDGQNIKLVQQQSLRKA----IGVVPQD 658
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVYPsGDIRFHGESLLHASEQTLRGVrgnkIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 659 TVLFNNTIfYNIE---YAKLGASDEAVYEAARAadiheRILGFPEKYETKVGERGLR-----LSGGEKQRVAIARTLLKA 730
Cdd:PRK15134 101 PMVSLNPL-HTLEkqlYEVLSLHRGMRREAARG-----EILNCLDRVGIRQAAKRLTdyphqLSGGERQRVMIAMALLTR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 731 PIIVLLDEATSALDTHTERNIQAALA--RVCANRTTIIVAHRLSTIIH-ADEILVLQQGSIAERGRHEELVLREDGIYAd 807
Cdd:PRK15134 175 PELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFSAPTHPYT- 253
|
250
....*....|....*
gi 19527665 808 mwqQQLknLDAEQSG 822
Cdd:PRK15134 254 ---QKL--LNSEPSG 263
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
576-786 |
1.25e-15 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 74.41 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSpEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRfYDVQTGAILIDGQNIKlvqqqslrkaIGVV 655
Cdd:cd03221 1 IELENLSKTYG-GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAG-ELEPDEGIVTWGSTVK----------IGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 656 PQdtvlfnntifynieyaklgasdeavyeaaraadiherilgfpekyetkvgerglrLSGGEKQRVAIARTLLKAPIIVL 735
Cdd:cd03221 69 EQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 19527665 736 LDEATSALDTHTERNIQAALARVcaNRTTIIVAH-R--LSTIihADEILVLQQG 786
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEY--PGTVILVSHdRyfLDQV--ATKIIELEDG 143
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
576-797 |
1.30e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 77.57 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSpEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQT-----GAILIDGQNI--KLVQQQSL 648
Cdd:PRK14267 5 IETVNLRVYYG-SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIysPDVDPIEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 649 RKAIGVVPQDTVLFNN-TIFYNI----EYAKLGAS----DEAVYEAARAADIHERIlgfpekyETKVGERGLRLSGGEKQ 719
Cdd:PRK14267 84 RREVGMVFQYPNPFPHlTIYDNVaigvKLNGLVKSkkelDERVEWALKKAALWDEV-------KDRLNDYPSNLSGGQRQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19527665 720 RVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVAHRLSTIIH-ADEILVLQQGSIAERGRHEEL 797
Cdd:PRK14267 157 RLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTRKV 235
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
576-798 |
2.08e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 77.33 E-value: 2.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNI-KLVQQQSLRKAIGV 654
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgDFSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 655 VPQ--DTVLFNNTIFYNIEYAKLGASDEAVyEAARAADIHERILGFpEKYETKVGERglrLSGGEKQRVAIARTLLKAPI 732
Cdd:PRK13644 82 VFQnpETQFVGRTVEEDLAFGPENLCLPPI-EIRKRVDRALAEIGL-EKYRHRSPKT---LSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19527665 733 IVLLDEATSALDTHTERNIQAALARVCANRTTII-VAHRLSTIIHADEILVLQQGSIAERGRHEELV 798
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVyITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
576-797 |
2.26e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 77.44 E-value: 2.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGY-----SPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQ-SLR 649
Cdd:PRK13633 5 IKCKNVSYKYesneeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 650 KAIGVVPQDTvlfNNTIFYNI--EYAKLGASDEAVyeaaRAADIHERI---LGFPEKYETKVGERGLrLSGGEKQRVAIA 724
Cdd:PRK13633 85 NKAGMVFQNP---DNQIVATIveEDVAFGPENLGI----PPEEIRERVdesLKKVGMYEYRRHAPHL-LSGGQKQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19527665 725 RTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANR--TTIIVAHRLSTIIHADEILVLQQGSIAERGRHEEL 797
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
556-779 |
2.31e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 80.16 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 556 EEEEIVDAPGcsPLLtagGG--IEFSNVTFGYSpEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLfrfydvqTGAI 633
Cdd:PRK11819 308 ETNEIFIPPG--PRL---GDkvIEAENLSKSFG-DRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMI-------TGQE 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 634 LIDGQNIKL---VQqqslrkaIGVVPQ--DTVLFNNTIFYNI----EYAKLGAsdeavYE-AARA---------ADiher 694
Cdd:PRK11819 375 QPDSGTIKIgetVK-------LAYVDQsrDALDPNKTVWEEIsgglDIIKVGN-----REiPSRAyvgrfnfkgGD---- 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 695 ilgfPEKyetKVGErglrLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARV--CAnrttIIVAH--- 769
Cdd:PRK11819 439 ----QQK---KVGV----LSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFpgCA----VVISHdrw 503
|
250
....*....|...
gi 19527665 770 ---RLSTIIHADE 779
Cdd:PRK11819 504 fldRIATHILAFE 516
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
580-798 |
3.19e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 76.75 E-value: 3.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 580 NVTFGYsPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGVVPQD- 658
Cdd:PRK10575 16 NVSFRV-PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 659 ------TVlfnntifynieyAKLGASDEAVYEAA----RAADiHERIlgfpEKYETKVGERGL------RLSGGEKQRVA 722
Cdd:PRK10575 95 paaegmTV------------RELVAIGRYPWHGAlgrfGAAD-REKV----EEAISLVGLKPLahrlvdSLSGGERQRAW 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19527665 723 IARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANR--TTIIVAHRLSTII-HADEILVLQQGSIAERGRHEELV 798
Cdd:PRK10575 158 IAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINMAArYCDYLVALRGGEMIAQGTPAELM 236
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
580-797 |
3.21e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 79.90 E-value: 3.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 580 NVTFGYSPEKI-VLRNVSFTVPAGKTVAIVGPSGAGKS----TIMRLLFRF-YDVQTGAILIDGQNIKLV--------QQ 645
Cdd:PRK10261 19 NIAFMQEQQKIaAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAgGLVQCDKMLLRRRSRQVIelseqsaaQM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 646 QSLRKA-IGVVPQDTVLFNNTIFY-------NIEYAKLGASDEAVYEAARAADiHERIlgfPEKyETKVGERGLRLSGGE 717
Cdd:PRK10261 99 RHVRGAdMAMIFQEPMTSLNPVFTvgeqiaeSIRLHQGASREEAMVEAKRMLD-QVRI---PEA-QTILSRYPHQLSGGM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 718 KQRVAIARTLLKAPIIVLLDEATSALDThterNIQA---ALARVCANRTT---IIVAHRLSTIIH-ADEILVLQQGSIAE 790
Cdd:PRK10261 174 RQRVMIAMALSCRPAVLIADEPTTALDV----TIQAqilQLIKVLQKEMSmgvIFITHDMGVVAEiADRVLVMYQGEAVE 249
|
....*..
gi 19527665 791 RGRHEEL 797
Cdd:PRK10261 250 TGSVEQI 256
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
576-792 |
3.42e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 77.08 E-value: 3.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSPEKI----VLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYD-----VQTGAILIDGQNiKLVQQQ 646
Cdd:PRK13643 2 IKFEKVNYTYQPNSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQptegkVTVGDIVVSSTS-KQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 647 SLRKAIGVVPQ--DTVLFNNTIFYNIEYA--KLGASDEavyEAARAADIHERILGFPEKYETKvgeRGLRLSGGEKQRVA 722
Cdd:PRK13643 81 PVRKKVGVVFQfpESQLFEETVLKDVAFGpqNFGIPKE---KAEKIAAEKLEMVGLADEFWEK---SPFELSGGQMRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19527665 723 IARTLLKAPIIVLLDEATSALDTHTERNIQAALARV-CANRTTIIVAHRLSTII-HADEILVLQQGSIAERG 792
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVAdYADYVYLLEKGHIISCG 226
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
595-803 |
4.67e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 75.74 E-value: 4.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 595 VSFTVPAGKTVAIVGPSGAGKSTimrLLFRFYDV--QTGAILIDGQNIKLVQQ--QSLRKAIgVVPQDTVLFNNTIFyni 670
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMAGLlpGSGSIQFAGQPLEAWSAaeLARHRAY-LSQQQTPPFAMPVF--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 671 EYAKLGASDEAVYEAARAAdIHE--RILGFPEKYETKVGerglRLSGGEKQRVAIARTLLK-APII------VLLDEATS 741
Cdd:PRK03695 88 QYLTLHQPDKTRTEAVASA-LNEvaEALGLDDKLGRSVN----QLSGGEWQRVRLAAVVLQvWPDInpagqlLLLDEPMN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19527665 742 ALDTHTERNIQAALARVCANRTTIIVA-HRLS-TIIHADEILVLQQGSIAERGRHEElVLREDG 803
Cdd:PRK03695 163 SLDVAQQAALDRLLSELCQQGIAVVMSsHDLNhTLRHADRVWLLKQGKLLASGRRDE-VLTPEN 225
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
576-738 |
5.06e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 75.96 E-value: 5.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSpEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSL---RKAI 652
Cdd:PRK11831 8 VDMRGVSFTRG-NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 653 GVVPQDTVLF-NNTIFYNIEYaklgasdeAVYEAAR--AADIHERILgfpEKYETkVGERGL------RLSGGEKQRVAI 723
Cdd:PRK11831 87 SMLFQSGALFtDMNVFDNVAY--------PLREHTQlpAPLLHSTVM---MKLEA-VGLRGAaklmpsELSGGMARRAAL 154
|
170
....*....|....*
gi 19527665 724 ARTLLKAPIIVLLDE 738
Cdd:PRK11831 155 ARAIALEPDLIMFDE 169
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
588-786 |
5.43e-15 |
|
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: 74.45 E-value: 5.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 588 EKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGVVPQDTVLFNNTIF 667
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 668 YNIEYAKLGASDEAVYEAAraadiherilgfpekyeTKVGERGL------RLSGGEKQRVAIARTLLKAPIIVLLDEATS 741
Cdd:cd03231 92 ENLRFWHADHSDEQVEEAL-----------------ARVGLNGFedrpvaQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 19527665 742 ALDTHTERNIQAALARVCANRTTIIVAHRLSTIIHADEILVLQQG 786
Cdd:cd03231 155 ALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDLG 199
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
589-738 |
7.72e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 75.07 E-value: 7.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 589 KIVLRNVSFTVPAGKTVAIVGPSGAGKSTImrllfrFY------DVQTGAILIDGQNI-KLVQQQSLRKAIGVVPQDTVL 661
Cdd:COG1137 16 RTVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDItHLPMHKRARLGIGYLPQEASI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 662 FNN-TIFYNIEyaklgasdeAVYEAAR--AADIHERIlgfpekyETKVGE---------RGLRLSGGEKQRVAIARTLLK 729
Cdd:COG1137 90 FRKlTVEDNIL---------AVLELRKlsKKEREERL-------EELLEEfgithlrksKAYSLSGGERRRVEIARALAT 153
|
....*....
gi 19527665 730 APIIVLLDE 738
Cdd:COG1137 154 NPKFILLDE 162
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
576-743 |
1.01e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 74.53 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSpeKI-VLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQ-QSLRKAIG 653
Cdd:PRK11614 6 LSFDKVSAHYG--KIqALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTaKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 654 VVPQDTVLFNN-TIFYNIEYAKLGASDEAVYEaaRAADIHERilgFPEKYETKVgERGLRLSGGEKQRVAIARTLLKAPI 732
Cdd:PRK11614 84 IVPEGRRVFSRmTVEENLAMGGFFAERDQFQE--RIKWVYEL---FPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPR 157
|
170
....*....|.
gi 19527665 733 IVLLDEATSAL 743
Cdd:PRK11614 158 LLLLDEPSLGL 168
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
588-798 |
1.10e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 75.89 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 588 EKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLfrfydvqTGAILIDGQNIKlV-------QQQSLRKAIGVV----- 655
Cdd:COG4586 34 EVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKML-------TGILVPTSGEVR-VlgyvpfkRRKEFARRIGVVfgqrs 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 656 -------PQDTVLFNNTIfYNIeyaklgasDEAVYEaARAADIHErILGFPEKYETKVgeRglRLSGGEKQRVAIARTLL 728
Cdd:COG4586 106 qlwwdlpAIDSFRLLKAI-YRI--------PDAEYK-KRLDELVE-LLDLGELLDTPV--R--QLSLGQRMRCELAAALL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19527665 729 KAPIIVLLDEATSALDTHTERNIQAALARVCANR-TTIIVA-HRLSTIIH-ADEILVLQQGSIAERGRHEELV 798
Cdd:COG4586 171 HRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgTTILLTsHDMDDIEAlCDRVIVIDHGRIIYDGSLEELK 243
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
577-786 |
1.14e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 77.64 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 577 EFSNVTFGYsPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNiklVQQQSLRKAI--GV 654
Cdd:PRK11288 6 SFDGIGKTF-PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE---MRFASTTAALaaGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 655 ---------VPQDTVLFNntIFYNIEYAKLGASDEAVYeAARAADIHERiLGFPEKYETKVGerglRLSGGEKQRVAIAR 725
Cdd:PRK11288 82 aiiyqelhlVPEMTVAEN--LYLGQLPHKGGIVNRRLL-NYEAREQLEH-LGVDIDPDTPLK----YLSIGQRQMVEIAK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19527665 726 TLLKAPIIVLLDEATSALDTHTERNIQAALARVCANRTTII-VAHRLSTIIH-ADEILVLQQG 786
Cdd:PRK11288 154 ALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILyVSHRMEEIFAlCDAITVFKDG 216
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
251-531 |
1.18e-14 |
|
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: 75.50 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 251 VIVCIILLLAGRVIKLFLPIYRKKLVDSLtIAPIVFRWD----FVLIYVALSFLQGggtgsmgLFNNLRTFLWIRVQQYT 326
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDY-IVPGQGDLQglllLALLYLGLLLLSF-------LLQYLQTYLLQKLGQRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 327 TREIEIELFRHLHQLSLRWHLQRKTGEVL-RVM-DrgTDSINNLLNYIVFSIAPTILdLLVAVAYFVYAFNWWFGLIVFL 404
Cdd:cd18544 73 IYDLRRDLFSHIQRLPLSFFDRTPVGRLVtRVTnD--TEALNELFTSGLVTLIGDLL-LLIGILIAMFLLNWRLALISLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 405 TM-FLYIASTIaitewrtkYQRRMNLAdnEQRARSVDSLLN---------FETVKYYGAEHYEVDCYREAILKYQ----K 470
Cdd:cd18544 150 VLpLLLLATYL--------FRKKSRKA--YREVREKLSRLNaflqesisgMSVIQLFNREKREFEEFDEINQEYRkanlK 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19527665 471 EEFLSMLTLNMLNTAQNIILCLGLLAGSLLcvylvVHHQTLTVGDFVLFSTYLMELYMPLN 531
Cdd:cd18544 220 SIKLFALFRPLVELLSSLALALVLWYGGGQ-----VLSGAVTLGVLYAFIQYIQRFFRPIR 275
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
251-545 |
1.22e-14 |
|
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: 75.55 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 251 VIVCIILLLAGRVIKLFLPIYRKKLVDSLTIAPIVFR-WDFVLIYVALSFLQGggtgsmgLFNNLRTFLWIRVQQYTTRE 329
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELlWLLALLILGVALLRG-------VFRYLQGYLAEKASQKVAYD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 330 IEIELFRHLHQLSLRWHLQRKTGEvlrVMDRGT---DSINNLLNYIVFSIAPTILdLLVAVAYFVYAFNWWFGLIVFLTM 406
Cdd:cd18542 74 LRNDLYDHLQRLSFSFHDKARTGD---LMSRCTsdvDTIRRFLAFGLVELVRAVL-LFIGALIIMFSINWKLTLISLAII 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 407 -FLYIASTIAITEWRTKYQR------RMNLADNEqrarsvdSLLNFETVKYYGAEHYEVD-------CYREAILKYQKEE 472
Cdd:cd18542 150 pFIALFSYVFFKKVRPAFEEireqegELNTVLQE-------NLTGVRVVKAFAREDYEIEkfdkeneEYRDLNIKLAKLL 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19527665 473 FLSMLTLNMLNTAQNIILclgLLAGSLLCVylvvhHQTLTVGDFVLFSTYLMELYMPLNWFGTYYRAIQKNFV 545
Cdd:cd18542 223 AKYWPLMDFLSGLQIVLV---LWVGGYLVI-----NGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASA 287
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
592-791 |
1.79e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.97 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 592 LRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKA-IGVVPQDTVLFNN-TIFYN 669
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgIGIIHQELNLIPQlTIAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 670 I----EYA-KLGASD-EAVYeaARAADIHERiLGFPEKYETKVGErglrLSGGEKQRVAIARTL-LKAPIIVlLDEATSA 742
Cdd:PRK10762 100 IflgrEFVnRFGRIDwKKMY--AEADKLLAR-LNLRFSSDKLVGE----LSIGEQQMVEIAKVLsFESKVII-MDEPTDA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 19527665 743 L-DTHTErniqaALARVC-----ANRTTIIVAHRLSTIIH-ADEILVLQQGS-IAER 791
Cdd:PRK10762 172 LtDTETE-----SLFRVIrelksQGRGIVYISHRLKEIFEiCDDVTVFRDGQfIAER 223
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
576-786 |
2.03e-14 |
|
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: 72.66 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTF---GYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYD--VQTGAILIDGQNIKlvqqQSLRK 650
Cdd:cd03232 4 LTWKNLNYtvpVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLD----KNFQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 651 AIGVVPQDTVLFNNTifynieyaklgasdeAVYEAAR-AADIherilgfpekyetkvgeRGLRLSggEKQRVAIARTLLK 729
Cdd:cd03232 80 STGYVEQQDVHSPNL---------------TVREALRfSALL-----------------RGLSVE--QRKRLTIGVELAA 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 730 APIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVA-HRLSTII--HADEILVLQQG 786
Cdd:cd03232 126 KPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTiHQPSASIfeKFDRLLLLKRG 185
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
588-744 |
2.09e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 72.78 E-value: 2.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 588 EKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRK------AIGVVPQDTVL 661
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENilylghLPGLKPELSAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 662 fNNTIFYNieyAKLGASDEAVYEAAraadiherilgfpekyeTKVGERGL------RLSGGEKQRVAIARTLLKAPIIVL 735
Cdd:TIGR01189 92 -ENLHFWA---AIHGGAQRTIEDAL-----------------AAVGLTGFedlpaaQLSAGQQRRLALARLWLSRRPLWI 150
|
....*....
