|
Name |
Accession |
Description |
Interval |
E-value |
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
154-750 |
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: 835.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 154 KEQRMVDWAIIRKLVQYVWPKGDFGTKQRVALALALLVGGKLLNVQVPFFFKAIVDRLNQVvnapldmtnPNTVWVVAGS 233
Cdd:COG5265 9 APAAPPRLDLLLRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSG---------AAALLVVPVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 234 AILGYGLARVGAAAFSELRNAVFANVAQQSIRRVARSVFTHLLALDLGWHLTRQTGGLTRAIDRGTKGISFLLTSIVFHI 313
Cdd:COG5265 80 LLLAYGLLRLLSVLFGELRDALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGGLSRDIERGTKGIEFLLRFLLFNI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 314 VPTALEISMVCGILSYKCGPSFAAVTAVTMAAYAWFTIRTTSWRTRFRKEANAADNRAATTSVDSLLNYEAVKYFNNEKH 393
Cdd:COG5265 160 LPTLLEIALVAGILLVKYDWWFALITLVTVVLYIAFTVVVTEWRTKFRREMNEADSEANTRAVDSLLNYETVKYFGNEAR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 394 EIAKYDAALADYEKSSIKVATSLAALNSGQNAIFSTSLTVMMLLAAQGVTNGTMSVGDLVMVNQLVFQLSLPLNFLGTVY 473
Cdd:COG5265 240 EARRYDEALARYERAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 474 RELRQSLVDMETMFNLENVNVAVKENADAPPLKVTGGEIRFENVTFGYHPDRPIFSNISFAVPAGYKTAFVGPSGCGKST 553
Cdd:COG5265 320 REIRQALADMERMFDLLDQPPEVADAPDAPPLVVGGGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKST 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 554 IFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGVVPQDTPLFNDDIRHNIRYGRLDASDADVEAAARAAKVDQIVQN 633
Cdd:COG5265 400 LARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIES 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 634 LPQGYNTKVGERGLMISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTEtelmRNINANL--LSEKRTAIFVAHRLRT 711
Cdd:COG5265 480 LPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTE----RAIQAALreVARGRTTLVIAHRLST 555
|
570 580 590
....*....|....*....|....*....|....*....
gi 2274528008 712 ISDSDLIVVLQSGQVAEKGTHAELMDRKGLYWDLWQAQS 750
Cdd:COG5265 556 IVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQ 594
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
160-750 |
7.11e-171 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 504.31 E-value: 7.11e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 160 DWAIIRKLVQYVWPKgdfgtKQRVALALALLVGGKLLNVQVPFFFKAIVDRLnqvvnapLDMTNPNTVWVVAgsaiLGYG 239
Cdd:COG1132 5 PRKLLRRLLRYLRPY-----RGLLILALLLLLLSALLELLLPLLLGRIIDAL-------LAGGDLSALLLLL----LLLL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 240 LARVGAAAFSELRNAVFANVAQQSIRRVARSVFTHLLALDLGWHLTRQTGGLTRAIDRGTKGISFLLTSIVFHIVPTALE 319
Cdd:COG1132 69 GLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 320 ISMVCGILSYKcGPSFAAVTAVTMAAYAWFTIRTTSWRTRFRKEANAADNRAATTSVDSLLNYEAVKYFNNEKHEIAKYD 399
Cdd:COG1132 149 LIGALVVLFVI-DWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 400 AALADYEKSSIKVATSLAALNSGQNAIFSTSLTVMMLLAAQGVTNGTMSVGDLVMVNQLVFQLSLPLNFLGTVYRELRQS 479
Cdd:COG1132 228 EANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 480 LVDMETMFNLENVNVAVKENADAPPLKVTGGEIRFENVTFGYHPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLF 559
Cdd:COG1132 308 LASAERIFELLDEPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 560 RFYKPQSGKIYIDGQDITKVSLESLRRHIGVVPQDTPLFNDDIRHNIRYGRLDASDADVEAAARAAKVDQIVQNLPQGYN 639
Cdd:COG1132 388 RFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYD 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 640 TKVGERGLMISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNINAnlLSEKRTAIFVAHRLRTISDSDLIV 719
Cdd:COG1132 468 TVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALER--LMKGRTTIVIAHRLSTIRNADRIL 545
|
570 580 590
....*....|....*....|....*....|.
gi 2274528008 720 VLQSGQVAEKGTHAELMDRKGLYWDLWQAQS 750
Cdd:COG1132 546 VLDDGRIVEQGTHEELLARGGLYARLYRLQF 576
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
186-486 |
1.77e-158 |
|
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: 461.58 E-value: 1.77e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 186 ALALLVGGKLLNVQVPFFFKAIVDRLNqvvnapldmTNPNTVWVVAGSAILGYGLARVGAAAFSELRNAVFANVAQQSIR 265
Cdd:cd18582 1 ALLLLVLAKLLNVAVPFLLKYAVDALS---------APASALLAVPLLLLLAYGLARILSSLFNELRDALFARVSQRAVR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 266 RVARSVFTHLLALDLGWHLTRQTGGLTRAIDRGTKGISFLLTSIVFHIVPTALEISMVCGILSYKCGPSFAAVTAVTMAA 345
Cdd:cd18582 72 RLALRVFRHLHSLSLRFHLSRKTGALSRAIERGTRGIEFLLRFLLFNILPTILELLLVCGILWYLYGWSYALITLVTVAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 346 YAWFTIRTTSWRTRFRKEANAADNRAATTSVDSLLNYEAVKYFNNEKHEIAKYDAALADYEKSSIKVATSLAALNSGQNA 425
Cdd:cd18582 152 YVAFTIKVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQAL 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2274528008 426 IFSTSLTVMMLLAAQGVTNGTMSVGDLVMVNQLVFQLSLPLNFLGTVYRELRQSLVDMETM 486
Cdd:cd18582 232 IISLGLTAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFLGFVYREIRQSLIDMEKL 292
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
512-749 |
2.45e-145 |
|
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: 425.49 E-value: 2.45e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGVV 591
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 592 PQDTPLFNDDIRHNIRYGRLDASDADVEAAARAAKVDQIVQNLPQGYNTKVGERGLMISGGEKQRLAVARLLLKNPSILF 671
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2274528008 672 FDEATSALDSYTETELMRNINAnlLSEKRTAIFVAHRLRTISDSDLIVVLQSGQVAEKGTHAELMDRKGLYWDLWQAQ 749
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRD--VSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
164-749 |
1.75e-141 |
|
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: 433.11 E-value: 1.75e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 164 IRKLVQYVWP-KGDFGTkqrvALALALLVGgkLLNVQVPFFFKAIVDRLnqVVNApldmtNPNTVWVVAgsaiLGYGLAR 242
Cdd:COG2274 144 LRWFLRLLRRyRRLLLQ----VLLASLLIN--LLALATPLFTQVVIDRV--LPNQ-----DLSTLWVLA----IGLLLAL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 243 VGAAAFSELRNAVFANVAQQSIRRVARSVFTHLLALDLGWHLTRQTGGLT---RAIDRGTKGISFLLTSIVFHIvPTALe 319
Cdd:COG2274 207 LFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLAsrfRDVESIREFLTGSLLTALLDL-LFVL- 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 320 ISMVCgILSYkcGPSFAAVTAVTMAAYAWFTIRTTSWRTRFRKEANAADNRAATTSVDSLLNYEAVKYFNNEKHEIAKYD 399
Cdd:COG2274 285 IFLIV-LFFY--SPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 400 AALADYEKSSIKVATSLAALNSGQNAIFSTSLTVMMLLAAQGVTNGTMSVGDLVMVNQLVFQLSLPLNFLGTVYRELRQS 479
Cdd:COG2274 362 NLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDA 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 480 LVDMETMFNLENVNVAVKENADAPPLKVTGGEIRFENVTFGYHPD-RPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLL 558
Cdd:COG2274 442 KIALERLDDILDLPPEREEGRSKLSLPRLKGDIELENVSFRYPGDsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLL 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 559 FRFYKPQSGKIYIDGQDITKVSLESLRRHIGVVPQDTPLFNDDIRHNIRYGRLDASDADVEAAARAAKVDQIVQNLPQGY 638
Cdd:COG2274 522 LGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGY 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 639 NTKVGERGLMISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNINAnlLSEKRTAIFVAHRLRTISDSDLI 718
Cdd:COG2274 602 DTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRR--LLKGRTVIIIAHRLSTIRLADRI 679
|
570 580 590
....*....|....*....|....*....|.
gi 2274528008 719 VVLQSGQVAEKGTHAELMDRKGLYWDLWQAQ 749
Cdd:COG2274 680 IVLDKGRIVEDGTHEELLARKGLYAELVQQQ 710
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
186-486 |
6.21e-103 |
|
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: 318.40 E-value: 6.21e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 186 ALALLVGGKLLNVQVPFFFKAIVDRLNQVVNAPLdmtnPNTVWvvagsAILGYGLARVGAAAFSELRNAVFANVAQQSIR 265
Cdd:cd18560 1 SLLLLILGKACNVLAPLFLGRAVNALTLAKVKDL----ESAVT-----LILLYALLRFSSKLLKELRSLLYRRVQQNAYR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 266 RVARSVFTHLLALDLGWHLTRQTGGLTRAIDRGTKGISFLLTSIVFHIVPTALEISMVCGILSYKCGPSFAAVTAVTMAA 345
Cdd:cd18560 72 ELSLKTFAHLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLELIVVSVVFAFHFGAWLALIVFLSVLL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 346 YAWFTIRTTSWRTRFRKEANAADNRAATTSVDSLLNYEAVKYFNNEKHEIAKYDAALADYEKSSIKVATSLAALNSGQNA 425
Cdd:cd18560 152 YGVFTIKVTEWRTKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQL 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2274528008 426 IFSTSLTVMMLLAAQGVTNGTMSVGDLVMVNQLVFQLSLPLNFLGTVYRELRQSLVDMETM 486
Cdd:cd18560 232 IIQLGLTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSLTDMENL 292
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
512-746 |
1.13e-99 |
|
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: 307.62 E-value: 1.13e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPD-RPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGV 590
Cdd:cd03251 1 VEFKNVTFRYPGDgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 591 VPQDTPLFNDDIRHNIRYGRLDASDADVEAAARAAKVDQIVQNLPQGYNTKVGERGLMISGGEKQRLAVARLLLKNPSIL 670
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2274528008 671 FFDEATSALDSYTETELMRNINAnlLSEKRTAIFVAHRLRTISDSDLIVVLQSGQVAEKGTHAELMDRKGLYWDLW 746
Cdd:cd03251 161 ILDEATSALDTESERLVQAALER--LMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
512-749 |
1.64e-98 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 304.85 E-value: 1.64e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGY--HPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIG 589
Cdd:cd03249 1 IEFKNVSFRYpsRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 590 VVPQDTPLFNDDIRHNIRYGRLDASDADVEAAARAAKVDQIVQNLPQGYNTKVGERGLMISGGEKQRLAVARLLLKNPSI 669
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 670 LFFDEATSALDSYTETELMRNINAnlLSEKRTAIFVAHRLRTISDSDLIVVLQSGQVAEKGTHAELMDRKGLYWDLWQAQ 749
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDR--AMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
510-740 |
4.28e-96 |
|
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: 298.37 E-value: 4.28e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 510 GEIRFENVTFGYHPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIG 589
Cdd:cd03254 1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 590 VVPQDTPLFNDDIRHNIRYGRLDASDADVEAAARAAKVDQIVQNLPQGYNTKVGERGLMISGGEKQRLAVARLLLKNPSI 669
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2274528008 670 LFFDEATSALDSYTETELMRNINAnlLSEKRTAIFVAHRLRTISDSDLIVVLQSGQVAEKGTHAELMDRKG 740
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEK--LMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
201-749 |
9.87e-96 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 309.97 E-value: 9.87e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 201 PFFFKAIVDRLNqvvnAPLDMTNPNTVWVvagsailGYGLARVGAAAFselrnavfanVAQQSIRRVAR-------SVFT 273
Cdd:PRK13657 39 PILFGRIIDAIS----GKGDIFPLLAAWA-------GFGLFNIIAGVL----------VARHADRLAHRrrlavltEYFE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 274 HLLALDLGWHLTRQTGGLTRAIDRGTKGISFL--------LTSIV--FHIVPTALEISMVCGILSYKCGpsfaavtavtm 343
Cdd:PRK13657 98 RIIQLPLAWHSQRGSGRALHTLLRGTDALFGLwlefmrehLATLValVVLLPLALFMNWRLSLVLVVLG----------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 344 aayAWFTIrTTSWRTRFRKEANAA-----DNRAATTSvDSLLNYEAVKYFNNEKHEIAkydaALADYEKSSIKVAT---S 415
Cdd:PRK13657 167 ---IVYTL-ITTLVMRKTKDGQAAveehyHDLFAHVS-DAIGNVSVVQSYNRIEAETQ----ALRDIADNLLAAQMpvlS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 416 LAALNSGQNAIFST-SLTVMMLLAAQGVTNGTMSVGDLVM----VNQLVFQLSLPLNFLGTVYrelrQSLVDMETMFNLE 490
Cdd:PRK13657 238 WWALASVLNRAASTiTMLAILVLGAALVQKGQLRVGEVVAfvgfATLLIGRLDQVVAFINQVF----MAAPKLEEFFEVE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 491 NVNVAVKENADAPPLKVTGGEIRFENVTFGYHPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIY 570
Cdd:PRK13657 314 DAVPDVRDPPGAIDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRIL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 571 IDGQDITKVSLESLRRHIGVVPQDTPLFNDDIRHNIRYGRLDASDADVEAAARAAKVDQIVQNLPQGYNTKVGERGLMIS 650
Cdd:PRK13657 394 IDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLS 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 651 GGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNINAnlLSEKRTAIFVAHRLRTISDSDLIVVLQSGQVAEKG 730
Cdd:PRK13657 474 GGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDE--LMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESG 551
|
570
....*....|....*....
gi 2274528008 731 THAELMDRKGLYWDLWQAQ 749
Cdd:PRK13657 552 SFDELVARGGRFAALLRAQ 570
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
386-740 |
7.02e-92 |
|
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: 298.98 E-value: 7.02e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 386 KYFNNEKHEIAKYDAALADYEKSSIKV---A-TSLAALNsgqnaIFST-SLTVMMLLAAQGVTNGTMSVGDLVMVNQLVF 460
Cdd:COG4988 211 KLFGRAKAEAERIAEASEDFRKRTMKVlrvAfLSSAVLE-----FFASlSIALVAVYIGFRLLGGSLTLFAALFVLLLAP 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 461 QLSLPLNFLGTVYRELRQSLVDMETMFNLENVNVAVKENADAPPLKVTGGEIRFENVTFGYHPDRPIFSNISFAVPAGYK 540
Cdd:COG4988 286 EFFLPLRDLGSFYHARANGIAAAEKIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGER 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 541 TAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGVVPQDTPLFNDDIRHNIRYGRLDASDADVEA 620
Cdd:COG4988 366 VALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 621 AARAAKVDQIVQNLPQGYNTKVGERGLMISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNINAnlLSEKR 700
Cdd:COG4988 446 ALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRR--LAKGR 523
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2274528008 701 TAIFVAHRLRTISDSDLIVVLQSGQVAEKGTHAELMDRKG 740
Cdd:COG4988 524 TVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
355-747 |
1.26e-91 |
|
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: 298.22 E-value: 1.26e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 355 SWRTRFRKEANAADNRAA--TTSVDSLLNYEAVKYFNNEKHEIAKYDAALADYEKSSIKVATSLAALNSGQNAIFSTSLT 432
Cdd:COG4987 176 AARLGRRAGRRLAAARAAlrARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVV 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 433 VMMLLAAQGVTNGTMSVGDLVMvnqLVFqLSLPLnF-----LGTVYRELRQSLVDMETMFNLENVNVAVKENADAPPLkV 507
Cdd:COG4987 256 AVLWLAAPLVAAGALSGPLLAL---LVL-AALAL-FealapLPAAAQHLGRVRAAARRLNELLDAPPAVTEPAEPAPA-P 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 508 TGGEIRFENVTFGYHP-DRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRR 586
Cdd:COG4987 330 GGPSLELEDVSFRYPGaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRR 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 587 HIGVVPQDTPLFNDDIRHNIRYGRLDASDADVEAAARAAKVDQIVQNLPQGYNTKVGERGLMISGGEKQRLAVARLLLKN 666
Cdd:COG4987 410 RIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRD 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 667 PSILFFDEATSALDSYTETELMRNINAnlLSEKRTAIFVAHRLRTISDSDLIVVLQSGQVAEKGTHAELMDRKGLYWDLW 746
Cdd:COG4987 490 APILLLDEPTEGLDAATEQALLADLLE--ALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLY 567
|
.
gi 2274528008 747 Q 747
Cdd:COG4987 568 Q 568
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
162-749 |
6.07e-91 |
|
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: 297.00 E-value: 6.07e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 162 AIIRKLVQYVWPKgdfgtKQRVALALALLVGGKLLNVQVPFFFKAIVDrlNQVVNAPLDMTNPNTVWVVAGSAILGYGLA 241
Cdd:TIGR02204 4 RPLAALWPFVRPY-----RGRVLAALVALLITAAATLSLPYAVRLMID--HGFSKDSSGLLNRYFAFLLVVALVLALGTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 242 rvgaaafseLRNAVFANVAQQSIRRVARSVFTHLLALDLGWHLTRQTGGLtraIDRGTKGiSFLLTSIVFHIVPTALEIS 321
Cdd:TIGR02204 77 ---------ARFYLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEV---VSRLTTD-TTLLQSVIGSSLSMALRNA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 322 MVC-------GILSYKCGpSFAAVTAVTMAAYAWFTIRttswrtRFRKEANAADNRAATTSV---DSLLNYEAVKYFNNE 391
Cdd:TIGR02204 144 LMCigglimmFITSPKLT-SLVLLAVPLVLLPILLFGR------RVRKLSRESQDRIADAGSyagETLGAIRTVQAFGHE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 392 KHEIAKYDAALADYEKSSIKVATSLAALNSGQNAIFSTSLTVMMLLAAQGVTNGTMSVGDLvmvNQLVFQLSLPLNFLGT 471
Cdd:TIGR02204 217 DAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTL---GQFVFYAVMVAGSIGT 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 472 ---VYRELRQSLVDMETMFNLENVNVAVKENAD--APPLKVTGgEIRFENVTFGY--HPDRPIFSNISFAVPAGYKTAFV 544
Cdd:TIGR02204 294 lseVWGELQRAAGAAERLIELLQAEPDIKAPAHpkTLPVPLRG-EIEFEQVNFAYpaRPDQPALDGLNLTVRPGETVALV 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 545 GPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGVVPQDTPLFNDDIRHNIRYGRLDASDADVEAAARA 624
Cdd:TIGR02204 373 GPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARA 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 625 AKVDQIVQNLPQGYNTKVGERGLMISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNINAnlLSEKRTAIF 704
Cdd:TIGR02204 453 AHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALET--LMKGRTTLI 530
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 2274528008 705 VAHRLRTISDSDLIVVLQSGQVAEKGTHAELMDRKGLYWDLWQAQ 749
Cdd:TIGR02204 531 IAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
357-749 |
1.16e-86 |
|
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: 285.46 E-value: 1.16e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 357 RTRFR---KEANAADNRAATTSVDSLLNYEAVKYFNNEKHEIAKYDAALADYEKSSIKVATSLAALNSGQNAIFSTSLTV 433
Cdd:TIGR02203 175 SKRLRrisKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQLIASLALAV 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 434 MMLLAAQGVTNGTMSVGDLVMVNQLVFQLSLPLNFLGTVYRELRQSLVDMETMFNLenvnvavkenADAPPLKVTG---- 509
Cdd:TIGR02203 255 VLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTL----------LDSPPEKDTGtrai 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 510 ----GEIRFENVTFGYHP-DRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESL 584
Cdd:TIGR02203 325 erarGDVEFRNVTFRYPGrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 585 RRHIGVVPQDTPLFNDDIRHNIRYGRL-DASDADVEAAARAAKVDQIVQNLPQGYNTKVGERGLMISGGEKQRLAVARLL 663
Cdd:TIGR02203 405 RRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARAL 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 664 LKNPSILFFDEATSALDsyTETElmRNINANL--LSEKRTAIFVAHRLRTISDSDLIVVLQSGQVAEKGTHAELMDRKGL 741
Cdd:TIGR02203 485 LKDAPILILDEATSALD--NESE--RLVQAALerLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGL 560
|
....*...