gi 19527665 736 LDEATSALD 744
Cdd:TIGR01189 151 LDEPTTALD 159
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
591-790 |
2.16e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 73.27 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 591 VLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLV---QQQSLR-KAIGVVPQDTVLFNN-T 665
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeARAKLRaKHVGFVFQSFMLIPTlN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 666 IFYNIEYAKL--GASDEAVYEAARA----ADIHERILGFPEKyetkvgerglrLSGGEKQRVAIARTLLKAPIIVLLDEA 739
Cdd:PRK10584 105 ALENVELPALlrGESSRQSRNGAKAlleqLGLGKRLDHLPAQ-----------LSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 19527665 740 TSALDTHTERNIQAALARVcaNR----TTIIVAHRLSTIIHADEILVLQQGSIAE 790
Cdd:PRK10584 174 TGNLDRQTGDKIADLLFSL--NRehgtTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
568-792 |
2.44e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 73.81 E-value: 2.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 568 PLLTAgggiefSNVTFGYSPEKiVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQS 647
Cdd:PRK11701 5 PLLSV------RGLTKLYGPRK-GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 648 L---------RKAIGVV---PQDTVLFNNTIFYNI-EyaKLGASDEAVYEAARAADIH---------ERILGFPEKYetk 705
Cdd:PRK11701 78 LseaerrrllRTEWGFVhqhPRDGLRMQVSAGGNIgE--RLMAVGARHYGDIRATAGDwlerveidaARIDDLPTTF--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 706 vgerglrlSGGEKQRVAIARTLLKAPIIVLLDEATSALDThterNIQAALARVCANRTT------IIVAHRLSTI-IHAD 778
Cdd:PRK11701 153 --------SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDV----SVQARLLDLLRGLVRelglavVIVTHDLAVArLLAH 220
|
250
....*....|....
gi 19527665 779 EILVLQQGSIAERG 792
Cdd:PRK11701 221 RLLVMKQGRVVESG 234
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
254-542 |
3.34e-14 |
|
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: 74.06 E-value: 3.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 254 CIILLLAGRVIKLFLPIYRKKLVDSLTIAPIVFRWD-FVLIYVALSFLQGggtgsmgLFNNLRTFLWIRVQQYTTREIEI 332
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAALGGGDTASLNqIALLLLGLFLLQA-------VFSFFRIYLFARVGERVVADLRK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 333 ELFRHLHQLSLRWHLQRKTGEVLRVMDRGTDSINNLLNYIVFSIAPTILDLLVAVAyFVYAFNWWFGLIVFLTMFLYIAS 412
Cdd:cd18576 74 DLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVV-LLFFISWKLTLLMLATVPVVVLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 413 TIAItewrTKYQRRMNLADNEQRARSV----DSLLNFETVKYYGAEHYEVDCYREAILKYqkeeFLSMLTLNMLNTAQNI 488
Cdd:cd18576 153 AVLF----GRRIRKLSKKVQDELAEANtiveETLQGIRVVKAFTREDYEIERYRKALERV----VKLALKRARIRALFSS 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 19527665 489 ILCLGLLAGSLLCVYLVVHHQ---TLTVGDFVLFSTYLMELYMPLNWFGTYYRAIQK 542
Cdd:cd18576 225 FIIFLLFGAIVAVLWYGGRLVlagELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQK 281
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
556-776 |
4.32e-14 |
|
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: 76.33 E-value: 4.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 556 EEEEIVDAPGCSPLLTAGG-------GIEFSNVTFgYSPEKIVLRN-VSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYD 627
Cdd:TIGR00954 425 EIESGREGGRNSNLVPGRGiveyqdnGIKFENIPL-VTPNGDVLIEsLSFEVPSGNNLLICGPNGCGKSSLFRILGELWP 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 628 VQTGAILIDG-QNIKLVQQQ------SLRkaigvvpqDTVLFNNTIFyniEYAKLGASD---EAVYEAARAADIHERILG 697
Cdd:TIGR00954 504 VYGGRLTKPAkGKLFYVPQRpymtlgTLR--------DQIIYPDSSE---DMKRRGLSDkdlEQILDNVQLTHILEREGG 572
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19527665 698 FpekyeTKVGERGLRLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARvcANRTTIIVAHRLSTIIH 776
Cdd:TIGR00954 573 W-----SAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHRKSLWKY 644
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
581-785 |
4.66e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 72.84 E-value: 4.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 581 VTFGyspEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAIlidgqniklVQQQSLRkaIGVVPQ--- 657
Cdd:PRK09544 12 VSFG---QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---------KRNGKLR--IGYVPQkly 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 658 -DTVL-FNNTIFYNIEYAKLGASDEAVYEAARAADIHErilgFPEKyetkvgerglRLSGGEKQRVAIARTLLKAPIIVL 735
Cdd:PRK09544 78 lDTTLpLTVNRFLRLRPGTKKEDILPALKRVQAGHLID----APMQ----------KLSGGETQRVLLARALLNRPQLLV 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 19527665 736 LDEATSALDThterNIQAAL------ARVCANRTTIIVAHRLSTII-HADEILVLQQ 785
Cdd:PRK09544 144 LDEPTQGVDV----NGQVALydlidqLRRELDCAVLMVSHDLHLVMaKTDEVLCLNH 196
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
252-541 |
5.68e-14 |
|
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: 73.31 E-value: 5.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 252 IVCIILL-LAGRVIKLFLPIYRKKLVDSLtIAPIVFRWDFVLIYVALSFLqgggtGSMGLFNNLRTFLWIRVQQYTTREI 330
Cdd:cd18555 4 LISILLLsLLLQLLTLLIPILTQYVIDNV-IVPGNLNLLNVLGIGILILF-----LLYGLFSFLRGYIIIKLQTKLDKSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 331 EIELFRHLHQLSLRWHLQRKTGEVL-RVMDrgTDSINNLLNYIVFSIaptILDLLVAVAYFVYAF--NWWFGLIVFLTMF 407
Cdd:cd18555 78 MSDFFEHLLKLPYSFFENRSSGDLLfRANS--NVYIRQILSNQVISL---IIDLLLLVIYLIYMLyySPLLTLIVLLLGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 408 LYIASTIaITEWRTKyqrrmNLADNEQRARS------VDSLLNFETVKYYGAEHYEVD----CYREAILKYQKEEFLSmL 477
Cdd:cd18555 153 LIVLLLL-LTRKKIK-----KLNQEEIVAQTkvqsylTETLYGIETIKSLGSEKNIYKkwenLFKKQLKAFKKKERLS-N 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19527665 478 TLNMLNTAQNIILCLGLLagsLLCVYLVVHHQtLTVGDFVLFSTYLMELYMPLNWFGTYYRAIQ 541
Cdd:cd18555 226 ILNSISSSIQFIAPLLIL---WIGAYLVINGE-LTLGELIAFSSLAGSFLTPIVSLINSYNQFI 285
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
592-792 |
8.25e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 72.51 E-value: 8.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 592 LRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDG------------QNIKLVQQQ---SL--RKAIGV 654
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfgdysyrsQRIRMIFQDpstSLnpRQRISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 655 VpQDTVLFNNTIFYNIEYAKlgasdeAVYEAARAADI-HERILGFPEKyetkvgerglrLSGGEKQRVAIARTLLKAPII 733
Cdd:PRK15112 109 I-LDFPLRLNTDLEPEQREK------QIIETLRQVGLlPDHASYYPHM-----------LAPGQKQRLGLARALILRPKV 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19527665 734 VLLDEATSALDTHTERNIQAALARVCANR--TTIIVAHRLSTIIH-ADEILVLQQGSIAERG 792
Cdd:PRK15112 171 IIADEALASLDMSMRSQLINLMLELQEKQgiSYIYVTQHLGMMKHiSDQVLVMHQGEVVERG 232
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
578-798 |
1.25e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 71.65 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 578 FSNVTFGYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLvqqqsLRKAIGVVPQ 657
Cdd:COG1134 28 LLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSAL-----LELGAGFHPE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 658 DT----VLFNNTIfynieyakLGASDEAVyeAARAADIHErilgFPE--KY-ETKVGerglRLSGGEKQRVAIARTLLKA 730
Cdd:COG1134 103 LTgrenIYLNGRL--------LGLSRKEI--DEKFDEIVE----FAElgDFiDQPVK----TYSSGMRARLAFAVATAVD 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 731 PIIVLLDEATSALDTH-TERNIQAALARVCANRTTIIVAHRLSTII-HADEILVLQQGSIAERGRHEELV 798
Cdd:COG1134 165 PDILLVDEVLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRrLCDRAIWLEKGRLVMDGDPEEVI 234
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
594-806 |
1.26e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 71.56 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 594 NVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIK-LVQQQSLRKaiGVVP--QDTVLFNN-TIFYN 669
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEgLPGHQIARM--GVVRtfQHVRLFREmTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 670 IEYA--------------KLGASDEAVYEA-ARAADIHERIlGFPEKYETKVGErglrLSGGEKQRVAIARTLLKAPIIV 734
Cdd:PRK11300 101 LLVAqhqqlktglfsgllKTPAFRRAESEAlDRAATWLERV-GLLEHANRQAGN----LAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19527665 735 LLDEATSALDTHTERNIQAALA--RVCANRTTIIVAHRLSTIIH-ADEILVLQQGSIAERGRHEELVLREDGIYA 806
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAelRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIRNNPDVIKA 250
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
576-787 |
1.91e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.67 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSPEKiVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNI-KLVQQQSLRKAIGV 654
Cdd:PRK09700 6 ISMAGIGKSFGPVH-ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYnKLDHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 655 VPQDTVLFNN-TIFYNIEYAKL------GASDEAVYEAARAADIHERILGFPEKYETKVGErglrLSGGEKQRVAIARTL 727
Cdd:PRK09700 85 IYQELSVIDElTVLENLYIGRHltkkvcGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19527665 728 LKAPIIVLLDEATSALdTHTERNIQAALARVCANRTTIIV--AHRLSTIIH-ADEILVLQQGS 787
Cdd:PRK09700 161 MLDAKVIIMDEPTSSL-TNKEVDYLFLIMNQLRKEGTAIVyiSHKLAEIRRiCDRYTVMKDGS 222
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
566-786 |
2.08e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 74.15 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 566 CSPLLtaGGGIEFSNVTFGYSpEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLF-RFY-DVQTGAILIDGQNIKlv 643
Cdd:PLN03211 61 IKRIL--GHKPKISDETRQIQ-ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQgNNFTGTILANNRKPT-- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 644 qQQSLRKaIGVVPQDTVLFNN-TIFYNIEYAKLGASDEAVY--EAARAADIHERILGFPEKYETKVGERGLR-LSGGEKQ 719
Cdd:PLN03211 136 -KQILKR-TGFVTQDDILYPHlTVRETLVFCSLLRLPKSLTkqEKILVAESVISELGLTKCENTIIGNSFIRgISGGERK 213
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 720 RVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVA-HRLSTIIHA--DEILVLQQG 786
Cdd:PLN03211 214 RVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSmHQPSSRVYQmfDSVLVLSEG 283
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
579-819 |
2.19e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 71.19 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 579 SNVTFGYSPEKiVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQ--SLRKAIGVVP 656
Cdd:PRK13638 5 SDLWFRYQDEP-VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGllALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 657 QDTvlfNNTIFY-----NIEYA--KLGASDEavyEAARAADiherilgfpeKYETKVGERGLR------LSGGEKQRVAI 723
Cdd:PRK13638 84 QDP---EQQIFYtdidsDIAFSlrNLGVPEA---EITRRVD----------EALTLVDAQHFRhqpiqcLSHGQKKRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 724 ARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCAN-RTTIIVAHRLSTIIH-ADEILVLQQGSIAERGRHEELVLRE 801
Cdd:PRK13638 148 AGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQgNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFACT 227
|
250
....*....|....*....
gi 19527665 802 DGI-YADMWQQQLKNLDAE 819
Cdd:PRK13638 228 EAMeQAGLTQPWLVKLHTQ 246
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
592-808 |
2.47e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 73.29 E-value: 2.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 592 LRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQT--GAILIDGQ-----NIKlvqqQSLRKAI-------GVVPQ 657
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEvcrfkDIR----DSEALGIviihqelALIPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 658 DTVLFNntIFYNIEYAKLGASD-EAVYeaARAADIHERIlGFPEKYETKVGERGLrlsgGEKQRVAIARTLLKAPIIVLL 736
Cdd:NF040905 93 LSIAEN--IFLGNERAKRGVIDwNETN--RRARELLAKV-GLDESPDTLVTDIGV----GKQQLVEIAKALSKDVKLLIL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19527665 737 DEATSALDthtERNIQAALARVCANR----TTIIVAHRLSTIIH-ADEILVLQQGSIAERGRHEELVLREDGIYADM 808
Cdd:NF040905 164 DEPTAALN---EEDSAALLDLLLELKaqgiTSIIISHKLNEIRRvADSITVLRDGRTIETLDCRADEVTEDRIIRGM 237
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
251-531 |
3.52e-13 |
|
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: 71.03 E-value: 3.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 251 VIVCIILLLAGRVIKLFLPIYRKKLVDSLTIAPIVFR--WDFVLIYVALSFLQGggtgsmgLFNNLRTFLWIRVQQYTTR 328
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSKSLGllLGLALLLLGAYLLRA-------LLNFLRIYLNHVAEQKVVA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 329 EIEIELFRHLHQLSLRWHLQRKTGEvlrVMDRGTDSINNLLNYIVFSIAPTILDLL--VAVAYFVYAFNWWFGLIVFLTM 406
Cdd:cd18778 74 DLRSDLYDKLQRLSLRYFDDRQTGD---LMSRVINDVANVERLIADGIPQGITNVLtlVGVAIILFSINPKLALLTLIPI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 407 -FLyiastIAITEWRTKYQRRmnLADNEQRARS------VDSLLNFETVKYYGAEHYEVDCYREAILKYQKEeflSMLTL 479
Cdd:cd18778 151 pFL-----ALGAWLYSKKVRP--RYRKVREALGelnallQDNLSGIREIQAFGREEEEAKRFEALSRRYRKA---QLRAM 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 19527665 480 NMLNTAQNIILCLGLLaGSLLCV----YLVVhHQTLTVGDFVLFSTYLMELYMPLN 531
Cdd:cd18778 221 KLWAIFHPLMEFLTSL-GTVLVLgfggRLVL-AGELTIGDLVAFLLYLGLFYEPIT 274
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
592-788 |
3.58e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.43 E-value: 3.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 592 LRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLfrfydvqTGAILID---GQNIKL----VQQQ-----SLRKA---IGVVP 656
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHL-------SGLITGDksaGSHIELlgrtVQREgrlarDIRKSranTGYIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 657 QDTVLFNN-TIFYNIEYAKLGA-----------SDEAVYEAARAAdiherilgfpekyeTKVG------ERGLRLSGGEK 718
Cdd:PRK09984 93 QQFNLVNRlSVLENVLIGALGStpfwrtcfswfTREQKQRALQAL--------------TRVGmvhfahQRVSTLSGGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19527665 719 QRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANR--TTIIVAHRLSTII-HADEILVLQQGSI 788
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDYALrYCERIVALRQGHV 231
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
548-838 |
7.71e-13 |
|
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: 72.74 E-value: 7.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 548 ENMFDLLKEEEeivdAPGCSPlltaggGIEFSNVTFGYSPE-KIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFY 626
Cdd:TIGR01257 911 EGINDSFFERE----LPGLVP------GVCVKNLVKIFEPSgRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLL 980
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 627 DVQTGAILIDGQNIKlVQQQSLRKAIGVVPQDTVLFNN-TIFYNIE-YAKL-GAS-DEAVYE-AARAADI---HERilgf 698
Cdd:TIGR01257 981 PPTSGTVLVGGKDIE-TNLDAVRQSLGMCPQHNILFHHlTVAEHILfYAQLkGRSwEEAQLEmEAMLEDTglhHKR---- 1055
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 699 pekyetkvGERGLRLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVAHRLSTI-IHA 777
Cdd:TIGR01257 1056 --------NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEAdLLG 1127
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19527665 778 DEILVLQQGSIAERGrhEELVLRE---DGIYADMwQQQLKNLDAeQSGGSDNGDASAESGSEKR 838
Cdd:TIGR01257 1128 DRIAIISQGRLYCSG--TPLFLKNcfgTGFYLTL-VRKMKNIQS-QRGGCEGTCSCTSKGFSTR 1187
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
251-542 |
1.06e-12 |
|
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: 69.76 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 251 VIVCIILLLAGRVIKLFLPIYRKKLVDSLTIA-PIVFRWDFVLIYVALSFLQGggtgsmgLFNNLRTFLWIRVQQYTTRE 329
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEkDLEALLLVPLAIIGLFLLRG-------LASYLQTYLMAYVGQRVVRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 330 IEIELFRHLHQLSLRWHLQRKTGEvlrVMDRGTDSINNLLNYIVFSIAPTILDLLVAVAYFVYAF--NWWFGLIVFLTMF 407
Cdd:cd18552 74 LRNDLFDKLLRLPLSFFDRNSSGD---LISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFylDWKLTLIALVVLP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 408 LYIASTIAItewrTKYQRRmnLADNEQRA------RSVDSLLNFETVKYYGAEHYEVDCYREAILKYQKeEFLSMLTLNM 481
Cdd:cd18552 151 LAALPIRRI----GKRLRK--ISRRSQESmgdltsVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRR-LSMKIARARA 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19527665 482 LNTAqnIILCLGLLAGSLLCVY--LVVHHQTLTVGDFVLFSTYLMELYMPLNWFGTYYRAIQK 542
Cdd:cd18552 224 LSSP--LMELLGAIAIALVLWYggYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQR 284
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
580-762 |
1.15e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 67.67 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 580 NVTFGYSpEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIK----LVQQQ--SLRKAIG 653
Cdd:PRK13540 6 ELDFDYH-DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKkdlcTYQKQlcFVGHRSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 654 VVPQDTVLFNntIFYNIEYAklgASDEAVYEAARAADIhERILGFPekyetkvgeRGLrLSGGEKQRVAIARTLLKAPII 733
Cdd:PRK13540 85 INPYLTLREN--CLYDIHFS---PGAVGITELCRLFSL-EHLIDYP---------CGL-LSSGQKRQVALLRLWMSKAKL 148
|
170 180
....*....|....*....|....*....
gi 19527665 734 VLLDEATSALDthtERNIQAALARVCANR 762
Cdd:PRK13540 149 WLLDEPLVALD---ELSLLTIITKIQEHR 174
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
250-519 |
1.33e-12 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 69.16 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 250 AVIVCIILLLAGRVIKLFLPIYRKKLVDSLtiapIVFR-----WDFVLIYVALSFLQGggtgsmgLFNNLRTFLWIRVQQ 324
Cdd:cd18782 3 ALIEVLALSFVVQLLGLANPLLFQVIIDKV----LVQQdlatlYVIGVVMLVAALLEA-------VLTALRTYLFTDTAN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 325 YTTREIEIELFRHLHQLSLRWHLQRKTGEVLRvmdRgTDSINNLLNYIVFSIAPTILDLLVAVAYFV--YAFNWWFGLIV 402
Cdd:cd18782 72 RIDLELGGTIIDHLLRLPLGFFDKRPVGELST---R-ISELDTIRGFLTGTALTTLLDVLFSVIYIAvlFSYSPLLTLVV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 403 FLTMFLYIASTIAITE-WRTKYQRRMNLADNEQrARSVDSLLNFETVKYYGAEHYEVDCYREAILKYQKEEF----LSML 477
Cdd:cd18782 148 LATVPLQLLLTFLFGPiLRRQIRRRAEASAKTQ-SYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFkltvLGTT 226
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 19527665 478 TLNMLNTAQNIILCLGLLAGSllcvYLVVHHQtLTVGDFVLF 519
Cdd:cd18782 227 SGSLSQFLNKLSSLLVLWVGA----YLVLRGE-LTLGQLIAF 263
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
594-788 |
1.83e-12 |
|
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: 70.62 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 594 NVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQ-TGAILIDGQNIKLVQ-QQSLRKAIGVVPQDT----------VL 661
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNpAQAIRAGIAMVPEDRkrhgivpilgVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 662 FNNTIFYNIEYAKLGASDEAVYEAARAADIherilgfpEKYETKVGERGL---RLSGGEKQRVAIARTLLKAPIIVLLDE 738
Cdd:TIGR02633 358 KNITLSVLKSFCFKMRIDAAAELQIIGSAI--------QRLKVKTASPFLpigRLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 19527665 739 ATSALDTHTERNIQAALARVCANRTTIIV-AHRLSTIIH-ADEILVLQQGSI 788
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQLAQEGVAIIVvSSELAEVLGlSDRVLVIGEGKL 481
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
251-534 |
1.86e-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: 68.66 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 251 VIVCIILLLAGRVIKLFLPIYRKKLVDSltiaPIVFR-----WDFVLIYVALSFLQGGGTGsmglfnnLRTFLWIRVQQY 325
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDG----PIAHGdrsalWPLVLLLLALGVAEAVLSF-------LRRYLAGRLSLG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 326 TTREIEIELFRHLHQLSLRWHLQRKTGEVL-RVMdrgTD--SINNLLNYIVFSIApTILDLLVAVAYFVYaFNWWFGLIV 402
Cdd:cd18543 70 VEHDLRTDLFAHLQRLDGAFHDRWQSGQLLsRAT---SDlsLVQRFLAFGPFLLG-NLLTLVVGLVVMLV-LSPPLALVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 403 FLTM-FLYIASTiaitewrtKYQRRMNLADNEQRARSVD-------SLLNFETVKYYGAEHYEVDCYREAILKYQKEEFL 474
Cdd:cd18543 145 LASLpPLVLVAR--------RFRRRYFPASRRAQDQAGDlatvveeSVTGIRVVKAFGRERRELDRFEAAARRLRATRLR 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 475 SMLTLNMLNTAQNIILCLGLLAGSLLCVYLVVHHQtLTVGDFVLFSTYLMELYMPLNWFG 534
Cdd:cd18543 217 AARLRARFWPLLEALPELGLAAVLALGGWLVANGS-LTLGTLVAFSAYLTMLVWPVRMLG 275
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
581-797 |
1.91e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 69.39 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 581 VTFG--YSPEKIVLRnVSFTVPAGKTVAIVGPSGAGKS----TIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIG- 653
Cdd:PRK11022 11 VHFGdeSAPFRAVDR-ISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLVGa 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 654 ---VVPQDTVLFNN---TIFYNI-EYAKL--GASDEAVYEaaRAADIHERIlGFPEKyETKVGERGLRLSGGEKQRVAIA 724
Cdd:PRK11022 90 evaMIFQDPMTSLNpcyTVGFQImEAIKVhqGGNKKTRRQ--RAIDLLNQV-GIPDP-ASRLDVYPHQLSGGMSQRVMIA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 725 RTLLKAPIIVLLDEATSALDThterNIQAALARVC------ANRTTIIVAHRLSTIIH-ADEILVLQQGSIAERGRHEEL 797
Cdd:PRK11022 166 MAIACRPKLLIADEPTTALDV----TIQAQIIELLlelqqkENMALVLITHDLALVAEaAHKIIVMYAGQVVETGKAHDI 241
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
595-797 |
1.94e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 69.35 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 595 VSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNI---KLVQQQSLRKAIGVVPQDTVLFNN---TIFY 668
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmKDDEWRAVRSDIQMIFQDPLASLNprmTIGE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 669 NIE------YAKLgaSDEAVYEAARAAdiherilgfpekyETKVGergLR----------LSGGEKQRVAIARTLLKAPI 732
Cdd:PRK15079 120 IIAeplrtyHPKL--SRQEVKDRVKAM-------------MLKVG---LLpnlinrypheFSGGQCQRIGIARALILEPK 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19527665 733 IVLLDEATSALDThterNIQAALARVCAN------RTTIIVAHRLSTIIH-ADEILVLQQGSIAERGRHEEL 797
Cdd:PRK15079 182 LIICDEPVSALDV----SIQAQVVNLLQQlqremgLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
580-744 |
2.55e-12 |
|
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: 70.35 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 580 NVTFGYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRF-YDVQTGAILIDGqnIKlvqqqslrkaIGVVPQD 658
Cdd:TIGR03719 9 RVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdKDFNGEARPQPG--IK----------VGYLPQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 659 TVLFNN-TIFYNIE----------------YAKLGASD-------------EAVYEAARAADIHERI------LGFPEKy 702
Cdd:TIGR03719 77 PQLDPTkTVRENVEegvaeikdaldrfneiSAKYAEPDadfdklaaeqaelQEIIDAADAWDLDSQLeiamdaLRCPPW- 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 19527665 703 ETKVGErglrLSGGEKQRVAIARTLLKAPIIVLLDEATSALD 744
Cdd:TIGR03719 156 DADVTK----LSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
580-819 |
2.63e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 68.98 E-value: 2.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 580 NVTFGySPEKIV--LRNVSFTVPAGKTVAIVGPSGAGKS----TIMRLLFRfYDVQTGAILIDGQNIKLVQQQSLRK--- 650
Cdd:PRK09473 19 RVTFS-TPDGDVtaVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSATFNGREILNLPEKELNKlra 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 651 -AIGVVPQDTVLFNNTifynieYAKLG-------------ASDEAVYEAARAADI------HERILGFPEKYetkvgerg 710
Cdd:PRK09473 97 eQISMIFQDPMTSLNP------YMRVGeqlmevlmlhkgmSKAEAFEESVRMLDAvkmpeaRKRMKMYPHEF-------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 711 lrlSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCA--NRTTIIVAHRLSTIIH-ADEILVLQQGS 787
Cdd:PRK09473 163 ---SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGR 239
|
250 260 270
....*....|....*....|....*....|..