gi 2274528008 742 YWDLWQAQ 749
Cdd:TIGR02203 561 YAQLHNMQ 568
|
|
| ABC_6TM_ABCB6 |
cd18581 |
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, ... |
187-486 |
5.72e-80 |
|
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, mitochondrial; This group represents the ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, ABCB6 (ABC transporter subfamily B, member 6) is closely related to yeast ATM1 and human ABCB7, which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350025 [Multi-domain] Cd Length: 300 Bit Score: 258.72 E-value: 5.72e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 187 LALLVGGKLLNVQVPFFFKAIVDRLNQvvnapldmTNPNTVWVVAGSAILGYGLAR------VGAAAF-SELRNAVFANV 259
Cdd:cd18581 2 LLLLAAGRVVNVLVPILYKKIVDSLTP--------DSADSPLAFPWALILLYVFLKflqgggSGSVGLlSNLRSFLWIPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 260 AQQSIRRVARSVFTHLLALDLGWHLTRQTGGLTRAIDRGTKGISFLLTSIVFHIVPTALEISMVCGILSYKCGPSFAAVT 339
Cdd:cd18581 74 QQFTTREISVKLFAHLHSLSLRWHLSRKTGEVLRVMDRGTSSINSLLSYVLFNIGPTIADIIIAIIYFAIAFNPWFGLIV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 340 AVTMAAYAWFTIRTTSWRTRFRKEANAADNRAATTSVDSLLNYEAVKYFNNEKHEIAKYDAALADYEKSSIKVATSLAAL 419
Cdd:cd18581 154 FVTMALYLILTIIITEWRTKFRREMNKLDNEKRAKAVDSLLNFETVKYYNAERFEVERYRRAIDDYQVAEWKSNASLNLL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2274528008 420 NSGQNAIFSTSLTVMMLLAAQGVTNGTMSVGDLVMVNQLVFQLSLPLNFLGTVYRELRQSLVDMETM 486
Cdd:cd18581 234 NTAQNLIITIGLLAGSLLCAYFVVEGKLTVGDFVLFLTYIIQLYAPLNFFGTYYRMIQQSFIDMENM 300
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
512-725 |
1.58e-76 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 244.60 E-value: 1.58e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHP-DRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGV 590
Cdd:cd03228 1 IEFKNVSFSYPGrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 591 VPQDTPLFNDDIRHNIrygrldasdadveaaaraakvdqivqnlpqgyntkvgerglmISGGEKQRLAVARLLLKNPSIL 670
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2274528008 671 FFDEATSALDSYTETELMRNINAnlLSEKRTAIFVAHRLRTISDSDLIVVLQSGQ 725
Cdd:cd03228 119 ILDEATSALDPETEALILEALRA--LAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
148-745 |
1.65e-76 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 261.58 E-value: 1.65e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 148 AREKSL-KEQRMVDWAIIRkLVQYVWPKgdfgtKQRVALALALLVGGKLLNVQVPFFFKAIVDRLNQVVNAPlDMTNPnt 226
Cdd:TIGR00958 133 ASEKEAeQGQSETADLLFR-LLGLSGRD-----WPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPP-ALASA-- 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 227 VWVVagsailgyGLARVGAAAFSELRNAVFANVAQQSIRRVARSVFTHLLALDLGWHLTRQTGGLTRAIDRGTKGISFLL 306
Cdd:TIGR00958 204 IFFM--------CLLSIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 307 TSIVfhivpTALEISMVCGILSY----KCGPS-------FAAVTAVTMAAYAWFtIRTTSWRTRfrkEANAADNRAATTS 375
Cdd:TIGR00958 276 SLNV-----NVLLRNLVMLLGLLgfmlWLSPRltmvtliNLPLVFLAEKVFGKR-YQLLSEELQ---EAVAKANQVAEEA 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 376 VDSLlnyEAVKYFNNEKHEIAKYDAALAD----YEKSSIKVATSLAALNSGQNAIFstslTVMMLLAAQGVTNGTMSVGD 451
Cdd:TIGR00958 347 LSGM---RTVRSFAAEEGEASRFKEALEEtlqlNKRKALAYAGYLWTTSVLGMLIQ----VLVLYYGGQLVLTGKVSSGN 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 452 LV--MVNQlvFQLSLPLNFLGTVYRELRQSLVDMETMFNLENVNVAVKENADAPPLKVTGgEIRFENVTFGY--HPDRPI 527
Cdd:TIGR00958 420 LVsfLLYQ--EQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLNLEG-LIEFQDVSFSYpnRPDVPV 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 528 FSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGVVPQDTPLFNDDIRHNIR 607
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIA 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 608 YGRLDASDADVEAAARAAKVDQIVQNLPQGYNTKVGERGLMISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETEL 687
Cdd:TIGR00958 577 YGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLL 656
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 2274528008 688 MRNINanllSEKRTAIFVAHRLRTISDSDLIVVLQSGQVAEKGTHAELMDRKGLYWDL 745
Cdd:TIGR00958 657 QESRS----RASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
349-749 |
3.44e-74 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 252.25 E-value: 3.44e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 349 FTIRTTSwrTRFRKEANAADNRAA--TTSVDSLLN-YEAVKYFNNEKHEIAKYDAALADYEKSSIKVATSLAALNSGQNA 425
Cdd:PRK11176 180 IAIRVVS--KRFRNISKNMQNTMGqvTTSAEQMLKgHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASSISDPIIQL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 426 IFSTSLTVMMLLAAQGVTNGTMSVGDLVMVNQLVFQLSLPLNFLGTVYRELRQSLVDMETMFNLenvnVAVKENADAPPL 505
Cdd:PRK11176 258 IASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAI----LDLEQEKDEGKR 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 506 KVT--GGEIRFENVTFGYH-PDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLE 582
Cdd:PRK11176 334 VIEraKGDIEFRNVTFTYPgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLA 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 583 SLRRHIGVVPQDTPLFNDDIRHNIRYGRLDA-SDADVEAAARAAKVDQIVQNLPQGYNTKVGERGLMISGGEKQRLAVAR 661
Cdd:PRK11176 414 SLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIAR 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 662 LLLKNPSILFFDEATSALDsyTETElmRNINANL--LSEKRTAIFVAHRLRTISDSDLIVVLQSGQVAEKGTHAELMDRK 739
Cdd:PRK11176 494 ALLRDSPILILDEATSALD--TESE--RAIQAALdeLQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQN 569
|
410
....*....|
gi 2274528008 740 GLYWDLWQAQ 749
Cdd:PRK11176 570 GVYAQLHKMQ 579
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
512-749 |
1.25e-72 |
|
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: 236.61 E-value: 1.25e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPDRP-IFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGV 590
Cdd:cd03252 1 ITFEHVRFRYKPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 591 VPQDTPLFNDDIRHNIRYGRLDASDADVEAAARAAKVDQIVQNLPQGYNTKVGERGLMISGGEKQRLAVARLLLKNPSIL 670
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2274528008 671 FFDEATSALDSYTETELMRNINAnlLSEKRTAIFVAHRLRTISDSDLIVVLQSGQVAEKGTHAELMDRKGLYWDLWQAQ 749
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHD--ICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
272-752 |
5.06e-71 |
|
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: 243.64 E-value: 5.06e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 272 FTHLLALDLGWHLTRQTGGLTRAIDRGTKGISFL--------LTSIV--FHIVPTALEISMVCGILSYKCGPSFaavtav 341
Cdd:TIGR01192 96 FGRIISMPLSWHQQRGTSNALHTLLRATETLFGLwlefmrqhLATFValFLLIPTAFAMDWRLSIVLMVLGILY------ 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 342 tmaayaWFTIRTTSWRTRFRKEANAADNRAATTSV-DSLLNYEAVKYFNnekhEIAKYDAALADYEKSSIKVATSLA--- 417
Cdd:TIGR01192 170 ------ILIAKLVMQRTKNGQAAVEHHYHNVFKHVsDSISNVSVVHSYN----RIEAETSALKQFTNNLLSAQYPVLdww 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 418 ALNSGQNAIFST-SLTVMMLLAAQGVTNGTMSVGDLV----MVNQLVFQLSLPLNFLGTVYrelrQSLVDMETMFNLENV 492
Cdd:TIGR01192 240 ALASGLNRMASTiSMMCILVIGTVLVIKGELSVGEVIafigFANLLIGRLDQMSGFITQIF----EARAKLEDFFDLEDS 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 493 NVAVKENADAPPLKVTGGEIRFENVTFGYHPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYID 572
Cdd:TIGR01192 316 VFQREEPADAPELPNVKGAVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILID 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 573 GQDITKVSLESLRRHIGVVPQDTPLFNDDIRHNIRYGRLDASDADVEAAARAAKVDQIVQNLPQGYNTKVGERGLMISGG 652
Cdd:TIGR01192 396 GIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGG 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 653 EKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNINAnlLSEKRTAIFVAHRLRTISDSDLIVVLQSGQVAEKGTH 732
Cdd:TIGR01192 476 ERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDA--LRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSF 553
|
490 500
....*....|....*....|
gi 2274528008 733 AELMDRKGLYWDLWQAQSTL 752
Cdd:TIGR01192 554 QELIQKDGRFYKLLRRSGLL 573
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
418-745 |
1.76e-67 |
|
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: 236.76 E-value: 1.76e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 418 ALNSGQ-----NAIFS------TSLTVMMLLAAQG--VTNGTMSVGDLVMVNQLVFQLSLPLNFL---GTVYRELRQSLV 481
Cdd:TIGR03796 365 LLNAQQelgvlTQILGvlptllTSLNSALILVVGGlrVMEGQLTIGMLVAFQSLMSSFLEPVNNLvgfGGTLQELEGDLN 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 482 DMETMFNLENVNVAVKENADA----PPLKVTGgEIRFENVTFGYHP-DRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFR 556
Cdd:TIGR03796 445 RLDDVLRNPVDPLLEEPEGSAatsePPRRLSG-YVELRNITFGYSPlEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAK 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 557 LLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGVVPQDTPLFNDDIRHNIRYGRLDASDADVEAAARAAKVDQIVQNLPQ 636
Cdd:TIGR03796 524 LVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPG 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 637 GYNTKVGERGLMISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNInanllsEKR--TAIFVAHRLRTISD 714
Cdd:TIGR03796 604 GYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL------RRRgcTCIIVAHRLSTIRD 677
|
330 340 350
....*....|....*....|....*....|.
gi 2274528008 715 SDLIVVLQSGQVAEKGTHAELMDRKGLYWDL 745
Cdd:TIGR03796 678 CDEIIVLERGKVVQRGTHEELWAVGGAYARL 708
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
510-731 |
1.87e-62 |
|
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: 208.89 E-value: 1.87e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 510 GEIRFENVTFGYHPD-RPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHI 588
Cdd:cd03244 1 GDIEFKNVSLRYRPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 589 GVVPQDTPLFNDDIRHNirygrLD----ASDADVEAAARAAKVDQIVQNLPQGYNTKVGERGLMISGGEKQRLAVARLLL 664
Cdd:cd03244 81 SIIPQDPVLFSGTIRSN-----LDpfgeYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2274528008 665 KNPSILFFDEATSALDSYTETELMRNINANLlsEKRTAIFVAHRLRTISDSDLIVVLQSGQVAEKGT 731
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIREAF--KDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
195-745 |
4.02e-62 |
|
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: 221.92 E-value: 4.02e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 195 LLNVQVPFFFKAIVDrlnqvVNAPLDMTNpnTVWVVAGSAILGYGLARVgaaaFSELRNAVFANVAQQSIRRVARSVFTH 274
Cdd:TIGR01193 170 LISIAGSYYLQKIID-----TYIPHKMMG--TLGIISIGLIIAYIIQQI----LSYIQIFLLNVLGQRLSIDIILSYIKH 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 275 LLALDLGWHLTRQTGGLTRAIDRGTKGISFLLTSI--VFHIVPTALEISMVCGILSYKcgpsFAAVTAVTMAAYA---WF 349
Cdd:TIGR01193 239 LFELPMSFFSTRRTGEIVSRFTDASSIIDALASTIlsLFLDMWILVIVGLFLVRQNML----LFLLSLLSIPVYAviiIL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 350 TIRTTSWRTRFRKEANAADNRAAttsVDSLLNYEAVKYFNNEKHEIAKYDAALADYEKSSIKVATSlaalNSGQNAIFST 429
Cdd:TIGR01193 315 FKRTFNKLNHDAMQANAVLNSSI---IEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKA----DQGQQAIKAV 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 430 ---SLTVMMLLA-AQGVTNGTMSVGDLVMVNQLVFQLSLPLNFLGTVYRELRQSLVDMETMFNLENVNVAVKENADAPPL 505
Cdd:TIGR01193 388 tklILNVVILWTgAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTEL 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 506 KVTGGEIRFENVTFGYHPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLR 585
Cdd:TIGR01193 468 NNLNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLR 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 586 RHIGVVPQDTPLFNDDIRHNIRYG-RLDASDADVEAAARAAKVDQIVQNLPQGYNTKVGERGLMISGGEKQRLAVARLLL 664
Cdd:TIGR01193 548 QFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALL 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 665 KNPSILFFDEATSALDSYTEtelmRNINANLLS-EKRTAIFVAHRLRTISDSDLIVVLQSGQVAEKGTHAELMDRKGLYW 743
Cdd:TIGR01193 628 TDSKVLILDESTSNLDTITE----KKIVNNLLNlQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYA 703
|
..
gi 2274528008 744 DL 745
Cdd:TIGR01193 704 SL 705
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
187-486 |
3.12e-61 |
|
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: 208.15 E-value: 3.12e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 187 LALLVGGKLLNVQVPFFFKAIVDRLNQVVNapldmTNPntvWVvagsAILGYGLARV--GAAAFSELRNAVFANVAQQSI 264
Cdd:cd18583 2 FLCLLAERVLNVLVPRQLGIIVDSLSGGSG-----KSP---WK----EIGLYVLLRFlqSGGGLGLLRSWLWIPVEQYSY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 265 RRVARSVFTHLLALDLGWHLTRQTGGLTRAIDRGTkGISFLLTSIVFHIVPTALEISMVCGILSYKCGPSFAAVTAVTMA 344
Cdd:cd18583 70 RALSTAAFNHVMNLSMDFHDSKKSGEVLKAIEQGS-SINDLLEQILFQIVPMIIDLVIAIVYLYYLFDPYMGLIVAVVMV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 345 AYAWFTIRTTSWRTRFRKEANAADNRAATTSVDSLLNYEAVKYFNNEKHEIAKYDAALADYEKSSIKVATSLAALNSGQN 424
Cdd:cd18583 149 LYVWSTIKLTSWRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYREAVKNYQKAERKYLFSLNLLNAVQS 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2274528008 425 AIFSTSLTVMMLLAAQGVTNGTMSVGDLVMVNQLVFQLSLPLNFLGTVYRELRQSLVDMETM 486
Cdd:cd18583 229 LILTLGLLAGCFLAAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDLIDAERL 290
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
510-726 |
9.43e-61 |
|
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: 204.36 E-value: 9.43e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 510 GEIRFENVTFGYHPD-RPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHI 588
Cdd:cd03245 1 GRIEFRNVSFSYPNQeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 589 GVVPQDTPLFNDDIRHNIRYGRLDASDADVEAAARAAKVDQIVQNLPQGYNTKVGERGLMISGGEKQRLAVARLLLKNPS 668
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2274528008 669 ILFFDEATSALDSYTETELMRNINAnLLSEKrTAIFVAHRLRTISDSDLIVVLQSGQV 726
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQ-LLGDK-TLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
434-749 |
8.97e-60 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 213.04 E-value: 8.97e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 434 MMLLAAQGVtnGTMSVGDLVMVNQLVFQLSLPLNFLGTVYRELRQSLVDMETMFNLENVNVAVKENADAPplkVTGGEIR 513
Cdd:PRK10790 268 LMLFGFSAS--GTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELMDGPRQQYGNDDRP---LQSGRID 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 514 FENVTFGYHPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGVVPQ 593
Cdd:PRK10790 343 IDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQ 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 594 DTPLFNDDIRHNIRYGRlDASDADVEAAARAAKVDQIVQNLPQGYNTKVGERGLMISGGEKQRLAVARLLLKNPSILFFD 673
Cdd:PRK10790 423 DPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILD 501
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2274528008 674 EATSALDSYTETELMRNINAnlLSEKRTAIFVAHRLRTISDSDLIVVLQSGQVAEKGTHAELMDRKGLYWDLWQAQ 749
Cdd:PRK10790 502 EATANIDSGTEQAIQQALAA--VREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQ 575
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
411-749 |
4.56e-58 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 210.20 E-value: 4.56e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 411 KVATSLAALNSGQNAIFSTsltVMMLLAAQGVTNGTMSVGDLVMVNQLVFQlslplnFLGTVyRELRQSLVDMetmfnle 490
Cdd:TIGR03797 356 RIENLLTVFNAVLPVLTSA---ALFAAAISLLGGAGLSLGSFLAFNTAFGS------FSGAV-TQLSNTLISI------- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 491 nVNV------------AVKENADA--PPLKVTGGeIRFENVTFGYHPDRP-IFSNISFAVPAGYKTAFVGPSGCGKSTIF 555
Cdd:TIGR03797 419 -LAViplwerakpileALPEVDEAktDPGKLSGA-IEVDRVTFRYRPDGPlILDDVSLQIEPGEFVAIVGPSGSGKSTLL 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 556 RLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGVVPQDTPLFNDDIRHNIRYGRLDASDaDVEAAARAAKVDQIVQNLP 635
Cdd:TIGR03797 497 RLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLD-EAWEAARMAGLAEDIRAMP 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 636 QGYNTKVGERGLMISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNINAnllsEKRTAIFVAHRLRTISDS 715
Cdd:TIGR03797 576 MGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLER----LKVTRIVIAHRLSTIRNA 651
|
330 340 350
....*....|....*....|....*....|....
gi 2274528008 716 DLIVVLQSGQVAEKGTHAELMDRKGLYWDLWQAQ 749
Cdd:TIGR03797 652 DRIYVLDAGRVVQQGTYDELMAREGLFAQLARRQ 685
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
510-726 |
1.01e-57 |
|
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: 196.15 E-value: 1.01e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 510 GEIRFENVTFGY--HPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRH 587
Cdd:cd03248 10 GIVKFQNVTFAYptRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 588 IGVVPQDTPLFNDDIRHNIRYGRLDASDADVEAAARAAKVDQIVQNLPQGYNTKVGERGLMISGGEKQRLAVARLLLKNP 667
Cdd:cd03248 90 VSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2274528008 668 SILFFDEATSALDsyTETELMRNINANLLSEKRTAIFVAHRLRTISDSDLIVVLQSGQV 726
Cdd:cd03248 170 QVLILDEATSALD--AESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
396-747 |
2.19e-57 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 205.83 E-value: 2.19e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 396 AKYDAALADYEKSSIKVATSLAALNSGQNA--IFSTSLTVMMLL--AAQGVTNGTMS---VGDLVMVNQLVFQLSLPLnf 468
Cdd:PRK11160 220 DRYRQQLEQTEQQWLAAQRRQANLTGLSQAlmILANGLTVVLMLwlAAGGVGGNAQPgalIALFVFAALAAFEALMPV-- 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 469 lGTVYRELRQSLVDMETMFNLENVNVAVKENADAPPlKVTGGEIRFENVTFGYhPDR--PIFSNISFAVPAGYKTAFVGP 546
Cdd:PRK11160 298 -AGAFQHLGQVIASARRINEITEQKPEVTFPTTSTA-AADQVSLTLNNVSFTY-PDQpqPVLKGLSLQIKAGEKVALLGR 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 547 SGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGVVPQDTPLFNDDIRHNIRYGRLDASDADVEAAARAAK 626
Cdd:PRK11160 375 TGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVG 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 627 VDQIVQNlPQGYNTKVGERGLMISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNINAnlLSEKRTAIFVA 706
Cdd:PRK11160 455 LEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAE--HAQNKTVLMIT 531
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2274528008 707 HRLRTISDSDLIVVLQSGQVAEKGTHAELMDRKGLYWDLWQ 747
Cdd:PRK11160 532 HRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQ 572
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
464-721 |
8.51e-57 |
|
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: 203.29 E-value: 8.51e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 464 LPLNFLGTVYRELRQSLVDMETMFNLENVN---VAVKENADAPPLKvtggEIRFENVTFGYHPDRPIFSNISFAVPAGYK 540
Cdd:TIGR02857 275 LPLRQLGAQYHARADGVAAAEALFAVLDAAprpLAGKAPVTAAPAS----SLEFSGVSVAYPGRRPALRPVSFTVPPGER 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 541 TAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGVVPQDTPLFNDDIRHNIRYGRLDASDADVEA 620
Cdd:TIGR02857 351 VALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIRE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 621 AARAAKVDQIVQNLPQGYNTKVGERGLMISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNINAnlLSEKR 700
Cdd:TIGR02857 431 ALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRA--LAQGR 508
|
250 260
....*....|....*....|.
gi 2274528008 701 TAIFVAHRLRTISDSDLIVVL 721
Cdd:TIGR02857 509 TVLLVTHRLALAALADRIVVL 529
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
359-749 |
6.07e-54 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 196.09 E-value: 6.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 359 RFrKEANAADNRAATTSVDSLLNYEAVKYFNNEKHEIAKYDAALADYEKSSIKVATSLAALNSgqnAIFsTSLTVMMLLA 438
Cdd:PRK10789 164 RF-KLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDP---TIY-IAIGMANLLA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 439 AQG----VTNGTMSVGDL---VMVNQLVFQLSLPLNFL-------GTVYRELRQSLvdmetmfnlenvnvavkenADAP- 503
Cdd:PRK10789 239 IGGgswmVVNGSLTLGQLtsfVMYLGLMIWPMLALAWMfnivergSAAYSRIRAML-------------------AEAPv 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 504 ------PLKVTGGEIRFENVTFGY-HPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDI 576
Cdd:PRK10789 300 vkdgsePVPEGRGELDVNIRQFTYpQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 577 TKVSLESLRRHIGVVPQDTPLFNDDIRHNIRYGRLDASDADVEAAARAAKVDQIVQNLPQGYNTKVGERGLMISGGEKQR 656
Cdd:PRK10789 380 TKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQR 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 657 LAVARLLLKNPSILFFDEATSALDSYTETELMRNInaNLLSEKRTAIFVAHRLRTISDSDLIVVLQSGQVAEKGTHAELM 736
Cdd:PRK10789 460 ISIARALLLNAEILILDDALSAVDGRTEHQILHNL--RQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLA 537
|
410
....*....|...