gi 19527665 788 IAERGRHEELVLREDGIYADMWQQQLKNLDAE 819
Cdd:PRK09473 240 TMEYGNARDVFYQPSHPYSIGLLNAVPRLDAE 271
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
567-797 |
2.64e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.08 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 567 SPLLTAGG-GIEFSNVTfgyspekiVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNI-KLVQ 644
Cdd:PRK15439 9 PPLLCARSiSKQYSGVE--------VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCaRLTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 645 QQSLRKAIGVVPQDTVLFNN-TIFYNIeyaklgasdeaVYEAARAADIHERI------LGFPEKYETKVGErglrLSGGE 717
Cdd:PRK15439 81 AKAHQLGIYLVPQEPLLFPNlSVKENI-----------LFGLPKRQASMQKMkqllaaLGCQLDLDSSAGS----LEVAD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 718 KQRVAIARTLLKAPIIVLLDEATSALDTH-TER---NIQAALARvcaNRTTIIVAHRLSTIIH-ADEILVLQQGSIAERG 792
Cdd:PRK15439 146 RQIVEILRGLMRDSRILILDEPTASLTPAeTERlfsRIRELLAQ---GVGIVFISHKLPEIRQlADRISVMRDGTIALSG 222
|
....*
gi 19527665 793 RHEEL 797
Cdd:PRK15439 223 KTADL 227
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
251-531 |
2.88e-12 |
|
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: 68.20 E-value: 2.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 251 VIVCIILLLAGRVIKLFLPIYRKKLVDSLtIAPIVFRW--DFVLIYVALSFLQGGGTGSMgLFNNLRTFLWIRVQQYTTR 328
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLI-IEGLGGGGgvDFSGLLRILLLLLGLYLLSA-LFSYLQNRLMARVSQRTVY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 329 EIEIELFRHLHQLSLRWHLQRKTGEVL-RV---MDRGTDSINNLLNYIVFSIAptildLLVAVAYFVYAFNWWFGLIVFL 404
Cdd:cd18547 79 DLRKDLFEKLQRLPLSYFDTHSHGDIMsRVtndVDNISQALSQSLTQLISSIL-----TIVGTLIMMLYISPLLTLIVLV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 405 TMFLYIASTIAITEWRTKY--QRRMNLAD-----NEqrarsvdSLLNFETVKYYGAEHYEV-------DCYREAILKYQk 470
Cdd:cd18547 154 TVPLSLLVTKFIAKRSQKYfrKQQKALGElngyiEE-------MISGQKVVKAFNREEEAIeefdeinEELYKASFKAQ- 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19527665 471 eeFLSMLTLNMLNTAQNIILCLGLLAGSLLCVylvvhHQTLTVGDFVLFSTYLMELYMPLN 531
Cdd:cd18547 226 --FYSGLLMPIMNFINNLGYVLVAVVGGLLVI-----NGALTVGVIQAFLQYSRQFSQPIN 279
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
249-520 |
3.29e-12 |
|
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: 67.97 E-value: 3.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 249 IAVIVCIILLLAgrVIKLFLPIYRKKLVDSltiapivfrwdfVLIYVALSFLQ--GGGTGSMGLFNNLRTFLWIRVQQYT 326
Cdd:cd18568 4 LAEILLASLLLQ--LLGLALPLFTQIILDR------------VLVHKNISLLNliLIGLLIVGIFQILLSAVRQYLLDYF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 327 TREIEIEL----FRHLHQLSLRWHLQRKTGEVL-RVMDRgtdsiNNLLNYIVFSIAPTILDLLVAVAYFV--YAFNWWFG 399
Cdd:cd18568 70 ANRIDLSLlsdfYKHLLSLPLSFFASRKVGDIItRFQEN-----QKIRRFLTRSALTTILDLLMVFIYLGlmFYYNLQLT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 400 LIVFLTMFLYIASTIAITEWRTKYQRRMNLADNEQRARSVDSLLNFETVKYYGAEHYEVDCYREAILKYQKEEFLSMLTL 479
Cdd:cd18568 145 LIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLS 224
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 19527665 480 NMLNTAQNIILCLGLLAGSLLCVYLVVHHQtLTVGDFVLFS 520
Cdd:cd18568 225 IVLQLISSLINHLGTIAVLWYGAYLVISGQ-LTIGQLVAFN 264
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
575-744 |
3.81e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 68.72 E-value: 3.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 575 GIEFSNVTFGYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIklvqqQSLRKA--- 651
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV-----NELEPAdrd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 652 IGVVPQDTVLFNN-TIFYNIEY----AKLGAS--DEAVYEAARAADIhERILgfpekyetkvgERGLR-LSGGEKQRVAI 723
Cdd:PRK11650 78 IAMVFQNYALYPHmSVRENMAYglkiRGMPKAeiEERVAEAARILEL-EPLL-----------DRKPReLSGGQRQRVAM 145
|
170 180
....*....|....*....|.
gi 19527665 724 ARTLLKAPIIVLLDEATSALD 744
Cdd:PRK11650 146 GRAIVREPAVFLFDEPLSNLD 166
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
356-738 |
3.86e-12 |
|
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: 69.83 E-value: 3.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 356 RVMDRGTDSINNLLNYiVFSIAPTILDLLVAVAYFVYAFnwWFGLIVFLTMFLYIASTIAItewrtkYQRRMNLADNE-Q 434
Cdd:COG4615 106 RLLAALTEDVRTISQA-FVRLPELLQSVALVLGCLAYLA--WLSPPLFLLTLVLLGLGVAG------YRLLVRRARRHlR 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 435 RARSVDSLLNfetvKYYGA---------------EHYEVDCYREAILKYQKEEFLSMLTLNMLNTAQNIILcLGLLAgsl 499
Cdd:COG4615 177 RAREAEDRLF----KHFRAllegfkelklnrrrrRAFFDEDLQPTAERYRDLRIRADTIFALANNWGNLLF-FALIG--- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 500 LCVYLVVHHQTLTVGDFVLFSTYLMELYMPL----NWFGTYYR---AIQKnfvdMENMFDLLKEEEEIVDAPGCSPLLTA 572
Cdd:COG4615 249 LILFLLPALGWADPAVLSGFVLVLLFLRGPLsqlvGALPTLSRanvALRK----IEELELALAAAEPAAADAAAPPAPAD 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 573 GGGIEFSNVTFGYSPEKI----VLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSL 648
Cdd:COG4615 325 FQTLELRGVTYRYPGEDGdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAY 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 649 RKAIGVVPQDTVLFNNTifynieyakLGASDEAvyEAARAADIHERIlgfpeKYETKVGERG-----LRLSGGEKQRVAI 723
Cdd:COG4615 405 RQLFSAVFSDFHLFDRL---------LGLDGEA--DPARARELLERL-----ELDHKVSVEDgrfstTDLSQGQRKRLAL 468
|
410
....*....|....*.
gi 19527665 724 ARTLL-KAPIIVlLDE 738
Cdd:COG4615 469 LVALLeDRPILV-FDE 483
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
585-744 |
1.77e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.45 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 585 YSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTG-AILIDGQNIklvqqqslrkaiGVVPQDTVLFN 663
Cdd:PRK11819 16 VPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGeARPAPGIKV------------GYLPQEPQLDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 664 N-TIFYNIE----------------YAKLGASD-------------EAVYEAARAADIHERI------LGFPEKyETKVG 707
Cdd:PRK11819 84 EkTVRENVEegvaevkaaldrfneiYAAYAEPDadfdalaaeqgelQEIIDAADAWDLDSQLeiamdaLRCPPW-DAKVT 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 19527665 708 erglRLSGGEKQRVAIARTLLKAPIIVLLDEATSALD 744
Cdd:PRK11819 163 ----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
592-783 |
3.08e-11 |
|
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: 64.56 E-value: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 592 LRNVSFTVPAGKTVAIVGPSGAGKST---------IMRLLFRF------YDVQTGAILIDgqniKLVQ-QQSLrkaIGVV 655
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSlindtlypaLARRLHLKkeqpgnHDRIEGLEHID----KVIViDQSP---IGRT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 656 PQD-----TVLFNN--TIF--------YN-----IEYakLGAS-----DEAVYEA----ARAADIHERI-------LGFp 699
Cdd:cd03271 84 PRSnpatyTGVFDEirELFcevckgkrYNretleVRY--KGKSiadvlDMTVEEAleffENIPKIARKLqtlcdvgLGY- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 700 ekyeTKVGERGLRLSGGEKQRVAIARTLLKA---PIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVA-HRLSTII 775
Cdd:cd03271 161 ----IKLGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIeHNLDVIK 236
|
....*...
gi 19527665 776 HADEILVL 783
Cdd:cd03271 237 CADWIIDL 244
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
587-788 |
3.38e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.49 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 587 PEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYD-VQTGAILIDGQNIKLVQ-QQSLRKAIGVVPQD------ 658
Cdd:PRK13549 273 PHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNpQQAIAQGIAMVPEDrkrdgi 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 659 -TVLfnnTIFYNI------EYAKLGASDEAvyeaARAADIHERILGFPEKY---ETKVGerglRLSGGEKQRVAIARTLL 728
Cdd:PRK13549 353 vPVM---GVGKNItlaaldRFTGGSRIDDA----AELKTILESIQRLKVKTaspELAIA----RLSGGNQQKAVLAKCLL 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19527665 729 KAPIIVLLDEATSALDTHTERNIQ---AALAR--VCanrtTIIVAHRLSTIIH-ADEILVLQQGSI 788
Cdd:PRK13549 422 LNPKILILDEPTRGIDVGAKYEIYkliNQLVQqgVA----IIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
252-530 |
3.64e-11 |
|
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: 65.13 E-value: 3.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 252 IVCIILLLAGRVIKLFLPIYRKKLVDSLTIAPIVFR--WDFVLIYVALSFLqgggtgsMGLFNNLRTFLWIRVQQYTTRE 329
Cdd:cd18541 2 LLGILFLILVDLLQLLIPRIIGRAIDALTAGTLTASqlLRYALLILLLALL-------IGIFRFLWRYLIFGASRRIEYD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 330 IEIELFRHLHQLSLRWHLQRKTGEVlrvMDRGTDSINNL-------LNYIVFSIAptildLLVAVAYFVYAFNWWFGLIV 402
Cdd:cd18541 75 LRNDLFAHLLTLSPSFYQKNRTGDL---MARATNDLNAVrmalgpgILYLVDALF-----LGVLVLVMMFTISPKLTLIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 403 FLTMFLyiastIAITEWRtkYQRRMNLADNE-QRA------RSVDSLLNFETVKYYGAEHYEVDCYREAILKYqKEEFLS 475
Cdd:cd18541 147 LLPLPL-----LALLVYR--LGKKIHKRFRKvQEAfsdlsdRVQESFSGIRVIKAFVQEEAEIERFDKLNEEY-VEKNLR 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 476 MLTLN-----MLNTAQNIILCLGLLAGSllcvYLVVHHQtLTVGDFVLFSTYLMELYMPL 530
Cdd:cd18541 219 LARVDalffpLIGLLIGLSFLIVLWYGG----RLVIRGT-ITLGDLVAFNSYLGMLIWPM 273
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
250-545 |
9.32e-11 |
|
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: 63.64 E-value: 9.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 250 AVIVCIILLLAGRVIKLFLPIYRKKLVDSLTIAPIVFR-WDFVLIYVALSFLQGggtgsmgLFNNLRTFLWIRVQQYTTR 328
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGlLIIALLFLALNLVNW-------VASRLRIYLMAKVGQRILY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 329 EIEIELFRHLHQLSLRWHLQRKTGEVL-RVM-DrgTDSINNLLNYIVFSIAPTILdLLVAVAYFVYAFNWWFGLIVFLTM 406
Cdd:cd18545 74 DLRQDLFSHLQKLSFSFFDSRPVGKILsRVInD--VNSLSDLLSNGLINLIPDLL-TLVGIVIIMFSLNVRLALVTLAVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 407 -FLYIASTIaiteWRTKYQRRMnladneQRARSVDSLLN---------FETVKYYGAEHYEVDCYREAILKYQKEE---- 472
Cdd:cd18545 151 pLLVLVVFL----LRRRARKAW------QRVRKKISNLNaylhesisgIRVIQSFAREDENEEIFDELNRENRKANmrav 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19527665 473 FLSMLTLNMLNTAQNIILCLGLLAGSLLcvylvVHHQTLTVGDFVLFSTYLMELYMPLNWFGTYYRAIQKNFV 545
Cdd:cd18545 221 RLNALFWPLVELISALGTALVYWYGGKL-----VLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMA 288
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
588-792 |
1.08e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 62.74 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 588 EKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRF--YDVQTGAILIDGQNIkLVQQQSLRKAIGvvpqdtvlfnnt 665
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESI-LDLEPEERAHLG------------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 666 IF----YNIEYAKLGASD--EAVYEAARAADIHERI--LGFPEKYETKVGERGLR-----------LSGGEKQRVAIART 726
Cdd:CHL00131 86 IFlafqYPIEIPGVSNADflRLAYNSKRKFQGLPELdpLEFLEIINEKLKLVGMDpsflsrnvnegFSGGEKKRNEILQM 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19527665 727 LLKAPIIVLLDEATSALDTHTERNIQAALARVC-ANRTTIIVAH--RLSTIIHADEILVLQQGSIAERG 792
Cdd:CHL00131 166 ALLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTG 234
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
602-783 |
1.20e-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: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 602 GKTVAIVGPSGAGKSTIMRLLFRFYDVQT-GAILIDGQNIKLVQQQSLRKAIgvvpqdtvlfnntifynieyaklgasde 680
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGgGVIYIDGEDILEEVLDQLLLII---------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 681 avyeaaraadiherilgfpekyetkVGERGLRLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAAL----- 755
Cdd:smart00382 54 -------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrll 108
|
170 180 190
....*....|....*....|....*....|
gi 19527665 756 --ARVCANRTTIIVAHRLSTIIHADEILVL 783
Cdd:smart00382 109 llLKSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
588-768 |
1.61e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 61.36 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 588 EKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRK------AIGVVPQDTVL 661
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDllylghQPGIKTELTAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 662 FNNTIfynieYAKLG--ASDEAVYEAARaadiherilgfpekyetKVGERGL------RLSGGEKQRVAIARTLLKAPII 733
Cdd:PRK13538 93 ENLRF-----YQRLHgpGDDEALWEALA-----------------QVGLAGFedvpvrQLSAGQQRRVALARLWLTRAPL 150
|
170 180 190
....*....|....*....|....*....|....*
gi 19527665 734 VLLDEATSALDTHTERNIQAALARVCANRTTIIVA 768
Cdd:PRK13538 151 WILDEPFTAIDKQGVARLEALLAQHAEQGGMVILT 185
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
251-531 |
2.04e-10 |
|
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: 62.89 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 251 VIVCIILLLAGRVIKLFLPIYRKKLVDSLTIAPivfrwDFVLIYVALSFLQGGGTGSmGLFNNLRTFLWIRVQQYTTREI 330
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDALPQG-----DLGLLVLLALGMVAVAVAS-ALLGVVQTYLSARIGQGVMYDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 331 EIELFRHLHQLSLRWHLQRKTGEVLRVMDRGTDSINNLLNYIVFSIAPTILDLLVAVAyFVYAFNWWFGLIVFLTM--FL 408
Cdd:cd18550 75 RVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLV-AMLALDWRLALLSLVLLplFV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 409 YIASTIAITEWRTKYQRRMNLADneqrarsVDSLLNfET--------VKYYGAEHYEVDCYREailkyqKEEFLSMLTL- 479
Cdd:cd18550 154 LPTRRVGRRRRKLTREQQEKLAE-------LNSIMQ-ETlsvsgallVKLFGREDDEAARFAR------RSRELRDLGVr 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 19527665 480 -NMLNTAQNIILCLGLLAGSLLcVYLV----VHHQTLTVGDFVLFSTYLMELYMPLN 531
Cdd:cd18550 220 qALAGRWFFAALGLFTAIGPAL-VYWVggllVIGGGLTIGTLVAFTALLGRLYGPLT 275
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
251-542 |
2.65e-10 |
|
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: 62.45 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 251 VIVCIILLLAGRVIKLFLPIYRKKLVDSLTIAPIVFRWdfVLIYVALSFLQGggtgsmgLFNNLRTFLWIRVQQYTTREI 330
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGGSSGGL--LALLVALFLLQA-------VLSALSSYLLGRTGERVVLDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 331 EIELFRHLHQLSLRWHLQRKTGEVL-RVM-DrgTDSINNLLNYIVFSIAPTILDLLVAVAYFVYaFNWWFGLIVFLTMFL 408
Cdd:cd18551 72 RRRLWRRLLRLPVSFFDRRRSGDLVsRVTnD--TTLLRELITSGLPQLVTGVLTVVGAVVLMFL-LDWVLTLVTLAVVPL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 409 YIASTIAITEWRTKYQRRMNLADNEQRARSVDSLLNFETVKYYGAEHYEVDCYREAILK-YQ---KEEFLSMLTLNMLNT 484
Cdd:cd18551 149 AFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERlYRaglKAAKIEALIGPLMGL 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 19527665 485 AQNIILCLGLLAGSllcvYLVVHHqTLTVGDFVLFSTYLMELYMPLNWFGTYYRAIQK 542
Cdd:cd18551 229 AVQLALLVVLGVGG----ARVASG-ALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQK 281
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
592-788 |
2.66e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.87 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 592 LRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQ-QQSL----------RKAIGVVPQDTV 660
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpQDGLangivyisedRKRDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 661 LFNNTIFYNIEYAKLGASDEAVYEAARAADIherILGFPEKYETKVGERGLrLSGGEKQRVAIARTLLKAPIIVLLDEAT 740
Cdd:PRK10762 348 KENMSLTALRYFSRAGGSLKHADEQQAVSDF---IRLFNIKTPSMEQAIGL-LSGGNQQKVAIARGLMTRPKVLILDEPT 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 19527665 741 SALDTHTERNIQAALARVCANRTTII-VAHRLSTII-HADEILVLQQGSI 788
Cdd:PRK10762 424 RGVDVGAKKEIYQLINQFKAEGLSIIlVSSEMPEVLgMSDRILVMHEGRI 473
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
542-786 |
4.59e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.59 E-value: 4.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 542 KNFVDMENMFDL----LKEEEEIVDAPGCSPLLTAGGGIEFSNVTF--GYSPEKIV-LRNVSFTVPAGKTVAIVGPSGAG 614
Cdd:TIGR00956 722 SNKNDIEAGEVLgstdLTDESDDVNDEKDMEKESGEDIFHWRNLTYevKIKKEKRViLNNVDGWVKPGTLTALMGASGAG 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 615 KSTIMRLLfrfYDVQTGAILIDGqnIKLVQ----QQSLRKAIGVVPQ-DTVLFNNTIFYNIEY-AKLGASDE-AVYEAAR 687
Cdd:TIGR00956 802 KTTLLNVL---AERVTTGVITGG--DRLVNgrplDSSFQRSIGYVQQqDLHLPTSTVRESLRFsAYLRQPKSvSKSEKME 876
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 688 AADIHERILGFPEKYETKVGERGLRLSGGEKQRVAIARTLLKAP-IIVLLDEATSALDTHTERNIqAALARVCAN--RTT 764
Cdd:TIGR00956 877 YVEEVIKLLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPkLLLFLDEPTSGLDSQTAWSI-CKLMRKLADhgQAI 955
|
250 260
....*....|....*....|....
gi 19527665 765 IIVAHRLSTIIHA--DEILVLQQG 786
Cdd:TIGR00956 956 LCTIHQPSAILFEefDRLLLLQKG 979
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
575-797 |
4.79e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 60.87 E-value: 4.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 575 GIEFSNVTFgySPEKIVLRNVSFTVPAGKTVAIVGPSGAGKS-TIMRLLfrfyDV------QT-GAILIDGQNIKLvqqQ 646
Cdd:PRK10418 4 QIELRNIAL--QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAAL----GIlpagvrQTaGRVLLDGKPVAP---C 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 647 SLR-KAIGVVPQDT-VLFN---NTIFYNIEYAK-LG--ASDEAVYEAARAADIHE--RILG-FPekyetkvgergLRLSG 715
Cdd:PRK10418 75 ALRgRKIATIMQNPrSAFNplhTMHTHARETCLaLGkpADDATLTAALEAVGLENaaRVLKlYP-----------FEMSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 716 GEKQRVAIARTLL-KAPIIVlLDEATSALDTHTERNIQAALARVCANRT--TIIVAHRLSTIIH-ADEILVLQQGSIAER 791
Cdd:PRK10418 144 GMLQRMMIALALLcEAPFII-ADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARlADDVAVMSHGRIVEQ 222
|
....*.
gi 19527665 792 GRHEEL 797
Cdd:PRK10418 223 GDVETL 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
593-789 |
5.16e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 62.76 E-value: 5.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 593 RNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNI-KLVQQQSLRKAIGVVPQD---TVLF-NNTIF 667
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEInALSTAQRLARGLVYLPEDrqsSGLYlDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 668 YNI---EYAKLG-----ASDEAVYEAARAAdiheriLGFpeKYETkvGERGLR-LSGGEKQRVAIARTLLKAPIIVLLDE 738
Cdd:PRK15439 360 WNVcalTHNRRGfwikpARENAVLERYRRA------LNI--KFNH--AEQAARtLSGGNQQKVLIAKCLEASPQLLIVDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 19527665 739 ATSALDTHTERNIQAALARVCANRTTII-VAHRLSTIIH-ADEILVLQQGSIA 789
Cdd:PRK15439 430 PTRGVDVSARNDIYQLIRSIAAQNVAVLfISSDLEEIEQmADRVLVMHQGEIS 482
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
575-796 |
5.40e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 62.62 E-value: 5.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 575 GIEFSNVtFGYSP-----EKIVLRN---------VSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNI 640
Cdd:PRK11288 239 GREIGDI-YGYRPrplgeVRLRLDGlkgpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPI 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 641 KL------VQQQSL-----RKAIGVVPQDTVLFNNTIFYNIEYAKLGASDEAVYEaARAADIHERILgfpeKYETKVGER 709
Cdd:PRK11288 318 DIrsprdaIRAGIMlcpedRKAEGIIPVHSVADNINISARRHHLRAGCLINNRWE-AENADRFIRSL----NIKTPSREQ 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 710 GLR-LSGGEKQRVAIARTLLKAPIIVLLDEATSALDT---HTERNIQAALARvcANRTTIIVAHRLSTIIH-ADEILVLQ 784
Cdd:PRK11288 393 LIMnLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVgakHEIYNVIYELAA--QGVAVLFVSSDLPEVLGvADRIVVMR 470
|
250
....*....|..
gi 19527665 785 QGSIAERGRHEE 796
Cdd:PRK11288 471 EGRIAGELAREQ 482
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
592-816 |
6.58e-10 |
|
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: 62.53 E-value: 6.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 592 LRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQT--GAILIDGQNIKLVQ-QQSLRKAIGVVPQDTVLFNN---- 664
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNiRDTERAGIVIIHQELTLVPElsva 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 665 -TIFYNIEYAKLGA--SDEAVYEAARAADIHERILGFPEKyeTKVGERGlrlsGGEKQRVAIARTLLKAPIIVLLDEATS 741
Cdd:TIGR02633 97 eNIFLGNEITLPGGrmAYNAMYLRAKNLLRELQLDADNVT--RPVGDYG----GGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19527665 742 ALdTHTERNIQAALARVCANR--TTIIVAHRLSTIIH-ADEILVLQQGSiaERGRHEELVLREDGIYADMWQQQLKNL 816
Cdd:TIGR02633 171 SL-TEKETEILLDIIRDLKAHgvACVYISHKLNEVKAvCDTICVIRDGQ--HVATKDMSTMSEDDIITMMVGREITSL 245
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
255-542 |
8.04e-10 |
|
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: 61.02 E-value: 8.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 255 IILLLAGRVIKLFLPIYRKKLVDSLTIAPIVFR-WDFVLIYVALSFLQGggtgsmgLFNNLRTFLWIRVQQYTTREIEIE 333
Cdd:cd18572 2 FVFLVVAALSELAIPHYTGAVIDAVVADGSREAfYRAVLLLLLLSVLSG-------LFSGLRGGCFSYAGTRLVRRLRRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 334 LFRHLHQLSLRWHLQRKTGEVLRVMDRGTDSINNLLNYIVFSIAPTILDLLVAVAYFVYAfNWWFGLIVFLTMFLyiasT 413
Cdd:cd18572 75 LFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSL-SWRLTLLAFITVPV----I 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 414 IAITEWRTKYQRRMNLADNEQRARS----VDSLLNFETVKYYGAEHYEVDCYREAILKY----QKEEFLSMLTLNMLNTA 485
Cdd:cd18572 150 ALITKVYGRYYRKLSKEIQDALAEAnqvaEEALSNIRTVRSFATEEREARRYERALDKAlklsVRQALAYAGYVAVNTLL 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 19527665 486 QNIILCLGLLAGSllcvYLVVHHQtLTVGDFVLFSTYLMELYMPLNWFGTYYRAIQK 542
Cdd:cd18572 230 QNGTQVLVLFYGG----HLVLSGR-MSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQ 281
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
576-744 |
8.48e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 62.57 E-value: 8.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILidgqniklvqqQSLRKAIGVV 655
Cdd:PLN03073 509 ISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF-----------RSAKVRMAVF 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 656 PQDTV----LFNNTIFYNIEYAKlgasdeavyeaaraadiherilGFPE-KYETKVGERGLR----------LSGGEKQR 720
Cdd:PLN03073 578 SQHHVdgldLSSNPLLYMMRCFP----------------------GVPEqKLRAHLGSFGVTgnlalqpmytLSGGQKSR 635
|
170 180
....*....|....*....|....
gi 19527665 721 VAIARTLLKAPIIVLLDEATSALD 744
Cdd:PLN03073 636 VAFAKITFKKPHILLLDEPSNHLD 659
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
587-786 |
8.85e-10 |
|
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: 59.20 E-value: 8.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 587 PEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLfrfydvqTGAIlidGQNIKlvqqqslrkaigvvPQDTVLFNNti 666
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKAL-------ANRT---EGNVS--------------VEGDIHYNG-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 667 fYNIEYAKLGASDEAVYEAARaaDIHERILGFPEKYETKVGERG---LR-LSGGEKQRVAIARTLLKAPIIVLLDEATSA 742
Cdd:cd03233 72 -IPYKEFAEKYPGEIIYVSEE--DVHFPTLTVRETLDFALRCKGnefVRgISGGERKRVSIAEALVSRASVLCWDNSTRG 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 19527665 743 LDTHTERNIQAALaRVCA---NRTTIIVAHRLSTIIHA--DEILVLQQG 786
Cdd:cd03233 149 LDSSTALEILKCI-RTMAdvlKTTTFVSLYQASDEIYDlfDKVLVLYEG 196
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
602-782 |
1.18e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.75 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 602 GKTVAIVGPSGAGKSTIMRLLfrfydvqtgailidgqniklvqqqslrkaIGVVPQD--TVLFNNTIFYNIEYAKlGASD 679
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLL-----------------------------AGVLKPDegEVDPELKISYKPQYIK-PDYD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 680 EAVYEAARAA-----------DIHERiLGFPEKYETKVGErglrLSGGEKQRVAIARTLLKAPIIVLLDEATSALDthTE 748
Cdd:PRK13409 415 GTVEDLLRSItddlgssyyksEIIKP-LQLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLD--VE 487
|
170 180 190
....*....|....*....|....*....|....*....
gi 19527665 749 RNIQAALA--RVCANR--TTIIVAHRLSTI-IHADEILV 782
Cdd:PRK13409 488 QRLAVAKAirRIAEEReaTALVVDHDIYMIdYISDRLMV 526
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
589-792 |
1.33e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.84 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 589 KIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLL-------FRFYDVQ-TGAILIDGQNIKLVQQQSLRKAIGVVPQDTv 660
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALagdltggGAPRGARvTGDVTLNGEPLAAIDAPRLARLRAVLPQAA- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 661 lfnntifyniEYAKLGASDEAV----YEAARAA--------DIHERILGFPEKyETKVGERGLRLSGGEKQRVAIARTLL 728
Cdd:PRK13547 93 ----------QPAFAFSAREIVllgrYPHARRAgalthrdgEIAWQALALAGA-TALVGRDVTTLSGGELARVQFARVLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 729 K---------APIIVLLDEATSALD-THTERNIQA--ALAR-----VCANRTTIIVAHRlstiiHADEILVLQQGSIAER 791
Cdd:PRK13547 162 QlwpphdaaqPPRYLLLDEPTAALDlAHQHRLLDTvrRLARdwnlgVLAIVHDPNLAAR-----HADRIAMLADGAIVAH 236
|
.
gi 19527665 792 G 792
Cdd:PRK13547 237 G 237
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
591-788 |
2.93e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 60.43 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 591 VLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKA-IGVVPQD-----TV---- 660
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPEDrlgrgLVpdms 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 661 LFNNTI---FYNIEYAKLGASD-EAVYEAARaadihERIlgfpEKY-------ETKVGerglRLSGGEKQRVAIARTLLK 729
Cdd:COG3845 353 VAENLIlgrYRRPPFSRGGFLDrKAIRAFAE-----ELI----EEFdvrtpgpDTPAR----SLSGGNQQKVILARELSR 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19527665 730 APIIVLLDEATSALDTHTERNIQAALARVCANRTTIIVahrLST----II-HADEILVLQQGSI 788
Cdd:COG3845 420 DPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLL---ISEdldeILaLSDRIAVMYEGRI 480
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
602-782 |
3.22e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 60.57 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 602 GKTVAIVGPSGAGKSTIMRLLfrfydvqTGAILIDGQNIklvqqqslrkaigvvpqDTVLfnnTIFYNIEYAKlGASDEA 681
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKIL-------AGVLKPDEGEV-----------------DEDL---KISYKPQYIS-PDYDGT 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 682 VYEAARAA------------DIHERiLGFPEKYETKVGErglrLSGGEKQRVAIARTLLKAPIIVLLDEATSALDthTER 749
Cdd:COG1245 418 VEEFLRSAntddfgssyyktEIIKP-LGLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLD--VEQ 490
|
170 180 190
....*....|....*....|....*....|....*...
gi 19527665 750 NIQAA--LARVCANR--TTIIVAHRLSTI-IHADEILV 782
Cdd:COG1245 491 RLAVAkaIRRFAENRgkTAMVVDHDIYLIdYISDRLMV 528
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
602-782 |
3.38e-09 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 58.19 E-value: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 602 GKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIGVVpqDTVLFNNT-IFYNIEYAKLgasde 680
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYEGTV--RDLLSSITkDFYTHPYFKT----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 681 avyEAARAADIhERIlgfpekYETKVGErglrLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVC- 759
Cdd:cd03237 98 ---EIAKPLQI-EQI------LDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAe 163
|
170 180
....*....|....*....|....*
gi 19527665 760 -ANRTTIIVAHRLSTIIH-ADEILV 782
Cdd:cd03237 164 nNEKTAFVVEHDIIMIDYlADRLIV 188
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
576-744 |
3.43e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 60.29 E-value: 3.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYsPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLfrfydvqTGAILIDGQNIKLvqqqSLRKAIGVV 655
Cdd:PRK15064 320 LEVENLTKGF-DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTL-------VGELEPDSGTVKW----SENANIGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 656 PQDTVL-FNN--TIF-YNIEYAKLGASDEAVyeaaRAadiherILG---FPE---KYETKVgerglrLSGGEKQRVAIAR 725
Cdd:PRK15064 388 AQDHAYdFENdlTLFdWMSQWRQEGDDEQAV----RG------TLGrllFSQddiKKSVKV------LSGGEKGRMLFGK 451
|
170
....*....|....*....
gi 19527665 726 TLLKAPIIVLLDEATSALD 744
Cdd:PRK15064 452 LMMQKPNVLVMDEPTNHMD 470
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
577-790 |
3.70e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.18 E-value: 3.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 577 EFSNVTfGYSPEKIvlRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQ-QSLRKAIGVV 655
Cdd:PRK09700 267 EVRNVT-SRDRKKV--RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAVKKGMAYI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 656 PQ---DTVLFNN-TIFYNIEYA---KLGASDEAV-----YEAARAADIHERILGFP-EKYETKVGErglrLSGGEKQRVA 722
Cdd:PRK09700 344 TEsrrDNGFFPNfSIAQNMAISrslKDGGYKGAMglfheVDEQRTAENQRELLALKcHSVNQNITE----LSGGNQQKVL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19527665 723 IARTLLKAPIIVLLDEATSALDTHTERNIQaALARVCAN--RTTIIVAHRLSTIIHA-DEILVLQQGSIAE 790
Cdd:PRK09700 420 ISKWLCCCPEVIIFDEPTRGIDVGAKAEIY-KVMRQLADdgKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
586-768 |
4.39e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.51 E-value: 4.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 586 SPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLL----FRFYDVQTGAILIDGQNIKLVQQQSLRKAIGVVPQDTVL 661
Cdd:TIGR00956 71 TKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 662 FNNTIFYNIEYAKLGAS--------DEAVYeAARAADIHERILGFPEKYETKVGERGLR-LSGGEKQRVAIARTLLKAPI 732
Cdd:TIGR00956 151 PHLTVGETLDFAARCKTpqnrpdgvSREEY-AKHIADVYMATYGLSHTRNTKVGNDFVRgVSGGERKRVSIAEASLGGAK 229
|
170 180 190
....*....|....*....|....*....|....*...