gi 2274528008 737 DRKGLYWDLWQAQ 749
Cdd:PRK10789 538 QQSGWYRDMYRYQ 550
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
495-738 |
1.04e-51 |
|
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: 189.57 E-value: 1.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 495 AVKENADAPPLKVTGGEIRFENVTFGYhP--DRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYID 572
Cdd:COG4618 314 AVPAEPERMPLPRPKGRLSVENLTVVP-PgsKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLD 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 573 GQDITKVSLESLRRHIGVVPQDTPLFNDDIRHNI-RYGrlDASDADVEAAARAAKVDQIVQNLPQGYNTKVGERGLMISG 651
Cdd:COG4618 393 GADLSQWDREELGRHIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSG 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 652 GEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNInANLLSEKRTAIFVAHRLRTISDSDLIVVLQSGQVAEKGT 731
Cdd:COG4618 471 GQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAI-RALKARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGP 549
|
....*..
gi 2274528008 732 HAELMDR 738
Cdd:COG4618 550 RDEVLAR 556
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
510-731 |
1.05e-51 |
|
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: 179.15 E-value: 1.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 510 GEIRFENVTFGYHPDRP-IFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHI 588
Cdd:cd03369 5 GEIEVENLSVRYAPDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 589 GVVPQDTPLFNDDIRHNI-RYGRLDAsdadveaaaraakvDQIVQNLpqgyntKVGERGLMISGGEKQRLAVARLLLKNP 667
Cdd:cd03369 85 TIIPQDPTLFSGTIRSNLdPFDEYSD--------------EEIYGAL------RVSEGGLNLSQGQRQLLCLARALLKRP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2274528008 668 SILFFDEATSALDSYTETELMRNINANLlsEKRTAIFVAHRLRTISDSDLIVVLQSGQVAEKGT 731
Cdd:cd03369 145 RVLVLDEATASIDYATDALIQKTIREEF--TNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
512-726 |
2.23e-49 |
|
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: 171.25 E-value: 2.23e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYhPD--RPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIG 589
Cdd:cd03246 1 LEVENVSFRY-PGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 590 VVPQDTPLFNDDIRHNIrygrldasdadveaaaraakvdqivqnlpqgyntkvgerglmISGGEKQRLAVARLLLKNPSI 669
Cdd:cd03246 80 YLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2274528008 670 LFFDEATSALDSYTETELMRNInANLLSEKRTAIFVAHRLRTISDSDLIVVLQSGQV 726
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAI-AALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
395-709 |
6.03e-48 |
|
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: 178.32 E-value: 6.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 395 IAKYDAALADYEKSSIKVATSLAALNSGQNAIFSTSLTVMMLLAAQGVTNGTMSVGDLVMVNQLVFQLSLPLNFLGTVYR 474
Cdd:TIGR02868 216 LAQVEEADRELTRAERRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQ 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 475 ELRQSLVDMETMFNLE--NVNVAVKENADAPPLKVTGGEIRFENVTFGYHPDRPIFSNISFAVPAGYKTAFVGPSGCGKS 552
Cdd:TIGR02868 296 QLTRVRAAAERIVEVLdaAGPVAEGSAPAAGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKS 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 553 TIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGVVPQDTPLFNDDIRHNIRYGRLDASDADVEAAARAAKVDQIVQ 632
Cdd:TIGR02868 376 TLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLR 455
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2274528008 633 NLPQGYNTKVGERGLMISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNINANLlsEKRTAIFVAHRL 709
Cdd:TIGR02868 456 ALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAAL--SGRTVVLITHHL 530
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
512-739 |
5.42e-47 |
|
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: 166.74 E-value: 5.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGVV 591
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 592 PQDtP---LFNDDIRHNIRYG--RLDASDADVEaaaraAKVDQIVQnlpqgyntKVGERGLM------ISGGEKQRLAVA 660
Cdd:COG1122 81 FQN-PddqLFAPTVEEDVAFGpeNLGLPREEIR-----ERVEEALE--------LVGLEHLAdrppheLSGGQKQRVAIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 661 RLLLKNPSILFFDEATSALDSYTETELMRNINaNLLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQVAEKGTHAELMDRK 739
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLK-RLNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
460-751 |
1.64e-45 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 172.34 E-value: 1.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 460 FQlslPLNFLGTVYRELRQSLVDMETMFNLENVNVAVKENADAPPLKVTGGEIRFENVTFGYHPDRPIFSNISFAVPAGY 539
Cdd:PRK11174 301 YQ---PLRDLGTFYHAKAQAVGAAESLVTFLETPLAHPQQGEKELASNDPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQ 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 540 KTAFVGPSGCGKSTIFRLLFRFYkPQSGKIYIDGQDITKVSLESLRRHIGVVPQDTPLFNDDIRHNIRYGRLDASDADVE 619
Cdd:PRK11174 378 RIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQ 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 620 AAARAAKVDQIVQNLPQGYNTKVGERGLMISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNINANllSEK 699
Cdd:PRK11174 457 QALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAA--SRR 534
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2274528008 700 RTAIFVAHRLRTISDSDLIVVLQSGQVAEKGTHAELMDRKGLYWDLWQAQST 751
Cdd:PRK11174 535 QTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQE 586
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
513-725 |
2.49e-44 |
|
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: 156.64 E-value: 2.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 513 RFENVTFGYhPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGVVP 592
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 593 QdtplfnddirhnirygrldasdadveaaaraakvdqivqnlpqgyntkvgerglmISGGEKQRLAVARLLLKNPSILFF 672
Cdd:cd00267 80 Q-------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2274528008 673 DEATSALDSYTETELMRNINAnLLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQ 725
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRE-LAEEGRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
528-677 |
1.23e-43 |
|
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: 154.34 E-value: 1.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 528 FSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGVVPQDTPLFND-DIRHNI 606
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2274528008 607 RYGRLDASDADVEaaaRAAKVDQIVQNLPQGY--NTKVGERGLMISGGEKQRLAVARLLLKNPSILFFDEATS 677
Cdd:pfam00005 81 RLGLLLKGLSKRE---KDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
512-730 |
7.59e-43 |
|
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: 153.24 E-value: 7.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGY-HPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSlESLRRHIGV 590
Cdd:cd03247 1 LSINNVSFSYpEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 591 VPQDTPLFNDDIRHNIrygrldasdadveaaaraakvdqivqnlpqgyntkvgerGLMISGGEKQRLAVARLLLKNPSIL 670
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 671 FFDEATSALDSYTETELMRNINANLlsEKRTAIFVAHRLRTISDSDLIVVLQSGQVAEKG 730
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVL--KDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
513-725 |
7.87e-43 |
|
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: 154.55 E-value: 7.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 513 RFENVTFGY-HPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGVV 591
Cdd:cd03225 1 ELKNLSFSYpDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 592 PQ--DTPLFNDDIRHNIRYG--RLDASDADVEaaaraAKVDQIVQnlpqgyntKVGERGLM------ISGGEKQRLAVAR 661
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVAFGleNLGLPEEEIE-----ERVEEALE--------LVGLEGLRdrspftLSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2274528008 662 LLLKNPSILFFDEATSALDSYTETELMRNInANLLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQ 725
Cdd:cd03225 148 VLAMDPDILLLDEPTAGLDPAGRRELLELL-KKLKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
476-742 |
2.03e-42 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 167.13 E-value: 2.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 476 LRQSLVDMEtmfnlENVNVAVKENADapplkvTGGEIRFENVTFGY--HPDRPIFSNISFAVPAGYKTAFVGPSGCGKST 553
Cdd:PTZ00265 1141 IRKSNIDVR-----DNGGIRIKNKND------IKGKIEIMDVNFRYisRPNVPIYKDLTFSCDSKKTTAIVGETGSGKST 1209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 554 IFRLLFRFYK------------------------------------------------------PQSGKIYIDGQDITKV 579
Cdd:PTZ00265 1210 VMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDY 1289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 580 SLESLRRHIGVVPQDTPLFNDDIRHNIRYGRLDASDADVEAAARAAKVDQIVQNLPQGYNTKVGERGLMISGGEKQRLAV 659
Cdd:PTZ00265 1290 NLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAI 1369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 660 ARLLLKNPSILFFDEATSALDSYTETELMRNINANLLSEKRTAIFVAHRLRTISDSDLIVVLQSGQ-----VAEKGTHAE 734
Cdd:PTZ00265 1370 ARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEE 1449
|
....*....
gi 2274528008 735 LMD-RKGLY 742
Cdd:PTZ00265 1450 LLSvQDGVY 1458
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
512-707 |
6.87e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 151.89 E-value: 6.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGVV 591
Cdd:COG4619 1 LELEGLSFRVG-GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 592 PQDTPLFNDDIRHNIRYGRLDAsdadvEAAARAAKVDQIVQ--NLPQGY-NTKVGErglmISGGEKQRLAVARLLLKNPS 668
Cdd:COG4619 80 PQEPALWGGTVRDNLPFPFQLR-----ERKFDRERALELLErlGLPPDIlDKPVER----LSGGERQRLALIRALLLQPD 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 2274528008 669 ILFFDEATSALDSYTETELMRNINANLLSEKRTAIFVAH 707
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSH 189
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
456-775 |
2.09e-41 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 163.99 E-value: 2.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 456 NQLVFQ------LSLPLNFLGTVYRELRQ------SLVDME---TMFNLENVNVAVKENADAPPLKVTGGEIRFENVTFG 520
Cdd:PLN03232 1164 NQAGFAstmgllLSYTLNITTLLSGVLRQaskaenSLNSVErvgNYIDLPSEATAIIENNRPVSGWPSRGSIKFEDVHLR 1243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 521 YHPD-RPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGVVPQDTPLFN 599
Cdd:PLN03232 1244 YRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFS 1323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 600 DDIRHNIRYGRlDASDADVEAAARAAKVDQIVQNLPQGYNTKVGERGLMISGGEKQRLAVARLLLKNPSILFFDEATSAL 679
Cdd:PLN03232 1324 GTVRFNIDPFS-EHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASV 1402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 680 DSYTETELMRNINANLLSekRTAIFVAHRLRTISDSDLIVVLQSGQVAEKGTHAELMDRKGLYWdLWQAQSTlgvghGAG 759
Cdd:PLN03232 1403 DVRTDSLIQRTIREEFKS--CTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF-FRMVHST-----GPA 1474
|
330
....*....|....*....
gi 2274528008 760 ANEHLQDL---EREQGQSQ 775
Cdd:PLN03232 1475 NAQYLSNLvfeRRENGMSL 1493
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
512-737 |
3.13e-40 |
|
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: 148.03 E-value: 3.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVS---LESLRRHI 588
Cdd:cd03261 1 IELRGLTKSFG-GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 589 GVVPQDTPLFND-DIRHNI-----RYGRLDASDadveaaaraakVDQIVQ------NLPQGYNTKVGErglmISGGEKQR 656
Cdd:cd03261 80 GMLFQSGALFDSlTVFENVafplrEHTRLSEEE-----------IREIVLekleavGLRGAEDLYPAE----LSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 657 LAVARLLLKNPSILFFDEATSALDSYTET---ELMRNINANLlseKRTAIFVAHRLRTI-SDSDLIVVLQSGQVAEKGTH 732
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDPIASGvidDLIRSLKKEL---GLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTP 221
|
....*
gi 2274528008 733 AELMD 737
Cdd:cd03261 222 EELRA 226
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
512-738 |
8.92e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 146.75 E-value: 8.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYhPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLEsLRRHIGVV 591
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 592 PQDTPLFND-DIRHNIRY-GRLdasdADVEAAARAAKVDQIVQ--NLPQGYNTKVGErglmISGGEKQRLAVARLLLKNP 667
Cdd:COG1131 79 PQEPALYPDlTVRENLRFfARL----YGLPRKEARERIDELLElfGLTDAADRKVGT----LSGGMKQRLGLALALLHDP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2274528008 668 SILFFDEATSALDSYTETELMRNINAnlLSEKRTAIFVA-HRLRTISD-SDLIVVLQSGQVAEKGTHAELMDR 738
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWELLRE--LAAEGKTVLLStHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
495-778 |
1.18e-39 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 158.75 E-value: 1.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 495 AVKENADAPPLKVTGGEIRFENVTFGYHPD-RPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDG 573
Cdd:PLN03130 1221 LVIENNRPPPGWPSSGSIKFEDVVLRYRPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDG 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 574 QDITKVSLESLRRHIGVVPQDTPLFNDDIRHNirygrLDA----SDADVEAAARAAKVDQIVQNLPQGYNTKVGERGLMI 649
Cdd:PLN03130 1301 CDISKFGLMDLRKVLGIIPQAPVLFSGTVRFN-----LDPfnehNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENF 1375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 650 SGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNINANLLSekRTAIFVAHRLRTISDSDLIVVLQSGQVAEK 729
Cdd:PLN03130 1376 SVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKS--CTMLIIAHRLNTIIDCDRILVLDAGRVVEF 1453
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2274528008 730 GTHAELMDRKGLYWDLwQAQSTlgvghGAGANEHLQDLEREQGQSQKTE 778
Cdd:PLN03130 1454 DTPENLLSNEGSAFSK-MVQST-----GAANAQYLRSLVFGGDEDRLAR 1496
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
512-737 |
2.49e-39 |
|
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: 145.51 E-value: 2.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVS---LESLRRHI 588
Cdd:COG1127 6 IEVRNLTKSFG-DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 589 GVVPQDTPLFND-DIRHNI-----RYGRLDASDadveaaaraakVDQIVqnlpqgyNTK---VGERG---LM---ISGGE 653
Cdd:COG1127 85 GMLFQGGALFDSlTVFENVafplrEHTDLSEAE-----------IRELV-------LEKlelVGLPGaadKMpseLSGGM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 654 KQRLAVARLLLKNPSILFFDEATSALDSYTET---ELMRNINANLlseKRTAIFVAHRLRTISD-SDLIVVLQSGQVAEK 729
Cdd:COG1127 147 RKRVALARALALDPEILLYDEPTAGLDPITSAvidELIRELRDEL---GLTSVVVTHDLDSAFAiADRVAVLADGKIIAE 223
|
....*...
gi 2274528008 730 GTHAELMD 737
Cdd:COG1127 224 GTPEELLA 231
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
512-737 |
1.09e-38 |
|
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: 144.42 E-value: 1.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYhPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGVV 591
Cdd:COG1120 2 LEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 592 PQDTPLfNDDI--RHNIRYGRL-------DASDADVEaaaraaKVDQIVQnlpqgyntKVG-----ERGLM-ISGGEKQR 656
Cdd:COG1120 81 PQEPPA-PFGLtvRELVALGRYphlglfgRPSAEDRE------AVEEALE--------RTGlehlaDRPVDeLSGGERQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 657 LAVARLLLKNPSILFFDEATSALDSYTETELM---RNINAnllSEKRTAIFVAHrlrtisD-------SDLIVVLQSGQV 726
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDLAHQLEVLellRRLAR---ERGRTVVMVLH------DlnlaaryADRLVLLKDGRI 216
|
250
....*....|.
gi 2274528008 727 AEKGTHAELMD 737
Cdd:COG1120 217 VAQGPPEEVLT 227
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
475-723 |
1.67e-38 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 154.80 E-value: 1.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 475 ELRQSLVDMETMFNLENVNVAVKENADAPPLKVTGgEIRFENVTFGY--HPDRPIFSNISFAVPAGYKTAFVGPSGCGKS 552
Cdd:PTZ00265 347 EYMKSLEATNSLYEIINRKPLVENNDDGKKLKDIK-KIQFKNVRFHYdtRKDVEIYKDLNFTLTEGKTYAFVGESGCGKS 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 553 TIFRLLFRFYKPQSGKIYI-DGQDITKVSLESLRRHIGVVPQDTPLFNDDIRHNIRYG-----RLDA------------- 613
Cdd:PTZ00265 426 TILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkDLEAlsnyynedgndsq 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 614 ---------------------------------------SDADVEAAARAAKVDQIVQNLPQGYNTKVGERGLMISGGEK 654
Cdd:PTZ00265 506 enknkrnscrakcagdlndmsnttdsneliemrknyqtiKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQK 585
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2274528008 655 QRLAVARLLLKNPSILFFDEATSALDSYTETELMRNINANLLSEKRTAIFVAHRLRTISDSDLIVVLQS 723
Cdd:PTZ00265 586 QRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYANTIFVLSN 654
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
512-725 |
4.38e-38 |
|
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: 140.01 E-value: 4.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLES--LRRHIG 589
Cdd:cd03229 1 LELKNVSKRYG-QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 590 VVPQDTPLF-NDDIRHNIRYGrldasdadveaaaraakvdqivqnlpqgyntkvgerglmISGGEKQRLAVARLLLKNPS 668
Cdd:cd03229 80 MVFQDFALFpHLTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2274528008 669 ILFFDEATSALDSYTETE---LMRNINANLlseKRTAIFVAHRL---RTISDSdlIVVLQSGQ 725
Cdd:cd03229 121 VLLLDEPTSALDPITRREvraLLKSLQAQL---GITVVLVTHDLdeaARLADR--VVVLRDGK 178
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
512-730 |
1.14e-37 |
|
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: 139.96 E-value: 1.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPDRpIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLEslRRHIGVV 591
Cdd:cd03259 1 LELKGLSKTYGSVR-ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 592 PQDTPLF-NDDIRHNIRYG--RLDASDADVEaaaraAKVDQIVQ--NLPQGYNTKVGErglmISGGEKQRLAVARLLLKN 666
Cdd:cd03259 78 FQDYALFpHLTVAENIAFGlkLRGVPKAEIR-----ARVRELLElvGLEGLLNRYPHE----LSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2274528008 667 PSILFFDEATSALDSYTETELMRNINANLLSEKRTAIFVAHRLR-TISDSDLIVVLQSGQVAEKG 730
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
515-730 |
1.34e-37 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 138.72 E-value: 1.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 515 ENVTFGYHpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGVVPQd 594
Cdd:cd03214 3 ENLSVGYG-GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 595 tplfnddirhNIRygRLDASDadveaaaraaKVDQIVQNLpqgyntkvgerglmiSGGEKQRLAVARLLLKNPSILFFDE 674
Cdd:cd03214 81 ----------ALE--LLGLAH----------LADRPFNEL---------------SGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2274528008 675 ATSALDSYTETELMRNINANLLSEKRTAIFVAHRL-RTISDSDLIVVLQSGQVAEKG 730
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
512-736 |
1.45e-37 |
|
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: 140.51 E-value: 1.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGVV 591
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 592 PQDTPLF-NDDIRHNIRygrLDASDADVEAAARAAKVDQIVQNL---PQGYNTKVGERglmISGGEKQRLAVARLLLKNP 667
Cdd:cd03295 81 IQQIGLFpHMTVEENIA---LVPKLLKWPKEKIRERADELLALVgldPAEFADRYPHE---LSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2274528008 668 SILFFDEATSALDSYTETEL---MRNINANLlseKRTAIFVAHRL-RTISDSDLIVVLQSGQVAEKGTHAELM 736
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLqeeFKRLQQEL---GKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
512-730 |
4.36e-37 |
|
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: 138.85 E-value: 4.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPDRpIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYK-----PQSGKIYIDGQDITK--VSLESL 584
Cdd:cd03260 1 IELRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDldVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 585 RRHIGVVPQDTPLFNDDIRHNIRY-----GRLDASDADVEAAARAAKVDqivqnLPQGYNTKVGERGLmiSGGEKQRLAV 659
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYglrlhGIKLKEELDERVEEALRKAA-----LWDEVKDRLHALGL--SGGQQQRLCL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2274528008 660 ARLLLKNPSILFFDEATSALDSY-TET--ELMRNinanlLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQVAEKG 730
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPIsTAKieELIAE-----LKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFG 222
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
512-734 |
4.46e-37 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 138.65 E-value: 4.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPDRPIFSNISFAVPAGyktAFV---GPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVS---LESLR 585
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKG---EFVfltGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 586 RHIGVVPQDTPLFND-DIRHNIRY-----GRldaSDADVEaaaraAKVDQIVQnlpqgyntKVGERGLM------ISGGE 653
Cdd:COG2884 79 RRIGVVFQDFRLLPDrTVYENVALplrvtGK---SRKEIR-----RRVREVLD--------LVGLSDKAkalpheLSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 654 KQRLAVARLLLKNPSILFFDEATSALDSYTETELMR---NINANllsekRTAIFVA-HrlrtisDSDLI-------VVLQ 722
Cdd:COG2884 143 QQRVAIARALVNRPELLLADEPTGNLDPETSWEIMElleEINRR-----GTTVLIAtH------DLELVdrmpkrvLELE 211
|
250
....*....|..