gi 19527665 733 IVLLDEATSALDTHTERNIQAALaRVCAN--RTTIIVA 768
Cdd:TIGR00956 230 IQCWDNATRGLDSATALEFIRAL-KTSANilDTTPLVA 266
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
588-794 |
1.02e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.11 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 588 EKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLF--RFYDVQTGAILIDGQNIkLVQQQSLRKAIGVV-----PQDTV 660
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDL-LELSPEDRAGEGIFmafqyPVEIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 661 LFNNTIFYNI------EYAKLGASDEAVYEAARAADIheRILGFPEKYETKVGERGLrlSGGEKQRVAIARTLLKAPIIV 734
Cdd:PRK09580 92 GVSNQFFLQTalnavrSYRGQEPLDRFDFQDLMEEKI--ALLKMPEDLLTRSVNVGF--SGGEKKRNDILQMAVLEPELC 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19527665 735 LLDEATSALDTHTERNIQAALARV-CANRTTIIVAH--RLSTIIHADEILVLQQGSIAERGRH 794
Cdd:PRK09580 168 ILDESDSGLDIDALKIVADGVNSLrDGKRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDF 230
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
577-747 |
1.18e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.81 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 577 EFSNVTFGYsPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIdGQNIKLVQQQSLRKAIGvvP 656
Cdd:PRK11147 321 EMENVNYQI-DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLEVAYFDQHRAELD--P 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 657 QDTVLFNntifynieyakLGASDEAVYEAARaaDIHerILGF-------PEKYETKVGErglrLSGGEKQRVAIARTLLK 729
Cdd:PRK11147 397 EKTVMDN-----------LAEGKQEVMVNGR--PRH--VLGYlqdflfhPKRAMTPVKA----LSGGERNRLLLARLFLK 457
|
170
....*....|....*...
gi 19527665 730 APIIVLLDEATSALDTHT 747
Cdd:PRK11147 458 PSNLLILDEPTNDLDVET 475
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
587-744 |
1.79e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.88 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 587 PEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLF-RFYDVQ-TGAILIDGQNIKLvqqQSLRKAIG----VVPQDT- 659
Cdd:NF040905 271 PERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgRSYGRNiSGTVFKDGKEVDV---STVSDAIDaglaYVTEDRk 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 660 ----VLfNNTIFYNIEYAKLGA-SDEAVYEAARAADIHERilgFPEKYETK---VGERGLRLSGGEKQRVAIARTLLKAP 731
Cdd:NF040905 348 gyglNL-IDDIKRNITLANLGKvSRRGVIDENEEIKVAEE---YRKKMNIKtpsVFQKVGNLSGGNQQKVVLSKWLFTDP 423
|
170
....*....|...
gi 19527665 732 IIVLLDEATSALD 744
Cdd:NF040905 424 DVLILDEPTRGID 436
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
592-787 |
1.92e-08 |
|
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: 54.64 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 592 LRNVSFTVPAGKTVAIVGPSGAGKSTImrllfrfydVQTGailidgqnIKLVQQQSLRKAIGVVPQDTVLF----NNTIF 667
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL---------VNEG--------LYASGKARLISFLPKFSRNKLIFidqlQFLID 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 668 YNIEYAKLGasdeavyeaaraadiheRILGfpekyetkvgerglRLSGGEKQRVAIARTLLKAP--IIVLLDEATSALDT 745
Cdd:cd03238 74 VGLGYLTLG-----------------QKLS--------------TLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQ 122
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 19527665 746 HTERNIQAALAR-VCANRTTIIVAHRLSTIIHADEILVLQQGS 787
Cdd:cd03238 123 QDINQLLEVIKGlIDLGNTVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
560-744 |
2.19e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 55.24 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 560 IVDAPGCSPLLTAGGGIEFSNvtfgysPEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQN 639
Cdd:PRK13543 1 MIEPLHTAPPLLAAHALAFSR------NEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 640 IKLVQQQSLRKAIGVVP---QDTVLFNNTIFYNIEYAklgasdeavYEAARAADIHERILGFPEKYETKVGErglrLSGG 716
Cdd:PRK13543 75 ATRGDRSRFMAYLGHLPglkADLSTLENLHFLCGLHG---------RRAKQMPGSALAIVGLAGYEDTLVRQ----LSAG 141
|
170 180
....*....|....*....|....*...
gi 19527665 717 EKQRVAIARTLLKAPIIVLLDEATSALD 744
Cdd:PRK13543 142 QKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
576-789 |
4.41e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.66 E-value: 4.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 576 IEFSNVTFGYSPEkivLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIK-------------L 642
Cdd:PRK10982 251 LEVRNLTSLRQPS---IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINnhnaneainhgfaL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 643 VQQQslRKAIGVVPQDTVLFNNTIFYNIEY-AKLGASDEAVYEAARAADIHERILGFPeKYETKVGErglrLSGGEKQRV 721
Cdd:PRK10982 328 VTEE--RRSTGIYAYLDIGFNSLISNIRNYkNKVGLLDNSRMKSDTQWVIDSMRVKTP-GHRTQIGS----LSGGNQQKV 400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 722 AIARTLLKAPIIVLLDEATSALDTHTERNI-QAALARVCANRTTIIVAHRLSTIIH-ADEILVLQQGSIA 789
Cdd:PRK10982 401 IIGRWLLTQPEILMLDEPTRGIDVGAKFEIyQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLVA 470
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
333-530 |
5.97e-08 |
|
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: 55.15 E-value: 5.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 333 ELFRHLHQLSLRWHLQRKTGEvlrVMDRgtdsINNLLNYI--VFSIAPTilDLLVAVAYFVYAF------NWWFGLIVFL 404
Cdd:cd18549 80 DLFEHLQKLSFSFFDNNKTGQ---LMSR----ITNDLFDIseLAHHGPE--DLFISIITIIGSFiilltiNVPLTLIVFA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 405 TMFLYIASTIaitewrtKYQRRMNLADNEQR-------ARSVDSLLNFETVKYYGAEHYEV-------DCYREAILKYQK 470
Cdd:cd18549 151 LLPLMIIFTI-------YFNKKMKKAFRRVRekigeinAQLEDSLSGIRVVKAFANEEYEIekfdegnDRFLESKKKAYK 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 471 EEFLSMLTLNMLNTAQNIILclgLLAGSLLcvylvVHHQTLTVGDFVLFSTYLMELYMPL 530
Cdd:cd18549 224 AMAYFFSGMNFFTNLLNLVV---LVAGGYF-----IIKGEITLGDLVAFLLYVNVFIKPI 275
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
592-786 |
1.06e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.51 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 592 LRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKL-VQQQSLRKAIGVVPQD-TVLFNNTIFYN 669
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFkSSKEALENGISMVHQElNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 670 I---EYAKLG--ASDEAVYEAARAA------DIHERilgfpekyetkvgERGLRLSGGEKQRVAIARTLLKAPIIVLLDE 738
Cdd:PRK10982 94 MwlgRYPTKGmfVDQDKMYRDTKAIfdeldiDIDPR-------------AKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 19527665 739 ATSALD----THTERNIQAALARVCAnrtTIIVAHRLSTIIH-ADEILVLQQG 786
Cdd:PRK10982 161 PTSSLTekevNHLFTIIRKLKERGCG---IVYISHKMEEIFQlCDEITILRDG 210
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
587-798 |
2.20e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 53.65 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 587 PEKIVLRnVSFTVPAGKTVAIVGPSGAGKSTIMRLL--------------FRFYDVQTGAIL------IDGQNIKLVQQ- 645
Cdd:PRK15093 19 WVKAVDR-VSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtkdnwrvtadrMRFDDIDLLRLSprerrkLVGHNVSMIFQe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 646 -QSL--------RKAIGVVPQDTvlfnntiFYNIEYAKLGASDEAVYEAARAADI--HERILG-FPekYEtkvgerglrL 713
Cdd:PRK15093 98 pQSCldpservgRQLMQNIPGWT-------YKGRWWQRFGWRKRRAIELLHRVGIkdHKDAMRsFP--YE---------L 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 714 SGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANRTTII--VAHRLSTIIH-ADEILVLQQGSIAE 790
Cdd:PRK15093 160 TEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTIllISHDLQMLSQwADKINVLYCGQTVE 239
|
....*...
gi 19527665 791 RGRHEELV 798
Cdd:PRK15093 240 TAPSKELV 247
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
711-793 |
2.83e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 51.42 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 711 LRLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVC--ANRTTIIVAHRLSTIIHADEILVLQQGSI 788
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSeeGKKTALVVEHDLAVLDYLSDRIHVFEGEP 149
|
....*
gi 19527665 789 AERGR 793
Cdd:cd03222 150 GVYGI 154
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
588-781 |
4.10e-07 |
|
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: 50.44 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 588 EKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRllfrfydvQTGAILidgqnikLVQQQSLRKAIGVVPQDTVlfnntif 667
Cdd:cd03227 7 FPSYFVPNDVTFGEGSLTIITGPNGSGKSTILD--------AIGLAL-------GGAQSATRRRSGVKAGCIV------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 668 ynieyaklgasdeavyeAARAADIHERILGfpekyetkvgerglrLSGGEKQRVAIARTL----LKAPIIVLLDEATSAL 743
Cdd:cd03227 65 -----------------AAVSAELIFTRLQ---------------LSGGEKELSALALILalasLKPRPLYILDEIDRGL 112
|
170 180 190
....*....|....*....|....*....|....*....
gi 19527665 744 DTHTERNIQAALAR-VCANRTTIIVAHRLSTIIHADEIL 781
Cdd:cd03227 113 DPRDGQALAEAILEhLVKGAQVIVITHLPELAELADKLI 151
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
602-773 |
4.20e-07 |
|
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: 53.63 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 602 GKTVAIVGPSGAGKSTIMRLL--------------------FRFYdvqTGAILidGQNIKLVQQQSLRKAIGvvPQdtvl 661
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILsgelkpnlgdydeepswdevLKRF---RGTEL--QDYFKKLANGEIKVAHK--PQ---- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 662 fnntifyNIEYA----KLGASD--EAVYEAARAADIHERiLGFPEKYETKVGErglrLSGGEKQRVAIARTLLKAPIIVL 735
Cdd:COG1245 168 -------YVDLIpkvfKGTVREllEKVDERGKLDELAEK-LGLENILDRDISE----LSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 19527665 736 LDEATSALDTHtERnIQAA-----LARvcANRTTIIVAHRLST 773
Cdd:COG1245 236 FDEPSSYLDIY-QR-LNVArlireLAE--EGKYVLVVEHDLAI 274
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
602-771 |
5.77e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.27 E-value: 5.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 602 GKTVAIVGPSGAGKSTIMRLL--------------------FRFYdvqTGAILidgQN-IKLVQQQSLRKAigVVPQdtv 660
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILsgelipnlgdyeeepswdevLKRF---RGTEL---QNyFKKLYNGEIKVV--HKPQ--- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 661 lfnntifYnIEYA------KLGASDEAVYEAARAADIHERiLGFpekyeTKVGERGLR-LSGGEKQRVAIARTLLKAPII 733
Cdd:PRK13409 168 -------Y-VDLIpkvfkgKVRELLKKVDERGKLDEVVER-LGL-----ENILDRDISeLSGGELQRVAIAAALLRDADF 233
|
170 180 190
....*....|....*....|....*....|....*....
gi 19527665 734 VLLDEATSALDThTER-NIQAALARVCANRTTIIVAHRL 771
Cdd:PRK13409 234 YFFDEPTSYLDI-RQRlNVARLIRELAEGKYVLVVEHDL 271
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
583-747 |
6.79e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.03 E-value: 6.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 583 FGYSPekiVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDgQNIKL--VQQQSLRKAIGVV----- 655
Cdd:PRK11147 13 FSDAP---LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLIVarLQQDPPRNVEGTVydfva 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 656 -----------------------PQDTVLfNntifyniEYAKLgasdEAVYEAARAADIHERI------LGFPEkyETKV 706
Cdd:PRK11147 89 egieeqaeylkryhdishlvetdPSEKNL-N-------ELAKL----QEQLDHHNLWQLENRInevlaqLGLDP--DAAL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 19527665 707 GErglrLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHT 747
Cdd:PRK11147 155 SS----LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
322-531 |
7.57e-07 |
|
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350013 [Multi-domain] Cd Length: 294 Bit Score: 51.71 E-value: 7.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 322 VQQYTTREIEIEL--------FRHLHQLSLRWHLQRKTGEVL-RVmdRGTDSINNLLnyiVFSIAPTILDLLVAVAYFV- 391
Cdd:cd18569 61 LQQYYLLRLETKLalssssrfFWHVLRLPVEFFSQRYAGDIAsRV--QSNDRVANLL---SGQLATTVLNLVMAVFYALl 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 392 -YAFNWWFGLIVFLTMFLYIASTIAITEWRTKYQRRMNLADNEQRARSVDSLLNFETVKYYGAEHYevdcYREAILKYQ- 469
Cdd:cd18569 136 mLQYDVPLTLIGIAIALLNLLVLRLVSRKRVDLNRRLLQDSGKLTGTTMSGLQMIETLKASGAESD----FFSRWAGYQa 211
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19527665 470 -----------KEEFLSMLT--LNMLNTAqnIILCLGllagsllcVYLVVHHQtLTVGDFVLFSTYLMELYMPLN 531
Cdd:cd18569 212 kvlnaqqelgrTNQLLGALPtlLSALTNA--AILGLG--------GLLVMDGA-LTIGMLVAFQSLMASFLAPVN 275
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
254-523 |
7.62e-07 |
|
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: 51.79 E-value: 7.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 254 CIILLLAGRVIKLFLPIYRKKLVDSL--TIAPIVFRWDFvLIYVALSFLQGggtgsmgLFNNLRTFLWIRVQQYTTREIE 331
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIikGGDLDVLNELA-LILLAIYLLQS-------VFTFVRYYLFNIAGERIVARLR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 332 IELFRHLHQLSLRWHLQRKTGEVLRVMDRGTDSINNLLNyivFSIAPTILDLLVAVAYFVyaFNWWFGLIVFLTMFLYIA 411
Cdd:cd18557 73 RDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVT---DNLSQLLRNILQVIGGLI--ILFILSWKLTLVLLLVIP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 412 STIAITEWRTKYQRRMN--LADNEQRARSV--DSLLNFETVKYYGAEHYEVDCYREAILKYQKEEFLSMLTLNMLNTAQN 487
Cdd:cd18557 148 LLLIASKIYGRYIRKLSkeVQDALAKAGQVaeESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITS 227
|
250 260 270
....*....|....*....|....*....|....*....
gi 19527665 488 IILCLGLLAGSLLCVYLVVHHQtLTVGD---FVLFSTYL 523
Cdd:cd18557 228 LLIYLSLLLVLWYGGYLVLSGQ-LTVGEltsFILYTIMV 265
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
581-839 |
1.17e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.09 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 581 VTFGYSpEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIdGQNIKLvqqqslrkaiGVVPQdtv 660
Cdd:PRK10636 318 VSAGYG-DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIKL----------GYFAQ--- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 661 lfnntifYNIEYakLGASDEAVYEAARAAD------IHERILGFPEKYEtKVGERGLRLSGGEKQRVAIARTLLKAPIIV 734
Cdd:PRK10636 383 -------HQLEF--LRADESPLQHLARLAPqeleqkLRDYLGGFGFQGD-KVTEETRRFSGGEKARLVLALIVWQRPNLL 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 735 LLDEATSALDTHTERNIQAALarVCANRTTIIVAHrlstiihaDEILVlqqgsiaeRGRHEELVLREDGIYA------DM 808
Cdd:PRK10636 453 LLDEPTNHLDLDMRQALTEAL--IDFEGALVVVSH--------DRHLL--------RSTTDDLYLVHDGKVEpfdgdlED 514
|
250 260 270
....*....|....*....|....*....|....*.
gi 19527665 809 WQQQLKNLDAEQSGGSD-----NGDASAESGSEKRR 839
Cdd:PRK10636 515 YQQWLSDVQKQENQTDEapkenNANSAQARKDQKRR 550
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
291-530 |
2.15e-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: 50.18 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 291 VLIYVALSFLQGGGTGsmglfnnLRTFLWIRVQQYTTREIEIELFRHLHQLSLRWHLQRKTGevlRVMDRGT---DSINN 367
Cdd:cd18546 42 AAAYLAVVLAGWVAQR-------AQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHERETSG---RIMTRMTsdiDALSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 368 LLNYIVFSIAPTILDLL-VAVAYFVyaFNWWFGLIVFLTM-FLYIAstiaiTEWrtkYQRRMNLADNEQRARSVDSLLNF 445
Cdd:cd18546 112 LLQTGLVQLVVSLLTLVgIAVVLLV--LDPRLALVALAALpPLALA-----TRW---FRRRSSRAYRRARERIAAVNADL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 446 -ET------VKYYGAEHY-------EVDCYREAILKYQKE--------EFLSMLTlnmlnTAqniilcLGLLAGSLLcvy 503
Cdd:cd18546 182 qETlagirvVQAFRRERRnaerfaeLSDDYRDARLRAQRLvaiyfpgvELLGNLA-----TA------AVLLVGAWR--- 247
|
250 260
....*....|....*....|....*..
gi 19527665 504 lvVHHQTLTVGDFVLFSTYLMELYMPL 530
Cdd:cd18546 248 --VAAGTLTVGVLVAFLLYLRRFFAPI 272
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
249-530 |
3.02e-06 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 49.85 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 249 IAVIVCIILLLagRVIKLFLPIYRKKLVDSltiapIVFRWDFVLIYVAlsflqGGGTGSMGLFNN----LRTFLWIRVQQ 324
Cdd:cd18779 4 LGQILLASLLL--QLLGLALPLLTGVLVDR-----VIPRGDRDLLGVL-----GLGLAALVLTQLlaglLRSHLLLRLRT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 325 YTTREIEIELFRHLHQLSLRWHLQRKTGEVL-RVmdRGTDSINNLLNYIVFSiapTILDLLVAVAYFV--YAFNWWFGLI 401
Cdd:cd18779 72 RLDTQLTLGFLEHLLRLPYRFFQQRSTGDLLmRL--SSNATIRELLTSQTLS---ALLDGTLVLGYLAllFAQSPLLGLV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 402 VFLTMFLYIAsTIAITewrTKYQRRMNLADNEQRARS----VDSLLNFETVKYYGAEHYEVDCYREAILKYQKEEFLSML 477
Cdd:cd18779 147 VLGLAALQVA-LLLAT---RRRVRELMARELAAQAEAqsylVEALSGIETLKASGAEDRALDRWSNLFVDQLNASLRRGR 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 19527665 478 TLNMLNTAQNIILCLGLLAGSLLCVYLVVHHQtLTVGDFVLFSTYLMELYMPL 530
Cdd:cd18779 223 LDALVDALLATLRLAAPLVLLWVGAWQVLDGQ-LSLGTMLALNALAGAFLAPL 274
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
334-522 |
3.64e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 49.77 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 334 LFRHLHQLSLRWHLQRKTGEVL-RVmdrgtDSINNLLNYIVFSIAPTILDLLVAVAYFV--YAFNWWFGLIVFLTMFLYI 410
Cdd:cd18567 81 LFRHLLRLPLSYFEKRHLGDIVsRF-----GSLDEIQQTLTTGFVEALLDGLMAILTLVmmFLYSPKLALIVLAAVALYA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 411 ASTIAItewrTKYQRRMNL----ADNEQRARSVDSLLNFETVKYYGAEHYEVDCYREAILKYQKEEF-LSMLTLNmLNTA 485
Cdd:cd18567 156 LLRLAL----YPPLRRATEeqivASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIrLQRLQIL-FSAA 230
|
170 180 190
....*....|....*....|....*....|....*..
gi 19527665 486 QNIILCLGLLAGSLLCVYLVVhHQTLTVGDFVLFSTY 522
Cdd:cd18567 231 NGLLFGLENILVIYLGALLVL-DGEFTVGMLFAFLAY 266
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
599-771 |
4.41e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 50.78 E-value: 4.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 599 VPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIkLVQQQSLRKAIGVVPQ----DTVLFNNTIFYniEYAK 674
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISDVHQNMGYCPQfdaiDDLLTGREHLY--LYAR 2038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 675 L-GASDEavyEAARAADIHERILGFPEKYETKVGErglrLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTER---N 750
Cdd:TIGR01257 2039 LrGVPAE---EIEKVANWSIQSLGLSLYADRLAGT----YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRmlwN 2111
|
170 180
....*....|....*....|.
gi 19527665 751 IQAALARvcANRTTIIVAHRL 771
Cdd:TIGR01257 2112 TIVSIIR--EGRAVVLTSHSM 2130
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
579-769 |
5.58e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.89 E-value: 5.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 579 SNVT--FGYSPekiVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILID-GQNI-KLVQQQSLRKAIGV 654
Cdd:PRK15064 5 ANITmqFGAKP---LFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDpNERLgKLRQDQFAFEEFTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 655 VpqDTVLFNNTIFYNIE------YAKLGASDEAVYEAA----------------RAADIherIL--GFPEKYETkvgerG 710
Cdd:PRK15064 82 L--DTVIMGHTELWEVKqerdriYALPEMSEEDGMKVAdlevkfaemdgytaeaRAGEL---LLgvGIPEEQHY-----G 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19527665 711 L--RLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAAL-ARVCanrTTIIVAH 769
Cdd:PRK15064 152 LmsEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLnERNS---TMIIISH 210
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
592-780 |
1.22e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 47.25 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 592 LRNVSFTVPAGKTVAIVGPSGAGKSTIM----------RLL------FRF---------YDVQTG---AILIDGQNIKlv 643
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrRYVeslsayARQflgqmdkpdVDSIEGlspAIAIDQKTTS-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 644 qqQSLRKAIGVVpqdTVLFNntiFYNIEYAKLGasdeavyeaaraadIHERI-----LGFPekYETkVGERGLRLSGGEK 718
Cdd:cd03270 89 --RNPRSTVGTV---TEIYD---YLRLLFARVG--------------IRERLgflvdVGLG--YLT-LSRSAPTLSGGEA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19527665 719 QRVAIARTL---LKApIIVLLDEATSALDTHTERNIQAALARV-CANRTTIIVAHRLSTIIHADEI 780
Cdd:cd03270 144 QRIRLATQIgsgLTG-VLYVLDEPSIGLHPRDNDRLIETLKRLrDLGNTVLVVEHDEDTIRAADHV 208
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
244-539 |
1.51e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 47.66 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 244 NIALQIAVIVCIIL---LLAGRVIKLFLPIYRKKLVDSLTIapivfrwdFVLIYValsflqgggtgsmglfnnLRT-FLW 319
Cdd:cd18561 1 SVLLGLLITALYIAqawLLARALARIFAGGPWEDIMPPLAG--------IAGVIV------------------LRAaLLW 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 320 IR--VQQYTT----REIEIELFRHLHQLSLRWHLQRKTGEVLRVMdrgTDSINNLLNYIVFSIAPTILDLLVAVAYFVYA 393
Cdd:cd18561 55 LRerVAHRAAqrvkQHLRRRLFAKLLKLGPGYLEGERTGELQTTV---VDGVEALEAYYGRYLPQLLVALLGPLLILIYL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 394 F--NWWFGLIVFLTMFLYIASTIAITEWRTKYQRRMNLADNEQRARSVDSLLNFETVKYYGAEhyevDCYREAiLKYQKE 471
Cdd:cd18561 132 FflDPLVALILLVFALLIPLSPALWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGAS----KRRGNE-LAARAE 206
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19527665 472 EFL--SMLTLNMLNTAQNIILCLGLLAGSLLCVYLVVHHQ----TLTVGDFVLFSTylMELYMPLNWFGTYYRA 539
Cdd:cd18561 207 DLRqaTMKVLAVSLLSSGIMGLATALGTALALGVGALRVLggqlTLSSLLLILFLS--REFFRPLRDLGAYWHA 278
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
638-797 |
2.83e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.93 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 638 QNIKLVQQQ-----SLRKAIGVVPQDTVLFNNTIFYNIE--YAKLGASDEAVYEAaRAADIHERiLGFPEKYETKvgeRG 710
Cdd:PLN03073 268 EEAQLVAQQrelefETETGKGKGANKDGVDKDAVSQRLEeiYKRLELIDAYTAEA-RAASILAG-LSFTPEMQVK---AT 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 711 LRLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARvcANRTTIIVAHR---LSTIIhaDEILVLQQGS 787
Cdd:PLN03073 343 KTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLK--WPKTFIVVSHArefLNTVV--TDILHLHGQK 418
|
170
....*....|....*....
gi 19527665 788 IA---------ERGRHEEL 797
Cdd:PLN03073 419 LVtykgdydtfERTREEQL 437
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
592-744 |
4.05e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.43 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 592 LRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIklvQQQSLRKA----IGVVPQDtvLFNN--- 664
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDM---ADARHRRAvcprIAYMPQG--LGKNlyp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 665 --TIFYNIEY-AKL-GASdeavyEAARAADIHE-----RILGFPEKYETKvgerglrLSGGEKQRVAIARTLLKAPIIVL 735
Cdd:NF033858 92 tlSVFENLDFfGRLfGQD-----AAERRRRIDEllratGLAPFADRPAGK-------LSGGMKQKLGLCCALIHDPDLLI 159
|
....*....
gi 19527665 736 LDEATSALD 744
Cdd:NF033858 160 LDEPTTGVD 168
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
251-532 |
4.80e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 46.32 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 251 VIVCIILLLAGRVIKLFLPIYRKKLVDSLtIAPIVFR--WDFVLIYVALSFLQGGGTGSMglfnnlrTFLWIRVQQYTTR 328
Cdd:cd18540 4 LILLIILMLLVALLDAVFPLLTKYAIDHF-ITPGTLDglTGFILLYLGLILIQALSVFLF-------IRLAGKIEMGVSY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 329 EIEIELFRHLHQLSLRWHLQRKTGEVL-RVM-DrgTDSINNLLNY----IVFSIAptildLLVAVAYFVYAFNWWFGLIV 402
Cdd:cd18540 76 DLRKKAFEHLQTLSFSYFDKTPVGWIMaRVTsD--TQRLGEIISWglvdLVWGIT-----YMIGILIVMLILNWKLALIV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 403 FLTM-FLYIASTIaitewrtkYQRRMnLADNeQRARSVDSLL--NF-------ETVKYYGAEhyevdcyreailKYQKEE 472
Cdd:cd18540 149 LAVVpVLAVVSIY--------FQKKI-LKAY-RKVRKINSRItgAFnegitgaKTTKTLVRE------------EKNLRE 206
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19527665 473 FLSmLTLNMLNTA----------QNIILCLGLLAGSLLCVY--LVVHHQTLTVGDFVLFSTYLMELYMPLNW 532
Cdd:cd18540 207 FKE-LTEEMRRASvraarlsalfLPIVLFLGSIATALVLWYggILVLAGAITIGTLVAFISYATQFFEPIQQ 277
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
705-783 |
4.94e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 47.32 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 705 KVGERGLRLSGGEKQRVAIARTLLK---APIIVLLDEATSALDTHTERNIQAALARVCANRTTIIV-AHRLSTIIHADEI 780
Cdd:TIGR00630 822 RLGQPATTLSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVViEHNLDVIKTADYI 901
|
...