gi 2274528008 723 SGQVAEKGTHAE 734
Cdd:COG2884 212 DGRLVRDEARGV 223
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
512-730 |
6.44e-37 |
|
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: 138.41 E-value: 6.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPDR---PIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVS---LESLR 585
Cdd:cd03257 2 LEVKNLSVSFPTGGgsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 586 RHIGVVPQD-----TPLFNddIRHNIR-----YGRLDASDADVEAAARAAKVdqiVQNLPQGYNTKVGErglmISGGEKQ 655
Cdd:cd03257 82 KEIQMVFQDpmsslNPRMT--IGEQIAeplriHGKLSKKEARKEAVLLLLVG---VGLPEEVLNRYPHE----LSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2274528008 656 RLAVARLLLKNPSILFFDEATSALDSYTETE---LMRNINANLlseKRTAIFVAHRLRTISD-SDLIVVLQSGQVAEKG 730
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQildLLKKLQEEL---GLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
512-725 |
7.41e-37 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 137.22 E-value: 7.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPDR----PIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGqditkvsleslrrH 587
Cdd:cd03250 1 ISVEDASFTWDSGEqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 588 IGVVPQdTP-LFNDDIRHNIRYGR----------LDAS--DADVEaaaraakvdqivqNLPQGYNTKVGERGLMISGGEK 654
Cdd:cd03250 68 IAYVSQ-EPwIQNGTIRENILFGKpfdeeryekvIKACalEPDLE-------------ILPDGDLTEIGEKGINLSGGQK 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2274528008 655 QRLAVARLLLKNPSILFFDEATSALDSYTETELMRNINANLLSEKRTAIFVAHRLRTISDSDLIVVLQSGQ 725
Cdd:cd03250 134 QRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
516-738 |
1.24e-36 |
|
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: 138.01 E-value: 1.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 516 NVTFGYHPDR-PIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGVVPQD 594
Cdd:COG1124 8 SVSYGQGGRRvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 595 tPLFNDDIRHNIR---------YGRLDASDadveaaaraaKVDQIVQ--NLPQGYNTKvgeRGLMISGGEKQRLAVARLL 663
Cdd:COG1124 88 -PYASLHPRHTVDrilaeplriHGLPDREE----------RIAELLEqvGLPPSFLDR---YPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2274528008 664 LKNPSILFFDEATSALDSYTETELMRNINANLLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQVAEKGTHAELMDR 738
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLAG 229
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
512-726 |
1.36e-36 |
|
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: 135.60 E-value: 1.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYhPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKvSLESLRRHIGVV 591
Cdd:cd03230 1 IEVRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 592 PQDTPLFND-DIRHNIRYgrldasdadveaaaraakvdqivqnlpqgyntkvgerglmiSGGEKQRLAVARLLLKNPSIL 670
Cdd:cd03230 79 PEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2274528008 671 FFDEATSALDSYTETELMRNINAnLLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQV 726
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRE-LKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
512-738 |
2.70e-36 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 140.23 E-value: 2.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLEslRRHIGVV 591
Cdd:COG3842 6 LELENVSKRYG-DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 592 PQDTPLF-NDDIRHNIRYG----RLDASDADveaaaraAKVDQIVQ--NLpQGY-NTKVGErglmISGGEKQRLAVARLL 663
Cdd:COG3842 83 FQDYALFpHLTVAENVAFGlrmrGVPKAEIR-------ARVAELLElvGL-EGLaDRYPHQ----LSGGQQQRVALARAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 664 LKNPSILFFDEATSALDSYTETELMRNInANLLSE-KRTAIFVAHrlrtisD-------SDLIVVLQSGQVAEKGTHAEL 735
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLREEMREEL-RRLQRElGITFIYVTH------DqeealalADRIAVMNDGRIEQVGTPEEI 223
|
...
gi 2274528008 736 MDR 738
Cdd:COG3842 224 YER 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
512-726 |
1.06e-35 |
|
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: 134.54 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPDR---PIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVS---LESLR 585
Cdd:cd03255 1 IELKNLSKTYGGGGekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekeLAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 586 R-HIGVVPQDTPLFND-DIRHNI----RYGRLDASDADVEAAARAAKVDqivqnLPQGYNTKVGErglmISGGEKQRLAV 659
Cdd:cd03255 81 RrHIGFVFQSFNLLPDlTALENVelplLLAGVPKKERRERAEELLERVG-----LGDRLNHYPSE----LSGGQQQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 660 ARLLLKNPSILFFDEATSALDSYTE---TELMRNINANllsEKRTAIFVAHRLRTISDSDLIVVLQSGQV 726
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGkevMELLRELNKE---AGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
494-738 |
1.50e-35 |
|
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: 141.58 E-value: 1.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 494 VAVKENADAPPLkvtggeIRFENVTFGYH----PDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKI 569
Cdd:COG1123 249 RAAPAAAAAEPL------LEVRNLSKRYPvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 570 YIDGQDITKVS---LESLRRHIGVVPQDtPL--FNDdiRHNIR---------YGRLDASDADveaaaraAKVDQIVQ--N 633
Cdd:COG1123 323 LFDGKDLTKLSrrsLRELRRRVQMVFQD-PYssLNP--RMTVGdiiaeplrlHGLLSRAERR-------ERVAELLErvG 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 634 LPQGYntkVGERGLMISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMrninaNLLSE-----KRTAIFVAHR 708
Cdd:COG1123 393 LPPDL---ADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQIL-----NLLRDlqrelGLTYLFISHD 464
|
250 260 270
....*....|....*....|....*....|.
gi 2274528008 709 LRTISD-SDLIVVLQSGQVAEKGTHAELMDR 738
Cdd:COG1123 465 LAVVRYiADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
183-466 |
2.45e-35 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 135.46 E-value: 2.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 183 VALALALLVGGKLLNVQVPFFFKAIVDRLnqvvnapLDMTNPNTVWVVAGSaiLGYGLARVGAAAFSELRNAVFANVAQQ 262
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVL-------LPDGDPETQALNVYS--LALLLLGLAQFILSFLQSYLLNHTGER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 263 SIRRVARSVFTHLLALDLGWHLTRQTGGLTRAIDRGTKGISFLLTSIVFHIVPTALEISMVCGILSYKcGPSFAAVTAVT 342
Cdd:pfam00664 72 LSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYY-GWKLTLVLLAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 343 MAAYAWFTIRTTSWRTRFRKEANAADNRAATTSVDSLLNYEAVKYFNNEKHEIAKYDAALADYEKSSIKVATSLAALNSG 422
Cdd:pfam00664 151 LPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGI 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2274528008 423 QNAIFSTSLTVMMLLAAQGVTNGTMSVGDLVMVNQLVFQLSLPL 466
Cdd:pfam00664 231 TQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
512-728 |
1.38e-34 |
|
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: 131.44 E-value: 1.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPDR---PIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSleslrRHI 588
Cdd:cd03293 1 LEVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 589 GVVPQDTPLF---NddIRHNIRYGrLDAsdADVEAAARAAKVDQIVQnlpqgyntKVGERGL------MISGGEKQRLAV 659
Cdd:cd03293 76 GYVFQQDALLpwlT--VLDNVALG-LEL--QGVPKAEARERAEELLE--------LVGLSGFenayphQLSGGMRQRVAL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2274528008 660 ARLLLKNPSILFFDEATSALDSYTETELMRNINANLLSEKRTAIFVAHRLR-TISDSDLIVVLQS--GQVAE 728
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
513-744 |
2.02e-34 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 130.73 E-value: 2.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 513 RFENVTFGYHpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVsleslRRHIGVVP 592
Cdd:cd03235 1 EVEDLTVSYG-GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 593 Q------DTPLFNDDI------RHNIRYGRLDASDADveaaaraaKVDQIVQnlpqgyntKVGERGL------MISGGEK 654
Cdd:cd03235 75 QrrsidrDFPISVRDVvlmglyGHKGLFRRLSKADKA--------KVDEALE--------RVGLSELadrqigELSGGQQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 655 QRLAVARLLLKNPSILFFDEATSALDSYTETELMRNINaNLLSEKRTAIFVAHrlrtisdsDLivvlqsGQVAEKGTHAE 734
Cdd:cd03235 139 QRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLR-ELRREGMTILVVTH--------DL------GLVLEYFDRVL 203
|
250
....*....|
gi 2274528008 735 LMDRKGLYWD 744
Cdd:cd03235 204 LLNRTVVASG 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
512-735 |
2.39e-34 |
|
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: 131.16 E-value: 2.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVT--FGYHPDR-PIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVS---LESLR 585
Cdd:cd03258 2 IELKNVSkvFGDTGGKvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkeLRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 586 RHIGVVPQDTPLFND-DIRHNIRYG-RLdasdADVEAAARAAKVDQIVQNLpqGYNTKVGERGLMISGGEKQRLAVARLL 663
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALPlEI----AGVPKAEIEERVLELLELV--GLEDKADAYPAQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2274528008 664 LKNPSILFFDEATSALDSYTET---ELMRNINANLlseKRTAIFVAHRLRTISD-SDLIVVLQSGQVAEKGTHAEL 735
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQsilALLRDINREL---GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
460-745 |
2.68e-34 |
|
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: 141.62 E-value: 2.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 460 FQLSLPLNFLGTVYRELRQSLVDMEtmfNLENVNVAVKE-----NADAPPLK-VTGGEIRFENVTFGYHPDRP-IFSNIS 532
Cdd:TIGR00957 1230 LQVTFYLNWLVRMSSEMETNIVAVE---RLKEYSETEKEapwqiQETAPPSGwPPRGRVEFRNYCLRYREDLDlVLRHIN 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 533 FAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGVVPQDTPLFNDDIRHNIR-YGRL 611
Cdd:TIGR00957 1307 VTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDpFSQY 1386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 612 daSDADVEAAARAAKVDQIVQNLPQGYNTKVGERGLMISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNI 691
Cdd:TIGR00957 1387 --SDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTI 1464
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2274528008 692 NANLlsEKRTAIFVAHRLRTISDSDLIVVLQSGQVAEKGTHAELMDRKGLYWDL 745
Cdd:TIGR00957 1465 RTQF--EDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
512-728 |
1.28e-33 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 129.01 E-value: 1.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYH---PDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVS---LESLR 585
Cdd:COG1136 5 LELRNLTKSYGtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSereLARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 586 R-HIGVVPQDTPLFND-DIRHNI----RYGRLDASDADveaaaraAKVDQIVQnlpqgyntKVGERGLM------ISGGE 653
Cdd:COG1136 85 RrHIGFVFQFFNLLPElTALENValplLLAGVSRKERR-------ERARELLE--------RVGLGDRLdhrpsqLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2274528008 654 KQRLAVARLLLKNPSILFFDEATSALDSYTETE---LMRNINANLlseKRTAIFVAHRLRTISDSDLIVVLQSGQVAE 728
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEvleLLRELNREL---GTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
512-741 |
2.16e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 128.67 E-value: 2.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVsleslRRHIGVV 591
Cdd:COG1121 7 IELENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 592 PQDTPlFNDD-------------IRHNIRYGRLDASDADveaaaraaKVDQIVQ--NLpQGY-NTKVGErglmISGGEKQ 655
Cdd:COG1121 81 PQRAE-VDWDfpitvrdvvlmgrYGRRGLFRRPSRADRE--------AVDEALErvGL-EDLaDRPIGE----LSGGQQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 656 RLAVARLLLKNPSILFFDEATSALDSYTETELMRNInANLLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQVAEkGTHAE 734
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELL-RELRREGKTILVVTHDLGAVREyFDRVLLLNRGLVAH-GPPEE 224
|
....*..
gi 2274528008 735 LMDRKGL 741
Cdd:COG1121 225 VLTPENL 231
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
512-739 |
4.04e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 128.96 E-value: 4.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPD-RPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGV 590
Cdd:PRK13632 8 IKVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 591 VPQDtP-------LFNDDIRHNIRYGRLDASdadveaaaraaKVDQIVQNlpqgYNTKVGERGLM------ISGGEKQRL 657
Cdd:PRK13632 88 IFQN-PdnqfigaTVEDDIAFGLENKKVPPK-----------KMKDIIDD----LAKKVGMEDYLdkepqnLSGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 658 AVARLLLKNPSILFFDEATSALD---SYTETELMRNINANllsEKRTAIFVAHRLRTISDSDLIVVLQSGQVAEKGTHAE 734
Cdd:PRK13632 152 AIASVLALNPEIIIFDESTSMLDpkgKREIKKIMVDLRKT---RKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKE 228
|
....*
gi 2274528008 735 LMDRK 739
Cdd:PRK13632 229 ILNNK 233
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
529-738 |
6.04e-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: 127.07 E-value: 6.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 529 SNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLEslRRHIGVVPQDTPLF-NDDIRHNIR 607
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 608 YG-RLdasdADVEAAARAAKVDQIVQNLPQGY--NTKVGErglmISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTE 684
Cdd:cd03299 94 YGlKK----RKVDKKEIERKVLEIAEMLGIDHllNRKPET----LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2274528008 685 TELMRNINANLLSEKRTAIFVAHRLRTI-SDSDLIVVLQSGQVAEKGTHAELMDR 738
Cdd:cd03299 166 EKLREELKKIRKEFGVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
511-736 |
6.02e-32 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 125.13 E-value: 6.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 511 EIRFENVTFGYHpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGV 590
Cdd:PRK11231 2 TLRTENLTVGYG-TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 591 VPQdTPLFNDDI--RHNIRYGR---------LDASDadveaaarAAKVDQIVQnlpQGYNTKVGERGLM-ISGGEKQRLA 658
Cdd:PRK11231 81 LPQ-HHLTPEGItvRELVAYGRspwlslwgrLSAED--------NARVNQAME---QTRINHLADRRLTdLSGGQRQRAF 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2274528008 659 VARLLLKNPSILFFDEATSALDSYTETELMRNINaNLLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQVAEKGTHAELM 736
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMR-ELNTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVM 226
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
512-737 |
6.13e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 125.25 E-value: 6.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPDRPI-FSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGV 590
Cdd:PRK13648 8 IVFKNVSFQYQSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 591 VPQ--DTPLFNDDIRHNIRYGRLDASdadVEAAARAAKVDQIVQNL---------PQGyntkvgerglmISGGEKQRLAV 659
Cdd:PRK13648 88 VFQnpDNQFVGSIVKYDVAFGLENHA---VPYDEMHRRVSEALKQVdmleradyePNA-----------LSGGQKQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2274528008 660 ARLLLKNPSILFFDEATSALDSYTETELMRNINaNLLSEKR-TAIFVAHRLRTISDSDLIVVLQSGQVAEKGTHAELMD 737
Cdd:PRK13648 154 AGVLALNPSVIILDEATSMLDPDARQNLLDLVR-KVKSEHNiTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
512-738 |
1.00e-31 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 123.95 E-value: 1.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVT--FGyhpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDIT--KVSLESLRRH 587
Cdd:COG1126 2 IEIENLHksFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdsKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 588 IGVVPQDTPLFND-DIRHNIRYG-----RLDASDADVEAAARAAKVdqivqnlpqgyntkvgerGL---------MISGG 652
Cdd:COG1126 79 VGMVFQQFNLFPHlTVLENVTLApikvkKMSKAEAEERAMELLERV------------------GLadkadaypaQLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 653 EKQRLAVARLLLKNPSILFFDEATSALDSytetEL-------MRninaNLLSEKRTAIFVAHRL---RTISDSdlIVVLQ 722
Cdd:COG1126 141 QQQRVAIARALAMEPKVMLFDEPTSALDP----ELvgevldvMR----DLAKEGMTMVVVTHEMgfaREVADR--VVFMD 210
|
250
....*....|....*.
gi 2274528008 723 SGQVAEKGTHAELMDR 738
Cdd:COG1126 211 GGRIVEEGPPEEFFEN 226
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
511-738 |
2.91e-31 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 125.64 E-value: 2.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 511 EIRFENVTFGYhPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITkVSLESLRRHIGV 590
Cdd:COG1118 2 SIEVRNISKRF-GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF-TNLPPRERRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 591 VPQDTPLFnddiRH-----NIRYG--RLDASDADVEAaaraaKVDQ---IVQnLPQGYNTKVGErglmISGGEKQRLAVA 660
Cdd:COG1118 80 VFQHYALF----PHmtvaeNIAFGlrVRPPSKAEIRA-----RVEElleLVQ-LEGLADRYPSQ----LSGGQRQRVALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 661 RLLLKNPSILFFDEATSALDSYTETELMRNInANLLSE-KRTAIFVAH------RLrtisdSDLIVVLQSGQVAEKGTHA 733
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALDAKVRKELRRWL-RRLHDElGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPD 219
|
....*
gi 2274528008 734 ELMDR 738
Cdd:COG1118 220 EVYDR 224
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
513-726 |
2.97e-31 |
|
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: 121.21 E-value: 2.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 513 RFENVTFGYHPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDItkvSLESLRRHIGVVP 592
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 593 QDT--PLFNDDIRHNIRYGrLDASDADVEaaaraaKVDQIVQNLpqGYNTKVGERGLMISGGEKQRLAVARLLLKNPSIL 670
Cdd:cd03226 78 QDVdyQLFTDSVREELLLG-LKELDAGNE------QAETVLKDL--DLYALKERHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2274528008 671 FFDEATSALDSYTetelMRNInANL---LSEKRTAIFVA-HRLRTISD-SDLIVVLQSGQV 726
Cdd:cd03226 149 IFDEPTSGLDYKN----MERV-GELireLAAQGKAVIVItHDYEFLAKvCDRVLLLANGAI 204
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
509-739 |
3.73e-31 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 122.71 E-value: 3.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 509 GGEIRFENVTFGYHPD-RPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRH 587
Cdd:cd03288 17 GGEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 588 IGVVPQDTPLFNDDIRHNIRYGRlDASDADVEAAARAAKVDQIVQNLPQGYNTKVGERGLMISGGEKQRLAVARLLLKNP 667
Cdd:cd03288 97 LSIILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKS 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2274528008 668 SILFFDEATSALDSYTETELMRNINANLlsEKRTAIFVAHRLRTISDSDLIVVLQSGQVAEKGTHAELMDRK 739
Cdd:cd03288 176 SILIMDEATASIDMATENILQKVVMTAF--ADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQE 245
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
512-728 |
1.19e-30 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 121.35 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHP---DRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSleslrRHI 588
Cdd:COG1116 8 LELRGVSKRFPTgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG-----PDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 589 GVVPQDTPLF---NddIRHNIRYGrLDAsdADVEAAARAAKVDQIVQnlpqgyntKVGERGLM------ISGGEKQRLAV 659
Cdd:COG1116 83 GVVFQEPALLpwlT--VLDNVALG-LEL--RGVPKAERRERARELLE--------LVGLAGFEdayphqLSGGMRQRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2274528008 660 ARLLLKNPSILFFDEATSALDSYTETELMRNINANLLSEKRTAIFVAH------RLrtisdSDLIVVLQS--GQVAE 728
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIVE 221
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
512-736 |
1.60e-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: 121.38 E-value: 1.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHP-DRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQD-ITKVSLESLRRHIG 589
Cdd:TIGR04520 1 IEVENVSFSYPEsEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDtLDEENLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 590 VVPQD------TPLFNDDI----------RHNIRYgRLDASDADVEAAARAakvDQIVQNLpqgyntkvgerglmiSGGE 653
Cdd:TIGR04520 81 MVFQNpdnqfvGATVEDDVafglenlgvpREEMRK-RVDEALKLVGMEDFR---DREPHLL---------------SGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 654 KQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNINANLLSEKRTAIFVAHRLRTISDSDLIVVLQSGQVAEKGTHA 733
Cdd:TIGR04520 142 KQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPR 221
|
...
gi 2274528008 734 ELM 736
Cdd:TIGR04520 222 EIF 224
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
183-484 |
3.15e-30 |
|
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: 121.12 E-value: 3.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 183 VALALALLVGGKLLNVQVPFFFKAIVDRLNqvvnapldmtnPNTVWVVAGSAILGYGLARVGAAAFSELRNAVFANVAQQ 262
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVI-----------PAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 263 SIRRVARSVFTHLLALDLGWHLTRQTGGLTRAIDRGTKGISFLLTSIVFHIVPTALEISMVCGILSYKcGPSFAAVTAVT 342
Cdd:cd07346 70 VVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYL-NWKLTLVALLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 343 MAAYAWFTIRTTSWRTRFRKEANAADNRAATTSVDSLLNYEAVKYFNNEKHEIAKYDAALADYEKSSIKVATSLAALNSG 422
Cdd:cd07346 149 LPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPL 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2274528008 423 QNAIFSTSLTVMMLLAAQGVTNGTMSVGDLVMVNQLVFQLSLPLNFLGTVYRELRQSLVDME 484
Cdd:cd07346 229 IGLLTALGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLE 290
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
512-738 |
3.66e-30 |
|
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: 125.40 E-value: 3.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHP-DRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQ---SGKIYIDGQDITKVSLESLRRH 587
Cdd:COG1123 5 LEVRDLSVRYPGgDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 588 IGVVPQDtPL--FN-----DDIRHNIRYGRLDASDADVEAAARAAKVDqivqnLPQGYNTKVGErglmISGGEKQRLAVA 660
Cdd:COG1123 85 IGMVFQD-PMtqLNpvtvgDQIAEALENLGLSRAEARARVLELLEAVG-----LERRLDRYPHQ----LSGGQRQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2274528008 661 RLLLKNPSILFFDEATSALDSYTETELMRNINANLLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQVAEKGTHAELMDR 738
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
512-730 |
9.05e-30 |
|
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: 117.36 E-value: 9.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYhPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVslESLRRHIGVV 591
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDL--PPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 592 PQDTPLF-NDDIRHNIRYG------RLDASDADVEAAARAAKVDQIVQNLPQgyntkvgerglMISGGEKQRLAVARLLL 664
Cdd:cd03301 78 FQNYALYpHMTVYDNIAFGlklrkvPKDEIDERVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRAIV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2274528008 665 KNPSILFFDEATSALDSYTETElMRNINANLLSE-KRTAIFVAH-RLRTISDSDLIVVLQSGQVAEKG 730
Cdd:cd03301 147 REPKVFLMDEPLSNLDAKLRVQ-MRAELKRLQQRlGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
462-742 |
1.72e-29 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 126.21 E-value: 1.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 462 LSLPLNFLGTVYRELRQSLVDMETMFNLENVNVAVKENADAPPLKVTGG-EIRFENVTFGY-HPDRPIFSNISFAVPAGY 539
Cdd:TIGR00957 586 LRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPGEGnSITVHNATFTWaRDLPPTLNGITFSIPEGA 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 540 KTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQditkvsleslrrhIGVVPQDTPLFNDDIRHNIRYGR--------- 610
Cdd:TIGR00957 666 LVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQAWIQNDSLRENILFGKalnekyyqq 732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 611 -LDASD--ADVEAaaraakvdqivqnLPQGYNTKVGERGLMISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETEL 687
Cdd:TIGR00957 733 vLEACAllPDLEI-------------LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHI 799
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2274528008 688 MRN-INANLLSEKRTAIFVAHRLRTISDSDLIVVLQSGQVAEKGTHAELMDRKGLY 742
Cdd:TIGR00957 800 FEHvIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
531-763 |
1.79e-29 |
|
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: 120.60 E-value: 1.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 531 ISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDG---QDITK-VSLESLRRHIGVVPQDTPLFND-DIRHN 605
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKgIFLPPEKRRIGYVFQEARLFPHlSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 606 IRYGRldaSDADVEAAARAAkvDQIVQNLpqGYNTKVGERGLMISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTET 685
Cdd:TIGR02142 96 LRYGM---KRARPSERRISF--ERVIELL--GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 686 ELM---RNINANLlseKRTAIFVAHRLRTISD-SDLIVVLQSGQVAEKGTHAELMDRKGLYWDLWQAQSTLGVGHGAGAN 761
Cdd:TIGR02142 169 EILpylERLHAEF---GIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASPDLPWLAREDQGSLIEGVVAEHD 245
|
..
gi 2274528008 762 EH 763
Cdd:TIGR02142 246 QH 247
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
509-730 |
4.51e-29 |
|
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: 114.57 E-value: 4.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 509 GGEIRFENVTFGYHPD-----RPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLL--FRFYKPQSGKIYIDGqdiTKVSL 581
Cdd:cd03213 1 GVTLSFRNLTVTVKSSpsksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLING---RPLDK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 582 ESLRRHIGVVPQDTPLF-NDDIRHNIRYgrldasdadveaaaraakvdqiVQNLpqgyntkvgeRGlmISGGEKQRLAVA 660
Cdd:cd03213 78 RSFRKIIGYVPQDDILHpTLTVRETLMF----------------------AAKL----------RG--LSGGERKRVSIA 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2274528008 661 RLLLKNPSILFFDEATSALDSYTETELMRNINAnLLSEKRTAIFVAHRLRT--ISDSDLIVVLQSGQVAEKG 730
Cdd:cd03213 124 LELVSNPSLLFLDEPTSGLDSSSALQVMSLLRR-LADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
530-736 |
7.61e-29 |
|
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: 116.59 E-value: 7.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 530 NISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVS---LESLRRH-IGVVPQDTPLF-NDDIRH 604
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRKkISMVFQSFALLpHRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 605 NIRYGRLDASDADVEAAARAAKVDQIVqNLPQGYNTKVGErglmISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTE 684
Cdd:cd03294 122 NVAFGLEVQGVPRAEREERAAEALELV-GLEGWEHKYPDE----LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIR 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2274528008 685 TElMRNINANLLSE-KRTAIFVAHRL-RTISDSDLIVVLQSGQVAEKGTHAELM 736
Cdd:cd03294 197 RE-MQDELLRLQAElQKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
512-714 |
1.06e-28 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 115.52 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYK--PQ---SGKIYIDGQDI--TKVSLESL 584
Cdd:COG1117 12 IEVRNLNVYYG-DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGarvEGEILLDGEDIydPDVDVVEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 585 RRHIGVVPQdTP-LFNDDIRHNIRYG-RL--DASDADveaaaraakVDQIVQN-LpqgynTKVG----------ERGLMI 649
Cdd:COG1117 91 RRRVGMVFQ-KPnPFPKSIYDNVAYGlRLhgIKSKSE---------LDEIVEEsL-----RKAAlwdevkdrlkKSALGL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2274528008 650 SGGEKQRLAVARLLLKNPSILFFDEATSALDSyTET----ELMRNinanlLSEKRTAIFVAHRL---RTISD 714
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDP-ISTakieELILE-----LKKDYTIVIVTHNMqqaARVSD 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
512-726 |
1.91e-28 |
|
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: 113.39 E-value: 1.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVT--FGyhpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDIT--KVSLESLRRH 587
Cdd:cd03262 1 IEIKNLHksFG---DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 588 IGVVPQDTPLF-NDDIRHNIRYG-----RLDASDADVEAAARAAKVdqivqnlpqGYNTKVGERGLMISGGEKQRLAVAR 661
Cdd:cd03262 78 VGMVFQQFNLFpHLTVLENITLApikvkGMSKAEAEERALELLEKV---------GLADKADAYPAQLSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2274528008 662 LLLKNPSILFFDEATSALDSYTETE---LMRninaNLLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQV 726
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPELVGEvldVMK----DLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
530-730 |
2.29e-28 |
|
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: 113.16 E-value: 2.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 530 NISFAVPAGYkTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDI----TKVSLESLRRHIGVVPQDTPLF-NDDIRH 604
Cdd:cd03297 16 KIDFDLNEEV-TGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQYALFpHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 605 NIRYG---RLDASDAD-VEAAARAAKVDQIVQNLPQGyntkvgerglmISGGEKQRLAVARLLLKNPSILFFDEATSALD 680
Cdd:cd03297 95 NLAFGlkrKRNREDRIsVDELLDLLGLDHLLNRYPAQ-----------LSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2274528008 681 SYTETEL---MRNINANLlseKRTAIFVAHRLRTI-SDSDLIVVLQSGQVAEKG 730
Cdd:cd03297 164 RALRLQLlpeLKQIKKNL---NIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
512-739 |
2.42e-28 |
|
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: 114.20 E-value: 2.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVS---LESLRRHI 588
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 589 GVVPQDTPLFND-DIRHNIRYGRLDA-----------SDADVEAAARAakVDQIvqNLPQGYNTKVGErglmISGGEKQR 656
Cdd:cd03256 81 GMIFQQFNLIERlSVLENVLSGRLGRrstwrslfglfPKEEKQRALAA--LERV--GLLDKAYQRADQ----LSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 657 LAVARLLLKNPSILFFDEATSALDSYTETELMRNINANLLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQVAEKGTHAEL 735
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAEL 232
|
....
gi 2274528008 736 MDRK 739
Cdd:cd03256 233 TDEV 236
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
512-735 |
3.26e-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: 112.98 E-value: 3.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYH-PDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKvSLESLRRHIGV 590
Cdd:cd03263 1 LQIRNLTKTYKkGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 591 VPQDTPLFND-DIRHNIR-YGRL---DASDADVEAAARAAKVdqivqNLPQGYNTKVGErglmISGGEKQRLAVARLLLK 665
Cdd:cd03263 80 CPQFDALFDElTVREHLRfYARLkglPKSEIKEEVELLLRVL-----GLTDKANKRART----LSGGMKRKLSLAIALIG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2274528008 666 NPSILFFDEATSALDSYTETELMRNINAnlLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQVAEKGTHAEL 735
Cdd:cd03263 151 GPSVLLLDEPTSGLDPASRRAIWDLILE--VRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
512-730 |
3.83e-28 |
|
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: 112.67 E-value: 3.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYhPDRPIFSNISFAVPAGYkTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKvSLESLRRHIGVV 591
Cdd:cd03264 1 LQLENLTKRY-GKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 592 PQDtPLFNDDIR------HNIRYGRLDASDADVEAAARAAKVdqivqNLPQGYNTKVGErglmISGGEKQRLAVARLLLK 665
Cdd:cd03264 78 PQE-FGVYPNFTvrefldYIAWLKGIPSKEVKARVDEVLELV-----NLGDRAKKKIGS----LSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2274528008 666 NPSILFFDEATSALDSyTETELMRNINANlLSEKRTAIFVAHRLRTISDS-DLIVVLQSGQVAEKG 730
Cdd:cd03264 148 DPSILIVDEPTAGLDP-EERIRFRNLLSE-LGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
512-738 |
4.27e-28 |
|
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: 113.10 E-value: 4.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKvsLESLRRHIGVV 591
Cdd:cd03300 1 IELENVSKFYG-GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN--LPPHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 592 PQDTPLFND-DIRHNIRYG-RLDASDADVEAAARAAKVDQIvqNLPQGYNTKVGErglmISGGEKQRLAVARLLLKNPSI 669
Cdd:cd03300 78 FQNYALFPHlTVFENIAFGlRLKKLPKAEIKERVAEALDLV--QLEGYANRKPSQ----LSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2274528008 670 LFFDEATSALD----SYTETELMRnINANLLSekrTAIFVAH-RLRTISDSDLIVVLQSGQVAEKGTHAELMDR 738
Cdd:cd03300 152 LLLDEPLGALDlklrKDMQLELKR-LQKELGI---TFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
515-737 |
5.56e-28 |
|
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: 112.53 E-value: 5.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 515 ENVTFGYhPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLES-LRRHIGVVPQ 593
Cdd:cd03224 4 ENLNAGY-GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 594 DTPLFND-DIRHNIRYGRLDASDADVEAAaraakVDQIVQNLPqgyntKVGER-----GLMiSGGEKQRLAVARLLLKNP 667
Cdd:cd03224 83 GRRIFPElTVEENLLLGAYARRRAKRKAR-----LERVYELFP-----RLKERrkqlaGTL-SGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2274528008 668 SILFFDEATSALDSYTETELMRNINAnlLSEKRTAIFV----AHRLRTISDSdlIVVLQSGQVAEKGTHAELMD 737
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRE--LRDEGVTILLveqnARFALEIADR--AYVLERGRVVLEGTAAELLA 221
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
512-738 |
7.69e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 113.67 E-value: 7.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPD--RPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIG 589
Cdd:PRK13650 5 IEVKNLTFKYKEDqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 590 VVPQ--DTPLFNDDIRHNIRYGrldASDADVEAAARAAKVDQIVQNLP-QGYNTKVGERglmISGGEKQRLAVARLLLKN 666
Cdd:PRK13650 85 MVFQnpDNQFVGATVEDDVAFG---LENKGIPHEEMKERVNEALELVGmQDFKEREPAR---LSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2274528008 667 PSILFFDEATSALDSYTETELMRNINANLLSEKRTAIFVAHRLRTISDSDLIVVLQSGQVAEKGTHAELMDR 738
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
512-734 |
1.13e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 113.60 E-value: 1.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPDRPI----FSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDIT--KVSLESLR 585
Cdd:PRK13637 3 IKIENLTHIYMEGTPFekkaLDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 586 RHIGVVPQ--DTPLFNDDIRHNIRYG--RLDASDADVEaaaraAKVDQIVQNLPQGYNTKVGERGLMISGGEKQRLAVAR 661
Cdd:PRK13637 83 KKVGLVFQypEYQLFEETIEKDIAFGpiNLGLSEEEIE-----NRVKRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2274528008 662 LLLKNPSILFFDEATSALDSYTETELMRNINANLLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQVAEKGTHAE 734
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
512-712 |
1.94e-27 |
|
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: 110.58 E-value: 1.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKV---SLESLRRHI 588
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 589 GVVPQDTPLFND-DIRHNIRYGrLDASdaDVEAAARAAKVDQIVQNLpqGYNTKVGERGLMISGGEKQRLAVARLLLKNP 667
Cdd:cd03292 81 GVVFQDFRLLPDrNVYENVAFA-LEVT--GVPPREIRKRVPAALELV--GLSHKHRALPAELSGGEQQRVAIARAIVNSP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2274528008 668 SILFFDEATSALDSYTETELMR---NINAN----LLSEKRTAIFVAHRLRTI 712
Cdd:cd03292 156 TILIADEPTGNLDPDTTWEIMNllkKINKAgttvVVATHAKELVDTTRHRVI 207
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
419-708 |
3.09e-27 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 117.22 E-value: 3.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 419 LNSGQNAIFSTSLTVMMLLAAQGVTNGTMSVGDLVMVNQLVFQLSLPLNFLGTVYRELRQ--SLVDMETMFNLENVNVAV 496
Cdd:COG4178 268 LTFFTTGYGQLAVIFPILVAAPRYFAGEITLGGLMQAASAFGQVQGALSWFVDNYQSLAEwrATVDRLAGFEEALEAADA 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 497 KENADAPPLKVTGGEIRFENVTFgYHPD-RPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYI-DGQ 574
Cdd:COG4178 348 LPEAASRIETSEDGALALEDLTL-RTPDgRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGA 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 575 DITkvsleslrrhigVVPQDTPLFNDDIRHNIRY--GRLDASDADVEAAARAAKVDQIVQNLPQGYNTkvgERGLmiSGG 652
Cdd:COG4178 427 RVL------------FLPQRPYLPLGTLREALLYpaTAEAFSDAELREALEAVGLGHLAERLDEEADW---DQVL--SLG 489
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2274528008 653 EKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNINANLlsEKRTAIFVAHR 708
Cdd:COG4178 490 EQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREEL--PGTTVISVGHR 543
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
505-724 |
4.00e-27 |
|
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: 110.11 E-value: 4.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 505 LKVTGGeirfenvTFGYHPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESL 584
Cdd:cd03290 1 VQVTNG-------YFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEAT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 585 ----RRHIGVVPQDTPLFNDDIRHNIRYG---RLDASDADVEAAARAAKVDQivqnLPQGYNTKVGERGLMISGGEKQRL 657
Cdd:cd03290 74 rsrnRYSVAYAAQKPWLLNATVEENITFGspfNKQRYKAVTDACSLQPDIDL----LPFGDQTEIGERGINLSGGQRQRI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2274528008 658 AVARLLLKNPSILFFDEATSALDSYTETELMR-NINANLLSEKRTAIFVAHRLRTISDSDLIVVLQSG 724
Cdd:cd03290 150 CVARALYQNTNIVFLDDPFSALDIHLSDHLMQeGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
511-737 |
6.65e-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: 109.74 E-value: 6.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 511 EIRFENVTFGYhPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLEslRRHIGV 590
Cdd:cd03296 2 SIEVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 591 VPQDTPLFND-DIRHNIRYG-RLDASDADVEAAARAAKVDQIVQ-----NLPQGYNTKvgerglmISGGEKQRLAVARLL 663
Cdd:cd03296 79 VFQHYALFRHmTVFDNVAFGlRVKPRSERPPEAEIRAKVHELLKlvqldWLADRYPAQ-------LSGGQRQRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2274528008 664 LKNPSILFFDEATSALDSYTETEL---MRNINANLlseKRTAIFVAH-RLRTISDSDLIVVLQSGQVAEKGTHAELMD 737
Cdd:cd03296 152 AVEPKVLLLDEPFGALDAKVRKELrrwLRRLHDEL---HVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
512-741 |
8.81e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 110.66 E-value: 8.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGVV 591
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 592 PQ--DTPLFNDDIRHNIRYGRLDASdadVEAAARAAKVDQIVQNLP-QGYNTKVGERglmISGGEKQRLAVARLLLKNPS 668
Cdd:PRK13652 84 FQnpDDQIFSPTVEQDIAFGPINLG---LDEETVAHRVSSALHMLGlEELRDRVPHH---LSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2274528008 669 ILFFDEATSALDSYTETELMRNINANLLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQVAEKGTHAELMDRKGL 741
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQPDL 231
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
512-735 |
9.60e-27 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 112.09 E-value: 9.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENV--TFGyHPDRPI--FSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVS---LESL 584
Cdd:COG1135 2 IELENLskTFP-TKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSereLRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 585 RRHIGVVPQDTPLFND-DIRHNIRYG-RLdasdADVEAAARAAKVDQIVQnlpqgyntKVG--ERG------LmiSGGEK 654
Cdd:COG1135 81 RRKIGMIFQHFNLLSSrTVAENVALPlEI----AGVPKAEIRKRVAELLE--------LVGlsDKAdaypsqL--SGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 655 QRLAVARLLLKNPSILFFDEATSALDSytET-----ELMRNINANL-LsekrTAIFVAHRL---RTISDSdlIVVLQSGQ 725
Cdd:COG1135 147 QRVGIARALANNPKVLLCDEATSALDP--ETtrsilDLLKDINRELgL----TIVLITHEMdvvRRICDR--VAVLENGR 218
|
250
....*....|
gi 2274528008 726 VAEKGTHAEL 735
Cdd:COG1135 219 IVEQGPVLDV 228
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
510-738 |
1.19e-26 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 112.09 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 510 GEIRFENVTFGYHpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLEslRRHIG 589
Cdd:COG3839 2 ASLELENVSKSYG-GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 590 VVPQDTPLF-NDDIRHNIRYG----RLDASDADveaaaraAKVDQIVQ--NLPQGYNTKVGErglmISGGEKQRLAVARL 662
Cdd:COG3839 79 MVFQSYALYpHMTVYENIAFPlklrKVPKAEID-------RRVREAAEllGLEDLLDRKPKQ----LSGGQRQRVALGRA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 663 LLKNPSILFFDEATSALD----SYTETELMRnINANLlseKRTAIFVAHrlrtisD-------SDLIVVLQSGQVAEKGT 731
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDaklrVEMRAEIKR-LHRRL---GTTTIYVTH------DqveamtlADRIAVMNDGRIQQVGT 217
|
....*..
gi 2274528008 732 HAELMDR 738
Cdd:COG3839 218 PEELYDR 224
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
502-756 |
1.58e-26 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 116.80 E-value: 1.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 502 APPLKVTGGEIRFENVTFGYHPDRP-IFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVS 580
Cdd:PTZ00243 1299 AAPHPVQAGSLVFEGVQMRYREGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYG 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 581 LESLRRHIGVVPQDTPLFNDDIRHNIRyGRLDASDADVEAAARAAKVDQIVQNLPQGYNTKVGERGLMISGGEKQRLAVA 660
Cdd:PTZ00243 1379 LRELRRQFSMIPQDPVLFDGTVRQNVD-PFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMA 1457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 661 RLLLKNPS-ILFFDEATSALDSytetELMRNINANLLS--EKRTAIFVAHRLRTISDSDLIVVLQSGQVAEKGTHAEL-M 736
Cdd:PTZ00243 1458 RALLKKGSgFILMDEATANIDP----ALDRQIQATVMSafSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvM 1533
|
250 260
....*....|....*....|
gi 2274528008 737 DRKGLYWDLWQAQSTLGVGH 756
Cdd:PTZ00243 1534 NRQSIFHSMVEALGRSEAKR 1553
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
516-735 |
2.50e-25 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 108.27 E-value: 2.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 516 NVT--FGyhpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLEslRRHIGVVPQ 593
Cdd:PRK11432 11 NITkrFG---SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 594 DTPLF-NDDIRHNIRYG-------------RLDASDADVEAAARAAK-VDQivqnlpqgyntkvgerglmISGGEKQRLA 658
Cdd:PRK11432 86 SYALFpHMSLGENVGYGlkmlgvpkeerkqRVKEALELVDLAGFEDRyVDQ-------------------ISGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 659 VARLLLKNPSILFFDEATSALD-----SYTET--ELMRNINAnllsekrTAIFVAH-RLRTISDSDLIVVLQSGQVAEKG 730
Cdd:PRK11432 147 LARALILKPKVLLFDEPLSNLDanlrrSMREKirELQQQFNI-------TSLYVTHdQSEAFAVSDTVIVMNKGKIMQIG 219
|
....*
gi 2274528008 731 THAEL 735
Cdd:PRK11432 220 SPQEL 224
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
530-738 |
2.91e-25 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 107.51 E-value: 2.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 530 NISFAVPAGyKT-AFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVS---LESLRRHIGVVPQDtPlfnddirhn 605
Cdd:COG4608 36 GVSFDIRRG-ETlGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQD-P--------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 606 irYGRLDASdadveaaaraAKVDQI------VQNL--PQGYNTKVGER----GL----------MISGGEKQRLAVARLL 663
Cdd:COG4608 105 --YASLNPR----------MTVGDIiaeplrIHGLasKAERRERVAELlelvGLrpehadryphEFSGGQRQRIGIARAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 664 LKNPSILFFDEATSALD-SytetelmrnINA---NLLSEKR-----TAIFVAHRL---RTISDSdlIVVLQSGQVAEKGT 731
Cdd:COG4608 173 ALNPKLIVCDEPVSALDvS---------IQAqvlNLLEDLQdelglTYLFISHDLsvvRHISDR--VAVMYLGKIVEIAP 241
|
....*..