gi 19527665 781 LVL 783
Cdd:TIGR00630 902 IDL 904
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
599-772 |
7.72e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 45.44 E-value: 7.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 599 VPA-GKTVAIVGPSGAGKSTIMRLLF--------RFYDVQTGAILID---GQNIKLVQQQSLRKAIGVV--PQDTVLFNN 664
Cdd:cd03236 22 VPReGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYFTKLLEGDVKVIvkPQYVDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 665 TIFYNIEyAKLGASDEavyeaaraadiheriLGFPEKYETKVGERGLR------LSGGEKQRVAIARTLLKAPIIVLLDE 738
Cdd:cd03236 102 AVKGKVG-ELLKKKDE---------------RGKLDELVDQLELRHVLdrnidqLSGGELQRVAIAAALARDADFYFFDE 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 19527665 739 ATSALDTHtERNIQAALARVCA--NRTTIIVAHRLS 772
Cdd:cd03236 166 PSSYLDIK-QRLNAARLIRELAedDNYVLVVEHDLA 200
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
251-530 |
7.87e-05 |
|
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: 45.47 E-value: 7.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 251 VIVCIILLLAGRVIKLFLPIYRKKLVDSLTIA---PIVFRWDFVLIYVAL-SFLQGGGTG------SMGLFNNLRTFLWI 320
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDEGIANgdlSYILRTGLLMLLLALlGLIAGILAGyfaakaSQGFGRDLRKDLFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 321 RVQQYTTREIEielfrHLHQLSLrwhlqrktgevlrvMDRGTDSINNLLNYIVFSIAPTILDLLVAVAYFVYAF--NWWF 398
Cdd:cd18548 81 KIQSFSFAEID-----KFGTSSL--------------ITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFriNPKL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 399 GLIVFLTMFLyIASTIAITEWRT-----KYQR---RMNLADNEQrarsvdsLLNFETVKYYGAEHYEVDCYREAILKYQK 470
Cdd:cd18548 142 ALILLVAIPI-LALVVFLIMKKAiplfkKVQKkldRLNRVVREN-------LTGIRVIRAFNREDYEEERFDKANDDLTD 213
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 471 EEFLSMLTLNMLNTAQNIILCLGLLAGSLLCVYLVVHHqTLTVGDFVLFSTYLMELYMPL 530
Cdd:cd18548 214 TSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAG-SLQVGDLVAFINYLMQILMSL 272
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
253-534 |
8.49e-05 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 45.55 E-value: 8.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 253 VCIILLLAGRVIKLFLPIYRKKLVDSLTIAPIVFRWDFVLIYVALSFLQGGGTGSMGLFNNLRTFLWIRVQQYTTREIei 332
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLI-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 333 elFRHLHQLSLRWHLQRKTGEVLRVM--DrgTDSINNLLNYIVFSIApTILDLLVAVaYFVYAFNWWFGLIVFLTMFLYI 410
Cdd:cd18579 79 --YRKALRLSSSARQETSTGEIVNLMsvD--VQRIEDFFLFLHYLWS-APLQIIVAL-YLLYRLLGWAALAGLGVLLLLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 411 ASTIAITEWRTKYQRR-MNLADneQRARSVDSLLN-FETVKYYGAEhyevDCYREAILKYQKEEFLSMLTLNMLNTAQNI 488
Cdd:cd18579 153 PLQAFLAKLISKLRKKlMKATD--ERVKLTNEILSgIKVIKLYAWE----KPFLKRIEELRKKELKALRKFGYLRALNSF 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 19527665 489 ILCLGLLAGSLLC--VYLVVHHqTLTVGD-FVLFSTYLMeLYMPLNWFG 534
Cdd:cd18579 227 LFFSTPVLVSLATfaTYVLLGN-PLTAAKvFTALSLFNL-LRFPLLMLP 273
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
255-524 |
1.33e-04 |
|
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: 44.77 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 255 IILLLAGRVIKLFLPIYrkklvdSLTIAPIVFRWD---FVLIYVALSFLqgggtgsMGLFNNLRTFLWIRVQQYTTREIE 331
Cdd:cd18577 17 LMTIVFGDLFDAFTDFG------SGESSPDEFLDDvnkYALYFVYLGIG-------SFVLSYIQTACWTITGERQARRIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 332 IELFRHLHQLSLRWHLQRKTGEVLRVMDRGTDSINNL----LNYIVFSIAptildllVAVAYFVYAF--NWWFGLIVFLT 405
Cdd:cd18577 84 KRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGigekLGLLIQSLS-------TFIAGFIIAFiySWKLTLVLLAT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 406 MFLYIASTIAITEWRTKYQRRMNLADNEqrARSV--DSLLNFETVKYYGAEHYEVDCYREAILK----YQKEEFLSMLTL 479
Cdd:cd18577 157 LPLIAIVGGIMGKLLSKYTKKEQEAYAK--AGSIaeEALSSIRTVKAFGGEEKEIKRYSKALEKarkaGIKKGLVSGLGL 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 19527665 480 NMLNTAQNIILCLGLLAGSLLcvylvVHHQTLTVGD-FVLFSTYLM 524
Cdd:cd18577 235 GLLFFIIFAMYALAFWYGSRL-----VRDGEISPGDvLTVFFAVLI 275
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
362-533 |
1.68e-04 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350040 [Multi-domain] Cd Length: 309 Bit Score: 44.41 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 362 TDSINNLLNYIVFSIApTILDLLVAVaYFVYAFNWWFGLIVFLTMFLYIASTIAITEWRTKYQRR-MNLADneQRARSVD 440
Cdd:cd18596 125 ANRISEFAAFLHLLVS-APLQIVIAI-VFLYRLLGWSALVGLAVMVLLLPLNGYLAKRYSRAQKElMKARD--ARVQLVT 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 441 SLLN-FETVKYYGAEHY---EVDCYREAILKYQKEEFLSMLTLNMLNTAQNIILCLgllagSLLCVYLVVHHQTLTVGdf 516
Cdd:cd18596 201 EVLQgIRMIKFFAWERKweeRILEAREEELKWLRKRFLLDLLLSLLWFLIPILVTV-----VTFATYTLVMGQELTAS-- 273
|
170
....*....|....*....
gi 19527665 517 VLFS--TYLMELYMPLNWF 533
Cdd:cd18596 274 VAFTslALFNMLRGPLNVL 292
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
592-838 |
2.13e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.88 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 592 LRNVSFTVPAGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAILIDGQNIKLVQQQSLRKAIgvvpqdtvlfnnTIFYNIE 671
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQL------------TGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 672 YAKL--GASDEAVYEaaraadIHERILGFPE--KYetkVGERGLRLSGGEKQRVAIARTLLKAPIIVLLDEATSALD-TH 746
Cdd:PRK13545 108 LKGLmmGLTKEKIKE------IIPEIIEFADigKF---IYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDqTF 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 747 TERNIQAALARVCANRTTIIVAHRLSTI-IHADEILVLQQGSIAERGRHEELVLREDGI---YADMWQQQLKNLDAEQ-- 820
Cdd:PRK13545 179 TKKCLDKMNEFKEQGKTIFFISHSLSQVkSFCTKALWLHYGQVKEYGDIKEVVDHYDEFlkkYNQMSVEERKDFREEQis 258
|
250 260
....*....|....*....|
gi 19527665 821 --SGGSDNGDASAESGSEKR 838
Cdd:PRK13545 259 qfQHGLLQEDQTGRERKRKK 278
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
587-781 |
2.15e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 43.36 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 587 PEKIVLRNV-SFTVPA------GKTVaIVGPSGAGKSTImrllfrfydvqtgailIDGQNIKLVQQQSLRKaIGVVPQDT 659
Cdd:cd03240 1 IDKLSIRNIrSFHERSeieffsPLTL-IVGQNGAGKTTI----------------IEALKYALTGELPPNS-KGGAHDPK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 660 VLFNNTifyNIEYAKLGASDEA--VYEAARAADIHERILGFPEKYETKVGERGL-RLSGGEKQ------RVAIARTL-LK 729
Cdd:cd03240 63 LIREGE---VRAQVKLAFENANgkKYTITRSLAILENVIFCHQGESNWPLLDMRgRCSGGEKVlasliiRLALAETFgSN 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 19527665 730 APIIVlLDEATSALDthtERNIQAALARV------CANRTTIIVAHRLSTIIHADEIL 781
Cdd:cd03240 140 CGILA-LDEPTTNLD---EENIEESLAEIieerksQKNFQLIVITHDEELVDAADHIY 193
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
588-778 |
2.20e-04 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 43.22 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 588 EKIVLRNV-SFtvpAGKTV--------AIVGPSGAGKSTImrllfrfydvqTGAIL--IDGQNIKLVQQQSL-------- 648
Cdd:cd03278 2 KKLELKGFkSF---ADKTTipfppgltAIVGPNGSGKSNI-----------IDAIRwvLGEQSAKSLRGEKMsdvifags 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 649 --RKAIGV--VpqdTVLFNNTI-FYNIeyaklgasdeavyeaARAADIhERILGFPEKyetKVGERGLrLSGGEKQRVAI 723
Cdd:cd03278 68 etRKPANFaeV---TLTFDNSDgRYSI---------------ISQGDV-SEIIEAPGK---KVQRLSL-LSGGEKALTAL 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19527665 724 ArtLL-------KAPiIVLLDEATSALDTHterNIQ--AALARVCANRT-TIIVAHRLSTIIHAD 778
Cdd:cd03278 125 A--LLfaifrvrPSP-FCVLDEVDAALDDA---NVErfARLLKEFSKETqFIVITHRKGTMEAAD 183
|
|
| ABC_6TM_NdvA_beta-glucan_exporter_like |
cd18562 |
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar ... |
335-523 |
2.70e-04 |
|
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar proteins; This group represents the six-transmembrane domain of NdvA, an ATP-dependent exporter of cyclic beta glucans, and similar proteins. NdvA is required for nodulation of legume roots and is involved in beta-(1,2)-glucan export to the periplasm. NdvA mutants in Brucella abortus and Sinorhizobium meliloti have been shown to exhibit decreased virulence in mice and inhibit intracellular multiplication in HeLa cells. These results suggest that cyclic beta-(1,2)-glucan is required to transport into the periplasmatic space to function as a virulence factor. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350006 [Multi-domain] Cd Length: 289 Bit Score: 43.77 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 335 FRHLHQLSLRWHLQRKTGEVLRVMDRGTDSINNL-LNYIVFSIAPTI-LDLLVAVAYFVyafNWWFGLIVFLTMFLYIAS 412
Cdd:cd18562 76 FEHVITLPLSFHSQRGSGRLLRIMLRGTDALFGLwLGFFREHLAALVsLIVLLPVALWM---NWRLALLLVVLAAVYAAL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 413 TIAITEwRTKY-QRRMNLADNEQRARSVDSLLNFETVKYYGAEHYEVDCYREAILKYQKEEFlSMLT----LNMLN-TAQ 486
Cdd:cd18562 153 NRLVMR-RTKAgQAAVEEHHSALSGRVGDVIGNVTVVQSYTRLAAETSALRGITRRLLAAQY-PVLNwwalASVLTrAAS 230
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 19527665 487 NIILCLGLLAGSLLcvylvVHHQTLTVGD---FVLFSTYL 523
Cdd:cd18562 231 TLTMVAIFALGAWL-----VQRGELTVGEivsFVGFATLL 265
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
601-633 |
5.03e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 42.39 E-value: 5.03e-04
10 20 30
....*....|....*....|....*....|...
gi 19527665 601 AGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAI 633
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALLPELVLATGEI 116
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
713-783 |
5.55e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.05 E-value: 5.55e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19527665 713 LSGGEKQRVAIARTLL---KAPIIVLLDEATSALDTH-TERNIQAALARVCANRTTIIVAHRLSTIIHADEILVL 783
Cdd:PRK00635 810 LSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHdIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLEL 884
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
249-521 |
7.91e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 42.44 E-value: 7.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 249 IAVIVCIIL--------LLAGRVIKLFLPIYRKKLVDSLTIapivfrwdFVLIYVALSFLQGggtgsmgLFNNLRTFLWI 320
Cdd:cd18578 13 LGLIGAIIAgavfpvfaILFSKLISVFSLPDDDELRSEANF--------WALMFLVLAIVAG-------IAYFLQGYLFG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 321 RVQQYTTREIEIELFRH-LHQlSLRWHLQRK--TGEVLRVMDRGTDSINNLLNYIVFSIAPTILDLLVAVAY-FVYafNW 396
Cdd:cd18578 78 IAGERLTRRLRKLAFRAiLRQ-DIAWFDDPEnsTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIaFVY--GW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 397 WFGLIVFLTMFLYIASTIAITEWRTKYQRRMNLADNEQRARSVDSLLNFETVKYYGAEHYEVDCYREAILKYQKEEFLSM 476
Cdd:cd18578 155 KLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRA 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 19527665 477 LTLNML----NTAQNIILCLGLLAGSLLcvylvVHHQTLTVGDF------VLFST 521
Cdd:cd18578 235 LISGLGfglsQSLTFFAYALAFWYGGRL-----VANGEYTFEQFfivfmaLIFGA 284
|
|
| ABC_6TM_McjD_like |
cd18556 |
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ... |
351-542 |
1.14e-03 |
|
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter McjD and similar proteins; This group represents the 6-TM subunit of the ABC transporter McjD that exports the antibacterial peptide microcin J25, which is an antimicrobial peptide produced by Enterobacteriaceae against other microorganisms for survival under nutrient starvation. Thus, the ABC exporter McjD provides self-immunity of the producing bacteria through export of the toxic peptide out of the cell. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.
Pssm-ID: 350000 Cd Length: 298 Bit Score: 41.86 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 351 TGEVLRVMDRGTDSINNLLNYIVFSIAPTILDLLVAVayFVYAFNwwFGLIVFLTMFLYIASTIAITEWRTK--YQRRMN 428
Cdd:cd18556 100 SGDITQRLNQASNDLYTLVRNLSTNILPPLLQLIIAI--VVILSS--GDYFVAALFLLYAVLFVINNTIFTKkiVSLRND 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 429 LADNEQRARSV--DSLLNFETVKYYGAEHYEVDCYREAILK---YQKEEFLSMLTLNMLNTAQNIILCLGLLAGSLlcvY 503
Cdd:cd18556 176 LMDAGRKSYSLltDSVKNIVAAKQNNAFDFLFKRYEATLTNdrnSQKRYWKLTFKMLILNSLLNVILFGLSFFYSL---Y 252
|
170 180 190
....*....|....*....|....*....|....*....
gi 19527665 504 LVVHhQTLTVGDFVLFSTYLMELYMPLNWFGTYYRAIQK 542
Cdd:cd18556 253 GVVN-GQVSIGHFVLITSYILLLSTPIESLGNMLSELRQ 290
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
562-622 |
1.24e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.31 E-value: 1.24e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19527665 562 DAPGCSPLLTAGGG-IEFSNVTFGYSpEKIVLRNVSFTVPAGKTVAIVGPSGAGKSTIMRLL 622
Cdd:PRK10938 246 DEPSARHALPANEPrIVLNNGVVSYN-DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI 306
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
686-803 |
1.32e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 42.03 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527665 686 ARAADIHERIlgfpeKYETKVGERGLRLSGGEKQRVAIARTLLKAPIIVLLDEATSALDTHTERNIQAALARVCANRTTI 765
Cdd:NF000106 123 ARADELLERF-----SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATV 197
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 19527665 766 IVAHRLSTIIH--ADEILVLQQGSIAERGRHEELVLREDG 803
Cdd:NF000106 198 LLTTQYMEEAEqlAHELTVIDRGRVIADGKVDELKTKVGG 237
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
602-633 |
2.46e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 41.07 E-value: 2.46e-03
10 20 30
....*....|....*....|....*....|..
gi 19527665 602 GKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAI 633
Cdd:PRK01889 195 GKTVALLGSSGVGKSTLVNALLGEEVQKTGAV 226
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
604-643 |
2.99e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 38.37 E-value: 2.99e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 19527665 604 TVAIVGPSGAGKSTIMRLLFR---------FY--DVQTGAILIDGQNIKLV 643
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGakaivsdypGTtrDPNEGRLELKGKQIILV 51
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
713-781 |
3.31e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.20 E-value: 3.31e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19527665 713 LSGGEKQRVAIArtLLKA-----PI-IVLLDEATSALDthtERNIQ--AALARVCANRTT-IIVAHRLSTIIHADEIL 781
Cdd:TIGR02168 1090 LSGGEKALTALA--LLFAifkvkPApFCILDEVDAPLD---DANVErfANLLKEFSKNTQfIVITHNKGTMEVADQLY 1162
|
|
| Cmk |
COG0283 |
Cytidylate kinase [Nucleotide transport and metabolism]; |
604-633 |
3.54e-03 |
|
Cytidylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 440052 [Multi-domain] Cd Length: 220 Bit Score: 39.62 E-value: 3.54e-03
10 20 30
....*....|....*....|....*....|....*
gi 19527665 604 TVAIVGPSGAGKSTIMRLL-----FRFYDvqTGAI 633
Cdd:COG0283 2 VIAIDGPAGSGKSTVAKALakrlgYHYLD--TGAM 34
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
605-633 |
6.48e-03 |
|
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.
Pssm-ID: 238978 [Multi-domain] Cd Length: 147 Bit Score: 37.85 E-value: 6.48e-03
10 20 30
....*....|....*....|....*....|....
gi 19527665 605 VAIVGPSGAGKSTIMRLL-----FRFYDvqTGAI 633
Cdd:cd02020 2 IAIDGPAGSGKSTVAKLLakklgLPYLD--TGGI 33
|
|
| PhnN |
COG3709 |
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism]; |
602-622 |
7.01e-03 |
|
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
Pssm-ID: 442923 Cd Length: 188 Bit Score: 38.64 E-value: 7.01e-03
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
592-623 |
7.65e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.06 E-value: 7.65e-03
10 20 30
....*....|....*....|....*....|...
gi 19527665 592 LRNVSFTVPAGKTVAIVGPSGAGKST-IMRLLF 623
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTlINETLY 657
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
601-633 |
8.90e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 37.91 E-value: 8.90e-03
10 20 30
....*....|....*....|....*....|...
gi 19527665 601 AGKTVAIVGPSGAGKSTIMRLLFRFYDVQTGAI 633
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNALLPELDLRTGEI 137
|
|
| |