gi 2274528008 732 HAELMDR 738
Cdd:COG4608 242 RDELYAR 248
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
524-723 |
3.61e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 104.41 E-value: 3.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 524 DRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGVVPQDTPLFNDDIR 603
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 604 HNIRYG---RLDASDADveaaaraAKVDQIVQ-NLPQGYNTK-VGErglmISGGEKQRLAVARLLLKNPSILFFDEATSA 678
Cdd:PRK10247 99 DNLIFPwqiRNQQPDPA-------IFLDDLERfALPDTILTKnIAE----LSGGEKQRISLIRNLQFMPKVLLLDEITSA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2274528008 679 LDSYTEtelmRNINA---NLLSEKRTAI-FVAHRLRTISDSDLIVVLQS 723
Cdd:PRK10247 168 LDESNK----HNVNEiihRYVREQNIAVlWVTHDKDEINHADKVITLQP 212
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
512-731 |
4.26e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 108.11 E-value: 4.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLEslRRHIGVV 591
Cdd:PRK09452 15 VELRGISKSFD-GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 592 PQDTPLF-NDDIRHNIRYG-RLDASDAD-----VEAAARAAKVDQIVQNLPQgyntkvgerglMISGGEKQRLAVARLLL 664
Cdd:PRK09452 92 FQSYALFpHMTVFENVAFGlRMQKTPAAeitprVMEALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2274528008 665 KNPSILFFDEATSALDsYTETELMRNinaNLLSEKR----TAIFVAH-RLRTISDSDLIVVLQSGQVAEKGT 731
Cdd:PRK09452 161 NKPKVLLLDESLSALD-YKLRKQMQN---ELKALQRklgiTFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
512-730 |
4.50e-25 |
|
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: 103.84 E-value: 4.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKvsLESLRRHIGVV 591
Cdd:cd03268 1 LKTNDLTKTYG-KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK--NIEALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 592 pQDTPLFNDDI--RHNIRYGR--LDASDADVEaaaraaKVDQIVqNLPQGYNTKVGERGLmisgGEKQRLAVARLLLKNP 667
Cdd:cd03268 78 -IEAPGFYPNLtaRENLRLLArlLGIRKKRID------EVLDVV-GLKDSAKKKVKGFSL----GMKQRLGIALALLGNP 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2274528008 668 SILFFDEATSALDSYTETElMRNINANLLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQVAEKG 730
Cdd:cd03268 146 DLLILDEPTNGLDPDGIKE-LRELILSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
512-738 |
6.13e-25 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 104.07 E-value: 6.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHpDRPIfsNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKvsLESLRRHIGVV 591
Cdd:COG3840 2 LRLDDLTYRYG-DFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA--LPPAERPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 592 PQDTPLFND-DIRHNIRYG-----RLDASDadveaaarAAKVDQIVQnlpqgyntKVGERGLM------ISGGEKQRLAV 659
Cdd:COG3840 77 FQENNLFPHlTVAQNIGLGlrpglKLTAEQ--------RAQVEQALE--------RVGLAGLLdrlpgqLSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 660 ARLLLKNPSILFFDEATSALDSYTETELMRNINANLLSEKRTAIFVAHRL---RTISDsDLIVVLQsGQVAEKGTHAELM 736
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPedaARIAD-RVLLVAD-GRIAADGPTAALL 218
|
..
gi 2274528008 737 DR 738
Cdd:COG3840 219 DG 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
512-727 |
1.36e-24 |
|
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: 100.58 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVT--FGyhpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVS-LESLRRHI 588
Cdd:cd03216 1 LELRGITkrFG---GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 589 GVVPQdtplfnddirhnirygrldasdadveaaaraakvdqivqnlpqgyntkvgerglmISGGEKQRLAVARLLLKNPS 668
Cdd:cd03216 78 AMVYQ-------------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 669 ILFFDEATSALDSyTETELMRNINANLLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQVA 727
Cdd:cd03216 103 LLILDEPTAALTP-AEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
525-736 |
1.70e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 103.31 E-value: 1.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 525 RPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGVVPQDTPL-FNDDIR 603
Cdd:PRK13548 15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 604 HNIRYGRLDASDADVEaaaraakvdqiVQNLPQGYNTKVGERGL------MISGGEKQRLAVARLLL------KNPSILF 671
Cdd:PRK13548 95 EVVAMGRAPHGLSRAE-----------DDALVAAALAQVDLAHLagrdypQLSGGEQQRVQLARVLAqlwepdGPPRWLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2274528008 672 FDEATSALDSYTETELMRnINANLLSEKRTA-IFVAHRLR-TISDSDLIVVLQSGQVAEKGTHAELM 736
Cdd:PRK13548 164 LDEPTSALDLAHQHHVLR-LARQLAHERGLAvIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVL 229
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
512-730 |
2.09e-24 |
|
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: 101.80 E-value: 2.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHpDRPIfsNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITkvSLESLRRHIGVV 591
Cdd:cd03298 1 VRLDKIRFSYG-EQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT--AAPPADRPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 592 PQDTPLFND-DIRHNIRYG-----RLDASDadveaaarAAKVDQIVQnlpqgyntKVGERGLM------ISGGEKQRLAV 659
Cdd:cd03298 76 FQENNLFAHlTVEQNVGLGlspglKLTAED--------RQAIEVALA--------RVGLAGLEkrlpgeLSGGERQRVAL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2274528008 660 ARLLLKNPSILFFDEATSALDSYTETELMRNINANLLSEKRTAIFVAHrlrTISDS----DLIVVLQSGQVAEKG 730
Cdd:cd03298 140 ARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTH---QPEDAkrlaQRVVFLDNGRIAAQG 211
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
519-736 |
2.88e-24 |
|
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: 102.96 E-value: 2.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 519 FGYHPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKV---SLESLRRHIGVVPQDT 595
Cdd:TIGR02769 18 FGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQRRAFRRDVQLVFQDS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 596 P-LFN--DDIRHNIR-----YGRLDASDADVEAAARAAKVD---QIVQNLPQgyntkvgerglMISGGEKQRLAVARLLL 664
Cdd:TIGR02769 98 PsAVNprMTVRQIIGeplrhLTSLDESEQKARIAELLDMVGlrsEDADKLPR-----------QLSGGQLQRINIARALA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2274528008 665 KNPSILFFDEATSALDSYTETELMRNINAnLLSEKRTA-IFVAHRLRTI-SDSDLIVVLQSGQVAEKGTHAELM 736
Cdd:TIGR02769 167 VKPKLIVLDEAVSNLDMVLQAVILELLRK-LQQAFGTAyLFITHDLRLVqSFCQRVAVMDKGQIVEECDVAQLL 239
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
512-720 |
3.90e-24 |
|
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: 101.02 E-value: 3.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKvSLESLRRHIGVV 591
Cdd:COG4133 3 LEAENLSCRRG-ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 592 PQDTPLFND-DIRHNIR-YGRLDASDADVEAaaraakVDQIVQ--NLPQGYNTKVGerglMISGGEKQRLAVARLLLKNP 667
Cdd:COG4133 81 GHADGLKPElTVRENLRfWAALYGLRADREA------IDEALEavGLAGLADLPVR----QLSAGQKRRVALARLLLSPA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2274528008 668 SILFFDEATSALDSYTETELMRNINAnLLSEKRTAIFVAHRLRTISDSDLIVV 720
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQPLELAAARVLDL 202
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
530-741 |
3.96e-24 |
|
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: 104.80 E-value: 3.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 530 NISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDG---QDITK-VSLESLRRHIGVVPQDTPLFND-DIRH 604
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARgIFLPPHRRRIGYVFQEARLFPHlSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 605 NIRYGRLDASDADveaaaRAAKVDQIVQNLpqgyntkvGERGLM------ISGGEKQRLAVARLLLKNPSILFFDEATSA 678
Cdd:COG4148 97 NLLYGRKRAPRAE-----RRISFDEVVELL--------GIGHLLdrrpatLSGGERQRVAIGRALLSSPRLLLMDEPLAA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2274528008 679 LDSYTETELMRNINAnlLSEkRTAI---FVAH------RLrtisdSDLIVVLQSGQVAEKGTHAELMDRKGL 741
Cdd:COG4148 164 LDLARKAEILPYLER--LRD-ELDIpilYVSHsldevaRL-----ADHVVLLEQGRVVASGPLAEVLSRPDL 227
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
531-738 |
4.57e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 103.89 E-value: 4.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 531 ISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLE---SLRRHIGVVPQDtPlfnddirhnir 607
Cdd:PRK11308 34 VSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEaqkLLRQKIQIVFQN-P----------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 608 YGRLDAsdadveaaarAAKVDQIVQNlPQGYNTKVG--ER-----------GL----------MISGGEKQRLAVARLLL 664
Cdd:PRK11308 102 YGSLNP----------RKKVGQILEE-PLLINTSLSaaERrekalammakvGLrpehydryphMFSGGQRQRIAIARALM 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2274528008 665 KNPSILFFDEATSALDSYTETELMrNINANLLSEKRTA-IFVAHRL---RTISDSDLIVVLqsGQVAEKGTHAELMDR 738
Cdd:PRK11308 171 LDPDVVVADEPVSALDVSVQAQVL-NLMMDLQQELGLSyVFISHDLsvvEHIADEVMVMYL--GRCVEKGTKEQIFNN 245
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
512-734 |
6.09e-24 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 103.73 E-value: 6.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYH-PDRPI--FSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVS---LESLR 585
Cdd:PRK11153 2 IELKNISKVFPqGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekeLRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 586 RHIGVVPQDtplFN--------DDIRHNIRYGRLDASDADveaaaraAKVDQIVQnlpqgyntKVGERGLM------ISG 651
Cdd:PRK11153 82 RQIGMIFQH---FNllssrtvfDNVALPLELAGTPKAEIK-------ARVTELLE--------LVGLSDKAdrypaqLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 652 GEKQRLAVARLLLKNPSILFFDEATSALDSYTET---ELMRNINANLlseKRTAIFVAHRL---RTISDSdlIVVLQSGQ 725
Cdd:PRK11153 144 GQKQRVAIARALASNPKVLLCDEATSALDPATTRsilELLKDINREL---GLTIVLITHEMdvvKRICDR--VAVIDAGR 218
|
....*....
gi 2274528008 726 VAEKGTHAE 734
Cdd:PRK11153 219 LVEQGTVSE 227
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
512-741 |
8.93e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 102.02 E-value: 8.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYhPD--RPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIG 589
Cdd:PRK13635 6 IRVEHISFRY-PDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 590 VVPQ--DTPLFNDDIRHNIRYGrldASDADVEAAARAAKVDQIVQnlpqgyntKVGERGLM------ISGGEKQRLAVAR 661
Cdd:PRK13635 85 MVFQnpDNQFVGATVQDDVAFG---LENIGVPREEMVERVDQALR--------QVGMEDFLnrephrLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 662 LLLKNPSILFFDEATSALDSYTETELMRNINaNLLSEKR-TAIFVAHRLRTISDSDLIVVLQSGQVAEKGT------HAE 734
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVR-QLKEQKGiTVLSITHDLDEAAQADRVIVMNKGEILEEGTpeeifkSGH 232
|
....*..
gi 2274528008 735 LMDRKGL 741
Cdd:PRK13635 233 MLQEIGL 239
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
500-736 |
1.53e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 107.13 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 500 ADAPPLKVTGGEIRFENVTFGYHP--DRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIdgqdit 577
Cdd:PLN03130 603 LPNPPLEPGLPAISIKNGYFSWDSkaERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------ 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 578 kvslesLRRHIGVVPQDTPLFNDDIRHNIRYGrLDASDADVEAAARAAKVDQIVQNLPQGYNTKVGERGLMISGGEKQRL 657
Cdd:PLN03130 677 ------IRGTVAYVPQVSWIFNATVRDNILFG-SPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRV 749
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2274528008 658 AVARLLLKNPSILFFDEATSALDSYTETELMRNINANLLSEKrTAIFVAHRLRTISDSDLIVVLQSGQVAEKGTHAELM 736
Cdd:PLN03130 750 SMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGK-TRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELS 827
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
529-736 |
1.58e-23 |
|
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: 99.82 E-value: 1.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 529 SNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSlESLRRHIGVVP--QDTPLFND-DIRHN 605
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLP-PHEIARLGIGRtfQIPRLFPElTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 606 IRYGRLDASDADVEAAARAAKVDQIVQ---------NLPQGYNTKVGErglmISGGEKQRLAVARLLLKNPSILFFDEAT 676
Cdd:cd03219 96 VMVAAQARTGSGLLLARARREEREAREraeellervGLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDEPA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2274528008 677 SALDSyTETELMRNINANLLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQVAEKGTHAELM 736
Cdd:cd03219 172 AGLNP-EETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVR 231
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
530-738 |
2.13e-23 |
|
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: 101.67 E-value: 2.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 530 NISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQ---SGKIYIDGQDITKVSLESLR----RHIGVVPQDtPL--FN- 599
Cdd:COG0444 23 GVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELRkirgREIQMIFQD-PMtsLNp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 600 -----DDIRHNIRY-GRLDASDADveaaaraakvDQIVQNLpqgynTKVG----ERGL-----MISGGEKQRLAVARLLL 664
Cdd:COG0444 102 vmtvgDQIAEPLRIhGGLSKAEAR----------ERAIELL-----ERVGlpdpERRLdryphELSGGMRQRVMIARALA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 665 KNPSILFFDEATSALDSyteT------ELMRNINAnllsEKRTA-IFVAHRLRTISD-SDLIVVLQSGQVAEKGTHAELM 736
Cdd:COG0444 167 LEPKLLIADEPTTALDV---TiqaqilNLLKDLQR----ELGLAiLFITHDLGVVAEiADRVAVMYAGRIVEEGPVEELF 239
|
..
gi 2274528008 737 DR 738
Cdd:COG0444 240 EN 241
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
512-728 |
1.61e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.07 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYhPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIdGQDItkvsleslrrHIGVV 591
Cdd:COG0488 316 LELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 592 PQDTPLFNDD--IRHNIRYGRLDASDADVEaaaraakvdqivqnlpqGY-----------NTKVGErglmISGGEKQRLA 658
Cdd:COG0488 384 DQHQEELDPDktVLDELRDGAPGGTEQEVR-----------------GYlgrflfsgddaFKPVGV----LSGGEKARLA 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2274528008 659 VARLLLKNPSILFFDEATSALDsyTETelmRNINANLLSE-KRTAIFVAH-R--LRTISDSdlIVVLQSGQVAE 728
Cdd:COG0488 443 LAKLLLSPPNVLLLDEPTNHLD--IET---LEALEEALDDfPGTVLLVSHdRyfLDRVATR--ILEFEDGGVRE 509
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
527-731 |
1.77e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 99.77 E-value: 1.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 527 IFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESlrRHIGVVPQDTPLFnddiRH-- 604
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYALF----RHmt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 605 ---NIRYG-----RLDASDADVeaaaRAAKVDQ---IVQ--NLPQGYNTKvgerglmISGGEKQRLAVARLLLKNPSILF 671
Cdd:PRK10851 91 vfdNIAFGltvlpRRERPNAAA----IKAKVTQlleMVQlaHLADRYPAQ-------LSGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2274528008 672 FDEATSALDSYTETELMRNINaNLLSE-KRTAIFVAH-RLRTISDSDLIVVLQSGQVAEKGT 731
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLR-QLHEElKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
512-735 |
2.30e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 97.86 E-value: 2.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPDRPI--FSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIG 589
Cdd:PRK13642 5 LEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 590 VVPQ--DTPLFNDDIRHNIRYGrldASDADVEAAARAAKVDQIVQNLPQ-GYNTKVGERglmISGGEKQRLAVARLLLKN 666
Cdd:PRK13642 85 MVFQnpDNQFVGATVEDDVAFG---MENQGIPREEMIKRVDEALLAVNMlDFKTREPAR---LSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2274528008 667 PSILFFDEATSALDSYTETELMRNINANLLSEKRTAIFVAHRLRTISDSDLIVVLQSGQVAEKGTHAEL 735
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
417-745 |
2.53e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 103.13 E-value: 2.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 417 AALNSGQNAIFSTSLTVMMLLAAQGVTngTMSVGDLVMVNQL----VFQ-LSLPLNFLGTVYRELRQ---SLVDMETMFN 488
Cdd:PLN03232 519 AQLLSAFNSFILNSIPVVVTLVSFGVF--VLLGGDLTPARAFtslsLFAvLRSPLNMLPNLLSQVVNanvSLQRIEELLL 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 489 LENvnvavKENADAPPLKVTGGEIRFENVTFGY--HPDRPIFSNISFAVPAGYKTAFVGPSGCGK-STIFRLLFRFYKPQ 565
Cdd:PLN03232 597 SEE-----RILAQNPPLQPGAPAISIKNGYFSWdsKTSKPTLSDINLEIPVGSLVAIVGGTGEGKtSLISAMLGELSHAE 671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 566 SGKIYIDGQditkvsleslrrhIGVVPQDTPLFNDDIRHNIRYGrldaSDADVEAAARAAKVDQIVQNL---PQGYNTKV 642
Cdd:PLN03232 672 TSSVVIRGS-------------VAYVPQVSWIFNATVRENILFG----SDFESERYWRAIDVTALQHDLdllPGRDLTEI 734
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 643 GERGLMISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNINANLLSEKrTAIFVAHRLRTISDSDLIVVLQ 722
Cdd:PLN03232 735 GERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGK-TRVLVTNQLHFLPLMDRIILVS 813
|
330 340
....*....|....*....|...
gi 2274528008 723 SGQVAEKGTHAELMDRKGLYWDL 745
Cdd:PLN03232 814 EGMIKEEGTFAELSKSGSLFKKL 836
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
512-731 |
4.61e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 96.98 E-value: 4.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVS-LESLRRHIGV 590
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 591 VPQ--DTPLFNDDIRHNIRYGRLDASDADVEaaaRAAKVDQIVQNLPQGYNTKVGERGLmiSGGEKQRLAVARLLLKNPS 668
Cdd:PRK13644 82 VFQnpETQFVGRTVEEDLAFGPENLCLPPIE---IRKRVDRALAEIGLEKYRHRSPKTL--SGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2274528008 669 ILFFDEATSALDSYTETELMRNINAnlLSEK-RTAIFVAHRLRTISDSDLIVVLQSGQVAEKGT 731
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKK--LHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
512-731 |
5.41e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 96.26 E-value: 5.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPDRpIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQS-----GKIYIDGQDI--TKVSLESL 584
Cdd:PRK14258 8 IKVNNLSFYYDTQK-ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 585 RRHIGVVPQDTPLFNDDIRHNIRYG-RLDASDADVEaaaraakVDQIVQN------LPQGYNTKVGERGLMISGGEKQRL 657
Cdd:PRK14258 87 RRQVSMVHPKPNLFPMSVYDNVAYGvKIVGWRPKLE-------IDDIVESalkdadLWDEIKHKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 658 AVARLLLKNPSILFFDEATSALDSYTETELMRNINANLLSEKRTAIFVAHRLRTISD-SDLIVVLQS-----GQVAEKGT 731
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLVEFGL 239
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
511-710 |
7.13e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 96.00 E-value: 7.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 511 EIRFENVTFgYHPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRF------YKPQsGKIYIDGQDI--TKVSLE 582
Cdd:PRK14243 10 VLRTENLNV-YYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndlipgFRVE-GKVTFHGKNLyaPDVDPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 583 SLRRHIGVVPQDTPLFNDDIRHNIRYG-RLDASDADveaaaraakVDQIVQ-NLPQG-----YNTKVGERGLMISGGEKQ 655
Cdd:PRK14243 88 EVRRRIGMVFQKPNPFPKSIYDNIAYGaRINGYKGD---------MDELVErSLRQAalwdeVKDKLKQSGLSLSGGQQQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2274528008 656 RLAVARLLLKNPSILFFDEATSALDSYTE---TELMRNinanlLSEKRTAIFVAHRLR 710
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPISTlriEELMHE-----LKEQYTIIIVTHNMQ 211
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
511-738 |
1.34e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 94.98 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 511 EIRFENVTFGyhpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFR----FYKPQ-SGKIYIDGQDITKVSLESLR 585
Cdd:PRK14247 5 EIRDLKVSFG---QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielYPEARvSGEVYLDGQDIFKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 586 RHIGVVPQ-DTPLFNDDIRHNIRYG----RLDASDADVEAaaraaKVDQIVQ--NLPQGYNTKVGERGLMISGGEKQRLA 658
Cdd:PRK14247 82 RRVQMVFQiPNPIPNLSIFENVALGlklnRLVKSKKELQE-----RVRWALEkaQLWDEVKDRLDAPAGKLSGGQQQRLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 659 VARLLLKNPSILFFDEATSALDSytetELMRNINANLLSEKR--TAIFVAHRLRTISD-SDLIVVLQSGQVAEKGTHAEL 735
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDP----ENTAKIESLFLELKKdmTIVLVTHFPQQAARiSDYVAFLYKGQIVEWGPTREV 232
|
...
gi 2274528008 736 MDR 738
Cdd:PRK14247 233 FTN 235
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
512-730 |
1.81e-21 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 93.59 E-value: 1.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPDRPIF---SNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRhI 588
Cdd:cd03266 2 ITADALTKRFRDVKKTVqavDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR-L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 589 GVVPQDTPLFND-DIRHNIRY-GRLDAsdadVEAAARAAKVDQIVQNLpqGYNTKVGERGLMISGGEKQRLAVARLLLKN 666
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYfAGLYG----LKGDELTARLEELADRL--GMEELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2274528008 667 PSILFFDEATSALDsYTETELMRNINANLLSEKRTAIFVAHRLRTI-SDSDLIVVLQSGQVAEKG 730
Cdd:cd03266 155 PPVLLLDEPTTGLD-VMATRALREFIRQLRALGKCILFSTHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
530-735 |
2.02e-21 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 93.59 E-value: 2.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 530 NISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLEsLRRHIGVVPQDTPLfnDDI---RHNI 606
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE-VRRRIGIVFQDLSV--DDEltgWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 607 R-YGRLdasdADVEAAARAAKVDQIVQ--NLPQGYNTKVGErglmISGGEKQRLAVARLLLKNPSILFFDEATSALDSYT 683
Cdd:cd03265 95 YiHARL----YGVPGAERRERIDELLDfvGLLEAADRLVKT----YSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2274528008 684 ETELMRNINANLLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQVAEKGTHAEL 735
Cdd:cd03265 167 RAHVWEYIEKLKEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
532-737 |
4.24e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 96.26 E-value: 4.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 532 SFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLR----RHIGVVPQDTPLF-NDDIRHNI 606
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMpHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 607 RYG-RLDASDADVEAAARAAKVDQI-VQNLPQGYNTKvgerglmISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTE 684
Cdd:PRK10070 128 AFGmELAGINAEERREKALDALRQVgLENYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2274528008 685 TELMRNINANLLSEKRTAIFVAHRL-RTISDSDLIVVLQSGQVAEKGTHAELMD 737
Cdd:PRK10070 201 TEMQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
502-736 |
4.44e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.45 E-value: 4.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 502 APPLKVTGgeirfENVTFGyhpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSL 581
Cdd:PRK09536 1 MPMIDVSD-----LSVEFG---DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 582 ESLRRHIGVVPQDTPL-FNDDIRHNIRYGRL----------DASDADVEAAARAAKVDQIVQnlpQGYNTkvgerglmIS 650
Cdd:PRK09536 73 RAASRRVASVPQDTSLsFEFDVRQVVEMGRTphrsrfdtwtETDRAAVERAMERTGVAQFAD---RPVTS--------LS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 651 GGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNInANLLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQVAEK 729
Cdd:PRK09536 142 GGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELV-RRLVDDGKTAVAAIHDLDLAARyCDELVLLADGRVRAA 220
|
....*..
gi 2274528008 730 GTHAELM 736
Cdd:PRK09536 221 GPPADVL 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
514-680 |
4.94e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.44 E-value: 4.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 514 FENVTFGYhPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQditkvslesLRrhIGVVPQ 593
Cdd:COG0488 1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG---------LR--IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 594 DTPLFNDD-IRHNI------------RYGRLDASDADVEAAARAA-----------------KVDQIVQNL---PQGYNT 640
Cdd:COG0488 69 EPPLDDDLtVLDTVldgdaelraleaELEELEAKLAEPDEDLERLaelqeefealggweaeaRAEEILSGLgfpEEDLDR 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2274528008 641 KVGErglmISGGEKQRLAVARLLLKNPSILFFDEATSALD 680
Cdd:COG0488 149 PVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
512-708 |
5.91e-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: 90.29 E-value: 5.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGqditkvsleslRRHIGVV 591
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 592 PQdTPLFNDdirhniryGRLDasdadveaaaraakvDQIV----QNLpqgyntkvgerglmiSGGEKQRLAVARLLLKNP 667
Cdd:cd03223 70 PQ-RPYLPL--------GTLR---------------EQLIypwdDVL---------------SGGEQQRLAFARLLLHKP 110
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2274528008 668 SILFFDEATSALDSYTETELMRninanLLSEKRTA-IFVAHR 708
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQ-----LLKELGITvISVGHR 147
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
512-737 |
6.36e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 92.34 E-value: 6.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYH--PDRpifsnISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLEslRRHIG 589
Cdd:PRK10771 2 LKLTDITWLYHhlPMR-----FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 590 VVPQDTPLFND-DIRHNIRYG-----RLDASDADveaaaraaKVDQIVQnlpqgyntKVGERGLM------ISGGEKQRL 657
Cdd:PRK10771 75 MLFQENNLFSHlTVAQNIGLGlnpglKLNAAQRE--------KLHAIAR--------QMGIEDLLarlpgqLSGGQRQRV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 658 AVARLLLKNPSILFFDEATSALDSYTETELMrninaNLLSE-----KRTAIFVAHRLR---TISDSDLIVVlqSGQVAEK 729
Cdd:PRK10771 139 ALARCLVREQPILLLDEPFSALDPALRQEML-----TLVSQvcqerQLTLLMVSHSLEdaaRIAPRSLVVA--DGRIAWD 211
|
....*...
gi 2274528008 730 GTHAELMD 737
Cdd:PRK10771 212 GPTDELLS 219
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
512-726 |
7.56e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 93.74 E-value: 7.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPDRPI----FSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDIT----KVSLES 583
Cdd:PRK13641 3 IKFENVDYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 584 LRRHIGVVPQ--DTPLFNDDIRHNIRYGRLDASDADVEAAARAAKVDQIVqnlpqGYNTKVGERG-LMISGGEKQRLAVA 660
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKV-----GLSEDLISKSpFELSGGQMRRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2274528008 661 RLLLKNPSILFFDEATSALDSYTETELMRnINANLLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQV 726
Cdd:PRK13641 158 GVMAYEPEILCLDEPAAGLDPEGRKEMMQ-LFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKL 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
530-738 |
1.60e-20 |
|
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: 95.91 E-value: 1.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 530 NISFAVPAGYKTAFVGPSGCGKST----IFRLLfrfykPQSGKIYIDGQDITKVS---LESLRRHIGVVPQD-----TPl 597
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDpfgslSP- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 598 fnddiRHNI--------RYGRLDASDADVEaaaraakvDQIVQNLpqgynTKVG-ERGLM------ISGGEKQRLAVARL 662
Cdd:COG4172 378 -----RMTVgqiiaeglRVHGPGLSAAERR--------ARVAEAL-----EEVGlDPAARhrypheFSGGQRQRIAIARA 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 663 LLKNPSILFFDEATSALDsytetelmRNINA---NLLSE--KR---TAIFVAHRL---RTISDSdlIVVLQSGQVAEKGT 731
Cdd:COG4172 440 LILEPKLLVLDEPTSALD--------VSVQAqilDLLRDlqREhglAYLFISHDLavvRALAHR--VMVMKDGKVVEQGP 509
|
....*..
gi 2274528008 732 HAELMDR 738
Cdd:COG4172 510 TEQVFDA 516
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
512-735 |
1.93e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 92.49 E-value: 1.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPDRPIFS----NISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVS----LES 583
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASralfDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 584 LRRHIGVVPQ--DTPLFNDDIRHNIRYGRLDASDADVEAAARAAKVDQIVqnlpqGYNTKVGERG-LMISGGEKQRLAVA 660
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMV-----GLADEFWEKSpFELSGGQMRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2274528008 661 RLLLKNPSILFFDEATSALDSYTETELMRnINANLLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQVAEKGTHAEL 735
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKARIEMMQ-LFESIHQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDV 231
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
512-707 |
2.26e-20 |
|
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: 87.89 E-value: 2.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIyIDGQDITkvsleslrrhIGVV 591
Cdd:cd03221 1 IELENLSKTYG-GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV-TWGSTVK----------IGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 592 PQdtplfnddirhnirygrldasdadveaaaraakvdqivqnlpqgyntkvgerglmISGGEKQRLAVARLLLKNPSILF 671
Cdd:cd03221 69 EQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190
....*....|....*....|....*....|....*.
gi 2274528008 672 FDEATSALDSYTETELmrnINAnLLSEKRTAIFVAH 707
Cdd:cd03221 94 LDEPTNHLDLESIEAL---EEA-LKEYPGTVILVSH 125
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
474-739 |
2.36e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 93.36 E-value: 2.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 474 RELRQSLVDMETMFNLENVNVAVKENADAPPLKVTGGEIRFENVTFGYHpDRPIFSNISFAVPAGYKTAFVGPSGCGKST 553
Cdd:PRK13536 4 RAVAEEAPRRLELSPIERKHQGISEAKASIPGSMSTVAIDLAGVSKSYG-DKAVVNGLSFTVASGECFGLLGPNGAGKST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 554 IFRLLFRFYKPQSGKIYIDGQDITKVSlESLRRHIGVVPQ-DTPLFNDDIRHNI----RYGRLDASDAD------VEAAA 622
Cdd:PRK13536 83 IARMILGMTSPDAGKITVLGVPVPARA-RLARARIGVVPQfDNLDLEFTVRENLlvfgRYFGMSTREIEavipslLEFAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 623 RAAKVDQIVQNLpqgyntkvgerglmiSGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNINAnLLSEKRTA 702
Cdd:PRK13536 162 LESKADARVSDL---------------SGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRS-LLARGKTI 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2274528008 703 IFVAH------RLrtisdSDLIVVLQSG-QVAEKGTHAeLMDRK 739
Cdd:PRK13536 226 LLTTHfmeeaeRL-----CDRLCVLEAGrKIAEGRPHA-LIDEH 263
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
513-680 |
2.37e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 90.23 E-value: 2.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 513 RFENVTFGYHpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQ---SGKIYIDGQDITKVSLEslRRHIG 589
Cdd:COG4136 3 SLENLTITLG-GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAE--QRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 590 VVPQDTPLF-NDDIRHNIRYGrLDASdadveaAARAAKVDQIVQNLpqgynTKVGERGL------MISGGEKQRLAVARL 662
Cdd:COG4136 80 ILFQDDLLFpHLSVGENLAFA-LPPT------IGRAQRRARVEQAL-----EEAGLAGFadrdpaTLSGGQRARVALLRA 147
|
170
....*....|....*...
gi 2274528008 663 LLKNPSILFFDEATSALD 680
Cdd:COG4136 148 LLAEPRALLLDEPFSKLD 165
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
512-735 |
2.45e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 91.79 E-value: 2.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYhPD--RPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQS---GKIYIDGQDITKVSLESLRR 586
Cdd:PRK13640 6 VEFKHVSFTY-PDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 587 HIGVVPQ--DTPLFNDDIRHNIRYGrLDasdadvEAAARAAKVDQIVQNLpqgyntkVGERGLM---------ISGGEKQ 655
Cdd:PRK13640 85 KVGIVFQnpDNQFVGATVGDDVAFG-LE------NRAVPRPEMIKIVRDV-------LADVGMLdyidsepanLSGGQKQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 656 RLAVARLLLKNPSILFFDEATSALDSYTETELMRNINaNLLSEKRTAIF-VAHRLRTISDSDLIVVLQSGQVAEKGTHAE 734
Cdd:PRK13640 151 RVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIR-KLKKKNNLTVIsITHDIDEANMADQVLVLDDGKLLAQGSPVE 229
|
.
gi 2274528008 735 L 735
Cdd:PRK13640 230 I 230
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
530-772 |
2.47e-20 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 96.77 E-value: 2.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 530 NISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDgqditkvsleslrRHIGVVPQDTPLFNDDIRHNIRYg 609
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGNILF- 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 610 rLDASD-ADVEAAARAAKVDQIVQNLPQGYNTKVGERGLMISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELM 688
Cdd:PTZ00243 744 -FDEEDaARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVV 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 689 RNINANLLSEKrTAIFVAHRLRTISDSDLIVVLQSGQVAEKGTHAELMdRKGLYWDLWQAQSTLGVGHGAGANEHLQDLE 768
Cdd:PTZ00243 823 EECFLGALAGK-TRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFM-RTSLYATLAAELKENKDSKEGDADAEVAEVD 900
|
....
gi 2274528008 769 REQG 772
Cdd:PTZ00243 901 AAPG 904
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
512-741 |
2.93e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 91.73 E-value: 2.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPDRPI----FSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVS----LES 583
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegraLFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 584 LRRHIGVVPQ--DTPLFNDDIRHNIRYGRLDASDADVEAAARAAKVDQIVqnlpqGYNTKVGERG-LMISGGEKQRLAVA 660
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALV-----GISESLFEKNpFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 661 RLLLKNPSILFFDEATSALDSYTETELMRnINANLLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQVAEKGT------HA 733
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPKGRKELMT-LFKKLHQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKpkdifqDV 236
|
....*...
gi 2274528008 734 ELMDRKGL 741
Cdd:PRK13649 237 DFLEEKQL 244
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
512-738 |
4.34e-20 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 90.15 E-value: 4.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVT--FGyhpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDIT--KVSLESLRRH 587
Cdd:PRK09493 2 IEFKNVSkhFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 588 IGVV-------PQDTPLfnddirHNIRYGRLD---ASDADVEaaaraakvDQIVQNLpqgynTKVGERGLM------ISG 651
Cdd:PRK09493 79 AGMVfqqfylfPHLTAL------ENVMFGPLRvrgASKEEAE--------KQARELL-----AKVGLAERAhhypseLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 652 GEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRnINANLLSEKRTAIFVAHRL---RTISdSDLIVVlQSGQVAE 728
Cdd:PRK09493 140 GQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLK-VMQDLAEEGMTMVIVTHEIgfaEKVA-SRLIFI-DKGRIAE 216
|
250
....*....|
gi 2274528008 729 KGTHAELMDR 738
Cdd:PRK09493 217 DGDPQVLIKN 226
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
512-736 |
4.82e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 90.82 E-value: 4.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGVV 591
Cdd:PRK10253 8 LRGEQLTLGYG-KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 592 PQD--TPlfnDDIR-----------HNIRYGRLDASDADVeaAARAAKVDQIVQNLPQGYNTkvgerglmISGGEKQRLA 658
Cdd:PRK10253 87 AQNatTP---GDITvqelvargrypHQPLFTRWRKEDEEA--VTKAMQATGITHLADQSVDT--------LSGGQRQRAW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 659 VARLLLKNPSILFFDEATSALDSYTETELMRninanLLSEKR-----TAIFVAHRL-RTISDSDLIVVLQSGQVAEKGTH 732
Cdd:PRK10253 154 IAMVLAQETAIMLLDEPTTWLDISHQIDLLE-----LLSELNrekgyTLAAVLHDLnQACRYASHLIALREGKIVAQGAP 228
|
....
gi 2274528008 733 AELM 736
Cdd:PRK10253 229 KEIV 232
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
525-736 |
5.72e-20 |
|
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: 89.52 E-value: 5.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 525 RPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSL-ESLRRHIGVVPQDTPLFND-DI 602
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYLPQEASIFRKlTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 603 RHNIrygRLDASDADVEAAARAAKVDQIVQNLPQGYNTKvgERGLMISGGEKQRLAVARLLLKNPSILFFDEATSALDSY 682
Cdd:cd03218 93 EENI---LAVLEIRGLSKKEREEKLEELLEEFHITHLRK--SKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2274528008 683 TETELMRNInaNLLSEKRTAIFVA-HRLR-TISDSDLIVVLQSGQVAEKGTHAELM 736
Cdd:cd03218 168 AVQDIQKII--KILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
512-739 |
6.63e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 90.61 E-value: 6.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPDRPI----FSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVS----LES 583
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqaIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 584 LRRHIGVVPQ--DTPLFNDDIRHNIRYGrldASDADVEAAARAAKVDQIVQNLpqGYNTKVGERG-LMISGGEKQRLAVA 660
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFG---PKNFKMNLDEVKNYAHRLLMDL--GFSRDVMSQSpFQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 661 RLLLKNPSILFFDEATSALDSYTETELMRNINANLLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQVAEKGTHAELMDRK 739
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKDK 237
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
512-736 |
1.05e-19 |
|
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: 89.37 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYhPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGK-IYIDGQDITKVSLESLRRHIGV 590
Cdd:COG1119 4 LELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 591 VpqdTPLFNDDIRHNI---------------RYGRLDASDADveaaaraaKVDQIVQNLpqGYNTKVGERGLMISGGEKQ 655
Cdd:COG1119 83 V---SPALQLRFPRDEtvldvvlsgffdsigLYREPTDEQRE--------RARELLELL--GLAHLADRPFGTLSQGEQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 656 RLAVARLLLKNPSILFFDEATSALDSYTETELMRNINANLLSEKRTAIFVAHRLRTISDS-DLIVVLQSGQVAEKGTHAE 734
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEE 229
|
..
gi 2274528008 735 LM 736
Cdd:COG1119 230 VL 231
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
519-728 |
1.38e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 89.36 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 519 FGYHPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLE---SLRRHIGVVPQDT 595
Cdd:PRK10419 19 SGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAqrkAFRRDIQMVFQDS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 596 P-LFNDdiRHNIRY---------GRLDASDADVEAAARAAKVD---QIVQNLPQgyntkvgerglMISGGEKQRLAVARL 662
Cdd:PRK10419 99 IsAVNP--RKTVREiireplrhlLSLDKAERLARASEMLRAVDlddSVLDKRPP-----------QLSGGQLQRVCLARA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2274528008 663 LLKNPSILFFDEATSALDSYTETELMRNINAnLLSEKRTA-IFVAHRLRTISD-SDLIVVLQSGQVAE 728
Cdd:PRK10419 166 LAVEPKLLILDEAVSNLDLVLQAGVIRLLKK-LQQQFGTAcLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
511-741 |
1.45e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 89.69 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 511 EIRFENVTFGYHPDRPI----FSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDIT----KVSLE 582
Cdd:PRK13634 2 DITFQKVEHRYQYKTPFerraLYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkkNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 583 SLRRHIGVVPQ--DTPLFNDDIRHNIRYGRLD--ASDADVEAaaraaKVDQIVQNLpqGYNTKVGERG-LMISGGEKQRL 657
Cdd:PRK13634 82 PLRKKVGIVFQfpEHQLFEETVEKDICFGPMNfgVSEEDAKQ-----KAREMIELV--GLPEELLARSpFELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 658 AVARLLLKNPSILFFDEATSALDSYTETELMrNINANLLSEKR-TAIFVAHRLRTISD-SDLIVVLQSGQVAEKGT---- 731
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKGRKEMM-EMFYKLHKEKGlTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTprei 233
|
250
....*....|..
gi 2274528008 732 --HAELMDRKGL 741
Cdd:PRK13634 234 faDPDELEAIGL 245
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
512-735 |
1.61e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 91.24 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVslESLRRHIGVV 591
Cdd:PRK11000 4 VTLRNVTKAYG-DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDV--PPAERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 592 PQDTPLF-NDDIRHNIRYG-RLdasdADVEAAARAAKVDQIVQNLPQGYNTKVGERGLmiSGGEKQRLAVARLLLKNPSI 669
Cdd:PRK11000 81 FQSYALYpHLSVAENMSFGlKL----AGAKKEEINQRVNQVAEVLQLAHLLDRKPKAL--SGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2274528008 670 LFFDEATSALDSYTETElMRnINANLLSEK--RTAIFVAH-RLRTISDSDLIVVLQSGQVAEKGTHAEL 735
Cdd:PRK11000 155 FLLDEPLSNLDAALRVQ-MR-IEISRLHKRlgRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
529-735 |
1.73e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.39 E-value: 1.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 529 SNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVS-LESLRRHIGVVPQDTPLFND-DIRHNI 606
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGIAIIHQELNLVPNlSVAENI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 607 RYGRLDASDADVEAAARAAKVDQIVQNL-----PqgyNTKVGErglmISGGEKQRLAVARLLLKNPSILFFDEATSALDS 681
Cdd:COG1129 101 FLGREPRRGGLIDWRAMRRRARELLARLgldidP---DTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTASLTE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2274528008 682 yTETELMRNINANLLSEKRTAIFVAHRL---RTISDSdlIVVLQSGQVAEKGTHAEL 735
Cdd:COG1129 174 -REVERLFRIIRRLKAQGVAIIYISHRLdevFEIADR--VTVLRDGRLVGTGPVAEL 227
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
513-736 |
1.79e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 89.08 E-value: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 513 RFENVTFGYhPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGVVP 592
Cdd:PRK10575 13 ALRNVSFRV-PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 593 QDTPLFND-DIRHNI---RY------GRLDASDADveaaaraaKVDQIVqnlpqgynTKVGERGLM------ISGGEKQR 656
Cdd:PRK10575 92 QQLPAAEGmTVRELVaigRYpwhgalGRFGAADRE--------KVEEAI--------SLVGLKPLAhrlvdsLSGGERQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 657 LAVARLLLKNPSILFFDEATSALDSYTETELMRNINAnlLSEKR--TAIFVAHRLRTISD-SDLIVVLQSGQVAEKGTHA 733
Cdd:PRK10575 156 AWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHR--LSQERglTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPA 233
|
...
gi 2274528008 734 ELM 736
Cdd:PRK10575 234 ELM 236
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
493-742 |
2.13e-19 |
|
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: 93.82 E-value: 2.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 493 NVAVKENADAPPLKVTGGEIRFENVTFGYHPD-RPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQsGKIYI 571
Cdd:TIGR01271 1199 TVLVIENPHAQKCWPSGGQMDVQGLTAKYTEAgRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQI 1277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 572 DGQDITKVSLESLRRHIGVVPQDTPLFNDDIRHNIR-YGRLdaSDADVEAAARAAKVDQIVQNLPQGYNTKVGERGLMIS 650
Cdd:TIGR01271 1278 DGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDpYEQW--SDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLS 1355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 651 GGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNINANLlsEKRTAIFVAHRLRTISDSDLIVVLQSGQVAEKG 730
Cdd:TIGR01271 1356 NGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSF--SNCTVILSEHRVEALLECQQFLVIEGSSVKQYD 1433
|
250
....*....|..
gi 2274528008 731 THAELMDRKGLY 742
Cdd:TIGR01271 1434 SIQKLLNETSLF 1445
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
512-739 |
3.47e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 88.25 E-value: 3.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGVV 591
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 592 PQ--DTPLFNDDIRHNIRYG----RLDASDADVEAAARAAKVDQivqnlpQGYNTKVGERglmISGGEKQRLAVARLLLK 665
Cdd:PRK13647 85 FQdpDDQVFSSTVWDDVAFGpvnmGLDKDEVERRVEEALKAVRM------WDFRDKPPYH---LSYGQKKRVAIAGVLAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2274528008 666 NPSILFFDEATSALDSYTETELMrNINANLLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQVAEKGTHAELMDRK 739
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLM-EILDRLHNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
510-742 |
3.61e-19 |
|
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: 88.37 E-value: 3.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 510 GEIRFENVTFGYHPD-RPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQsGKIYIDGQDITKVSLESLRRHI 588
Cdd:cd03289 1 GQMTVKDLTAKYTEGgNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 589 GVVPQDTPLFNDDIRHNIR-YGRLdaSDADVEAAARAAKVDQIVQNLPQGYNTKVGERGLMISGGEKQRLAVARLLLKNP 667
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDpYGKW--SDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2274528008 668 SILFFDEATSALDSYTETELMRNINANLLSekRTAIFVAHRLRTISDSDLIVVLQSGQVAEKGTHAELMDRKGLY 742
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRKTLKQAFAD--CTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
516-735 |
3.96e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 88.21 E-value: 3.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 516 NVTFGYHPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDIT--KVSLESLRRHIGVVPQ 593
Cdd:PRK13639 6 DLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydKKSLLEVRKTVGIVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 594 --DTPLFNDDIRHNIRYGRLDA--SDADVEaaaraAKVDQIVQNLP-QGYNTKVGERglmISGGEKQRLAVARLLLKNPS 668
Cdd:PRK13639 86 npDDQLFAPTVEEDVAFGPLNLglSKEEVE-----KRVKEALKAVGmEGFENKPPHH---LSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2274528008 669 ILFFDEATSALDSYTETELMRNINaNLLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQVAEKGTHAEL 735
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLY-DLNKEGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEV 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
512-726 |
4.00e-19 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 86.57 E-value: 4.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVT--FGyhpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITkvslESLRRHIG 589
Cdd:cd03269 1 LEVENVTkrFG---RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD----IAARNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 590 VVPQDTPLFND-DIRHNIRY-GRLDA---SDADVEAAARAAKVDqivqnLPQGYNTKVGErglmISGGEKQRLAVARLLL 664
Cdd:cd03269 74 YLPEERGLYPKmKVIDQLVYlAQLKGlkkEEARRRIDEWLERLE-----LSEYANKRVEE----LSKGNQQKVQFIAAVI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2274528008 665 KNPSILFFDEATSALDSyTETELMRNINANLLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQV 726
Cdd:cd03269 145 HDPELLILDEPFSGLDP-VNVELLKDVIRELARAGKTVILSTHQMELVEElCDRVLLLNKGRA 206
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
512-735 |
4.99e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 87.50 E-value: 4.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDgqDIT----------KVSL 581
Cdd:PRK11264 4 IEVKNLVKKFH-GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVG--DITidtarslsqqKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 582 ESLRRHIGVVPQDTPLF-NDDIRHNIRYGRLdasdadveaaaraakvdqIVQNLPQGYNTKVGERGLM------------ 648
Cdd:PRK11264 81 RQLRQHVGFVFQNFNLFpHRTVLENIIEGPV------------------IVKGEPKEEATARARELLAkvglagketsyp 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 649 --ISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNINAnLLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQ 725
Cdd:PRK11264 143 rrLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQ-LAQEKRTMVIVTHEMSFARDvADRAIFMDQGR 221
|
250
....*....|
gi 2274528008 726 VAEKGTHAEL 735
Cdd:PRK11264 222 IVEQGPAKAL 231
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
512-738 |
1.15e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 87.47 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVT--FGyhpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITkvslESLRRHIG 589
Cdd:COG4152 2 LELKGLTkrFG---DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD----PEDRRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 590 VVPQDTPLF-NDDIRHNIRY-GRL---DASDADVEAAARAAKVDqivqnLPQGYNTKVGErglmISGGEKQR--LAVArl 662
Cdd:COG4152 75 YLPEERGLYpKMKVGEQLVYlARLkglSKAEAKRRADEWLERLG-----LGDRANKKVEE----LSKGNQQKvqLIAA-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 663 LLKNPSILFFDEATSALDSytetelmrnINANLLSE--------KRTAIFVAHRLRTISD-SDLIVVLQSGQVAEKGTHA 733
Cdd:COG4152 144 LLHDPELLILDEPFSGLDP---------VNVELLKDvirelaakGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVD 214
|
....*
gi 2274528008 734 ELMDR 738
Cdd:COG4152 215 EIRRQ 219
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
511-733 |
1.45e-18 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 85.83 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 511 EIRFENVTFGYHPDRPIFsNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDG------QDITKVSLESL 584
Cdd:COG4161 2 SIQLKNINCFYGSHQALF-DINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 585 RRHIGVVPQDTPLF------NDDIRHNIRYGRLDASDAdveaaarAAKVDQIVQNLpqGYNTKVGERGLMISGGEKQRLA 658
Cdd:COG4161 81 RQKVGMVFQQYNLWphltvmENLIEAPCKVLGLSKEQA-------REKAMKLLARL--RLTDKADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2274528008 659 VARLLLKNPSILFFDEATSALDSYTETELMRNINaNLLSEKRTAIFVAHRL----RTISDsdlIVVLQSGQVAEKGTHA 733
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPEITAQVVEIIR-ELSQTGITQVIVTHEVefarKVASQ---VVYMEKGRIIEQGDAS 226
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
530-730 |
2.05e-18 |
|
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: 85.21 E-value: 2.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 530 NISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLrrhigVVPQDTPLFN-DDIRHNIrY 608
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI-A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 609 GRLDASDADVEAAARAAKVDQIVQ--NLPQGYNTKVGErglmISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETE 686
Cdd:TIGR01184 77 LAVDRVLPDLSKSERRAIVEEHIAlvGLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2274528008 687 LMRNInANLLSEKR-TAIFVAHRL-RTISDSDLIVVLQSGQVAEKG 730
Cdd:TIGR01184 153 LQEEL-MQIWEEHRvTVLMVTHDVdEALLLSDRVVMLTNGPAANIG 197
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
513-730 |
3.94e-18 |
|
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: 84.24 E-value: 3.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 513 RFENVTfGYHP----DRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLL---FRFYKPQSGKIYIDGQDITKvslESLR 585
Cdd:cd03234 5 PWWDVG-LKAKnwnkYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNGQPRKP---DQFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 586 RHIGVVPQ-DTPLFNDDIRHNIRYG---RLDASDADveaaARAAKVDQIVQnLPQGYNTKVGERgLM--ISGGEKQRLAV 659
Cdd:cd03234 81 KCVAYVRQdDILLPGLTVRETLTYTailRLPRKSSD----AIRKKRVEDVL-LRDLALTRIGGN-LVkgISGGERRRVSI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2274528008 660 ARLLLKNPSILFFDEATSALDSYTETELMRnINANLLSEKRTAIFVAHRLRtiSD----SDLIVVLQSGQVAEKG 730
Cdd:cd03234 155 AVQLLWDPKVLILDEPTSGLDSFTALNLVS-TLSQLARRNRIVILTIHQPR--SDlfrlFDRILLLSSGEIVYSG 226
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
512-732 |
4.30e-18 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 84.30 E-value: 4.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPDRPIFsNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDG------QDITKVSLESLR 585
Cdd:PRK11124 3 IQLNGINCFYGAHQALF-DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 586 RHIGVVPQDTPLF------NDDIRHNIRYGRLDASDAdveaaarAAKVDQIVQNLPqgYNTKVGERGLMISGGEKQRLAV 659
Cdd:PRK11124 82 RNVGMVFQQYNLWphltvqQNLIEAPCRVLGLSKDQA-------LARAEKLLERLR--LKPYADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2274528008 660 ARLLLKNPSILFFDEATSALDSYTETELMRNINAnlLSEKR-TAIFVAHRL---RTISDSdlIVVLQSGQVAEKGTH 732
Cdd:PRK11124 153 ARALMMEPQVLLFDEPTAALDPEITAQIVSIIRE--LAETGiTQVIVTHEVevaRKTASR--VVYMENGHIVEQGDA 225
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
512-739 |
7.57e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 84.51 E-value: 7.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQ--DITKVSLESLRRHIG 589
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 590 VVPQ--DTPLFNDDIRHNIRYGRLDASDADVEaaaRAAKVDQIVQnlpqgyntKVGERGL------MISGGEKQRLAVAR 661
Cdd:PRK13636 86 MVFQdpDNQLFSASVYQDVSFGAVNLKLPEDE---VRKRVDNALK--------RTGIEHLkdkpthCLSFGQKKRVAIAG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2274528008 662 LLLKNPSILFFDEATSALDSYTETELMRNINANLLSEKRTAIFVAHRLRTIS-DSDLIVVLQSGQVAEKGTHAELMDRK 739
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
521-714 |
1.37e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 83.29 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 521 YHPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRF--YKPQ---SGKIYIDGQDI--TKVSLESLRRHIGVVPQ 593
Cdd:PRK14239 14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIysPRTDTVDLRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 594 DTPLFNDDIRHNIRYGRLDASDADVEaaaraaKVDQIVQNLPQGYNT--KVGER----GLMISGGEKQRLAVARLLLKNP 667
Cdd:PRK14239 94 QPNPFPMSIYENVVYGLRLKGIKDKQ------VLDEAVEKSLKGASIwdEVKDRlhdsALGLSGGQQQRVCIARVLATSP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2274528008 668 SILFFDEATSALDSYTEtelmRNINANL--LSEKRTAIFVAHRLRT---ISD 714
Cdd:PRK14239 168 KIILLDEPTSALDPISA----GKIEETLlgLKDDYTMLLVTRSMQQasrISD 215
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
511-735 |
3.85e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 82.12 E-value: 3.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 511 EIRFENVTFGyhpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVS---LESLRRH 587
Cdd:PRK11831 9 DMRGVSFTRG---NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrLYTVRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 588 IGVVPQDTPLFND-DIRHNIRYGRLDASDADveaaaraakvDQIVQNLPQGYNTKVGERG---LM---ISGGEKQRLAVA 660
Cdd:PRK11831 86 MSMLFQSGALFTDmNVFDNVAYPLREHTQLP----------APLLHSTVMMKLEAVGLRGaakLMpseLSGGMARRAALA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2274528008 661 RLLLKNPSILFFDEATSALDSYTETELMRNINANLLSEKRTAIFVAH---RLRTISDSDLIVVLQsgQVAEKGTHAEL 735
Cdd:PRK11831 156 RAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHdvpEVLSIADHAYIVADK--KIVAHGSAQAL 231
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
519-741 |
4.76e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 81.98 E-value: 4.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 519 FGYHpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQ--DITKVSLESLRRHIGVVPQD-- 594
Cdd:PRK13638 9 FRYQ-DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQDpe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 595 TPLFNDDIRHNIRYGRLDASDADVEaaaRAAKVDQIVQNL-PQGYNTKVGErglMISGGEKQRLAVARLLLKNPSILFFD 673
Cdd:PRK13638 88 QQIFYTDIDSDIAFSLRNLGVPEAE---ITRRVDEALTLVdAQHFRHQPIQ---CLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2274528008 674 EATSALDSYTETELMRNINaNLLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQVAEKG------THAELMDRKGL 741
Cdd:PRK13638 162 EPTAGLDPAGRTQMIAIIR-RIVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGapgevfACTEAMEQAGL 235
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
512-689 |
5.09e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 80.69 E-value: 5.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKV---SLESLRRHI 588
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrEVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 589 GVVPQDTPLFND-DIRHNIRYGRL--DASDADVEAAARAAkVDQIvqnlpqGYNTKVGERGLMISGGEKQRLAVARLLLK 665
Cdd:PRK10908 82 GMIFQDHHLLMDrTVYDNVAIPLIiaGASGDDIRRRVSAA-LDKV------GLLDKAKNFPIQLSGGEQQRVGIARAVVN 154
|
170 180
....*....|....*....|....
gi 2274528008 666 NPSILFFDEATSALDSYTETELMR 689
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILR 178
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
511-680 |
5.44e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 83.73 E-value: 5.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 511 EIRfeNVTFGYHpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSleSLRRHIGV 590
Cdd:PRK11607 21 EIR--NLTKSFD-GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP--PYQRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 591 VPQDTPLF-NDDIRHNIRYG----RLDASD--ADVEAAARAAKVDQIVQNLPQgyntkvgerglMISGGEKQRLAVARLL 663
Cdd:PRK11607 96 MFQSYALFpHMTVEQNIAFGlkqdKLPKAEiaSRVNEMLGLVHMQEFAKRKPH-----------QLSGGQRQRVALARSL 164
|
170
....*....|....*..
gi 2274528008 664 LKNPSILFFDEATSALD 680
Cdd:PRK11607 165 AKRPKLLLLDEPMGALD 181
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
519-736 |
6.84e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 81.17 E-value: 6.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 519 FGYHPdrpIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDIT-------------KVSLESLR 585
Cdd:PRK10619 15 YGEHE---VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 586 RHIGVVPQDTPLFN------DDIRHNIRYGRLDASDADVEAAARAAKV--DQIVQnlpqgyntkvGERGLMISGGEKQRL 657
Cdd:PRK10619 92 TRLTMVFQHFNLWShmtvleNVMEAPIQVLGLSKQEARERAVKYLAKVgiDERAQ----------GKYPVHLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 658 AVARLLLKNPSILFFDEATSALDSYTETELMRnINANLLSEKRTAIFVAHRL---RTISDSdlIVVLQSGQVAEKGTHAE 734
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLR-IMQQLAEEGKTMVVVTHEMgfaRHVSSH--VIFLHQGKIEEEGAPEQ 238
|
..
gi 2274528008 735 LM 736
Cdd:PRK10619 239 LF 240
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
526-739 |
8.69e-17 |
|
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: 81.44 E-value: 8.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 526 PIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQditkvsleslrrhIGVVPQDTPLFNDDIRHN 605
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 606 IRYGrLDASDADVEAAARAAKVDQIVQNLPQGYNTKVGERGLMISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTET 685
Cdd:cd03291 118 IIFG-VSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEK 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2274528008 686 ELMRNINANLLSEKrTAIFVAHRLRTISDSDLIVVLQSGQVAEKGTHAELMDRK 739
Cdd:cd03291 197 EIFESCVCKLMANK-TRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
521-735 |
8.92e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 80.86 E-value: 8.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 521 YHPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYID------GQDITKVSLESLRRHIGVV-PQ 593
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDgkvlyfGKDIFQIDAIKLRKEVGMVfQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 594 DTPLFNDDIRHNIRYGRLDASDADveaaarAAKVDQIVQN------LPQGYNTKVGERGLMISGGEKQRLAVARLLLKNP 667
Cdd:PRK14246 99 PNPFPHLSIYDNIAYPLKSHGIKE------KREIKKIVEEclrkvgLWKEVYDRLNSPASQLSGGQQQRLTIARALALKP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2274528008 668 SILFFDEATSALDSYTETELMRNINAnlLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQVAEKGTHAEL 735
Cdd:PRK14246 173 KVLLMDEPTSMIDIVNSQAIEKLITE--LKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
530-736 |
1.00e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 83.92 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 530 NISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQditKVSLES----LRRHIGVVPQDTPLFN-----D 600
Cdd:COG3845 23 DVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGK---PVRIRSprdaIALGIGMVHQHFMLVPnltvaE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 601 DI---RHNIRYGRLDASDAdveaaaraakvDQIVQNLPQGY------NTKVGErglmISGGEKQRLAVARLLLKNPSILF 671
Cdd:COG3845 100 NIvlgLEPTKGGRLDRKAA-----------RARIRELSERYgldvdpDAKVED----LSVGEQQRVEILKALYRGARILI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 672 FDEATSALdsyT--ET-ELMRNINaNLLSEKRTAIFVAHRLR---TISDSdlIVVLQSGQVAekGTH----------AEL 735
Cdd:COG3845 165 LDEPTAVL---TpqEAdELFEILR-RLAAEGKSIIFITHKLRevmAIADR--VTVLRRGKVV--GTVdtaetseeelAEL 236
|
.
gi 2274528008 736 M 736
Cdd:COG3845 237 M 237
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
512-741 |
1.67e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 80.52 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPD-----RPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVS-LESLR 585
Cdd:PRK13633 5 IKCKNVSYKYESNeesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 586 RHIGVVPQ--DTPLFNDDIRHNIRYGrldASDADVEAAARAAKVDQIVQnlpqgyntKVGERGL------MISGGEKQRL 657
Cdd:PRK13633 85 NKAGMVFQnpDNQIVATIVEEDVAFG---PENLGIPPEEIRERVDESLK--------KVGMYEYrrhaphLLSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 658 AVARLLLKNPSILFFDEATSALDSYTETELMRNINANLLSEKRTAIFVAHRLRTISDSDLIVVLQSGQVAEKGT------ 731
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTpkeifk 233
|
250
....*....|
gi 2274528008 732 HAELMDRKGL 741
Cdd:PRK13633 234 EVEMMKKIGL 243
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
510-741 |
1.79e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 80.82 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 510 GEIRFENVTFGYHPDRPI----FSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKI----YIDGQDITKV-S 580
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFefkaLNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTivgdYAIPANLKKIkE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 581 LESLRRHIGVVPQ--DTPLFNDDIRHNIRYGRLDASDADVEAAARAAKVDQIVQnLPQGYntkVGERGLMISGGEKQRLA 658
Cdd:PRK13645 85 VKRLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQ-LPEDY---VKRSPFELSGGQKRRVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 659 VARLLLKNPSILFFDEATSALDSYTETELMR---NINANllsEKRTAIFVAHRL-RTISDSDLIVVLQSGQVAEKGTHAE 734
Cdd:PRK13645 161 LAGIIAMDGNTLVLDEPTGGLDPKGEEDFINlfeRLNKE---YKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGSPFE 237
|
....*..
gi 2274528008 735 LMDRKGL 741
Cdd:PRK13645 238 IFSNQEL 244
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
527-728 |
2.43e-16 |
|
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: 79.01 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 527 IFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESL----RRHIGVVPQDTPLfnddI 602
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarlrARHVGFVFQSFQL----L 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 603 RH-----NI-----RYGRLDASDADVEAAaraakvdqivqnlpqgynTKVG--ER------GLmiSGGEKQRLAVARLLL 664
Cdd:COG4181 103 PTltaleNVmlpleLAGRRDARARARALL------------------ERVGlgHRldhypaQL--SGGEQQRVALARAFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2274528008 665 KNPSILFFDEATSALDSYT-ET--ELMRNINANLLSekrTAIFVAHRLRTISDSDLIVVLQSGQVAE 728
Cdd:COG4181 163 TEPAILFADEPTGNLDAATgEQiiDLLFELNRERGT---TLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
526-739 |
4.02e-16 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 83.04 E-value: 4.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 526 PIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQditkvsleslrrhIGVVPQDTPLFNDDIRHN 605
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 606 IRYGrLDASDADVEAAARAAKVDQIVQNLPQGYNTKVGERGLMISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTET 685
Cdd:TIGR01271 507 IIFG-LSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEK 585
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2274528008 686 ELMRNINANLLSEKrTAIFVAHRLRTISDSDLIVVLQSGQVAEKGTHAELMDRK 739
Cdd:TIGR01271 586 EIFESCLCKLMSNK-TRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
526-680 |
5.65e-16 |
|
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: 77.86 E-value: 5.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 526 PIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQ----DITKVS----LEsLRRH-IG------- 589
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASpreiLA-LRRRtIGyvsqflr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 590 VVPQDT-------PLfnddirhnIRYGrLDASDADVEAAARAAKVdqivqNLPQGY-----NTkvgerglmISGGEKQRL 657
Cdd:COG4778 104 VIPRVSaldvvaePL--------LERG-VDREEARARARELLARL-----NLPERLwdlppAT--------FSGGEQQRV 161
|
170 180
....*....|....*....|...
gi 2274528008 658 AVARLLLKNPSILFFDEATSALD 680
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLD 184
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
528-726 |
6.68e-16 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 76.32 E-value: 6.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 528 FSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVS-LESLRRHIGVVPQDtplfnddiRHni 606
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAGIAYVPED--------RK-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 607 RYGrldasdadveaaaraakvdqIVQNLPQGYNTKVGergLMISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETE 686
Cdd:cd03215 86 REG--------------------LVLDLSVAENIALS---SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2274528008 687 LMRNINAnlLSEKRTAIFVahrlrtISD--------SDLIVVLQSGQV 726
Cdd:cd03215 143 IYRLIRE--LADAGKAVLL------ISSeldellglCDRILVMYEGRI 182
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
513-737 |
7.55e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.11 E-value: 7.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 513 RFENVTFGYhPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDI----TKVSLESlrrhi 588
Cdd:PRK11288 6 SFDGIGKTF-PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasTTAALAA----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 589 GV---------VPQDTplfnddIRHNIRYGRLDASDADVEAAARAAKVDQIVQNL-----PqgyNTKVGErglmISGGEK 654
Cdd:PRK11288 80 GVaiiyqelhlVPEMT------VAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLgvdidP---DTPLKY----LSIGQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 655 QRLAVARLLLKNPSILFFDEATSALdSYTETE-LMRNINAnLLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQVAEkgTH 732
Cdd:PRK11288 147 QMVEIAKALARNARVIAFDEPTSSL-SAREIEqLFRVIRE-LRAEGRVILYVSHRMEEIFAlCDAITVFKDGRYVA--TF 222
|
....*
gi 2274528008 733 AELMD 737
Cdd:PRK11288 223 DDMAQ 227
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
183-470 |
8.19e-16 |
|
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: 78.63 E-value: 8.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 183 VALALALLVGGKLLNVQVPFFFKAIVDRLnqvvnapLDMTNPNTVWVVAGsAILGYGLARvgaAAFSELRNAVFANVAQQ 262
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSV-------IGGGLRELLWLLAL-LILGVALLR---GVFRYLQGYLAEKASQK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 263 SIRRVARSVFTHLLALDLGWHLTRQTGGLtraIDRGT-----------KGISFLLTSIVFHIVPTALEISM--------- 322
Cdd:cd18542 70 VAYDLRNDLYDHLQRLSFSFHDKARTGDL---MSRCTsdvdtirrflaFGLVELVRAVLLFIGALIIMFSInwkltlisl 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 323 ----VCGILSY----KCGPsfaavtavtmaayAWFTIRttswrtrfrkEANAADNRAAT---TSVdsllnyEAVKYFNNE 391
Cdd:cd18542 147 aiipFIALFSYvffkKVRP-------------AFEEIR----------EQEGELNTVLQenlTGV------RVVKAFARE 197
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2274528008 392 KHEIAKYDAALADYEKSSIKVATSLAALNSGQNAIFSTSLTVMMLLAAQGVTNGTMSVGDLVMVNQLVFQLSLPLNFLG 470
Cdd:cd18542 198 DYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLG 276
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
512-739 |
8.19e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 79.08 E-value: 8.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESlRRHIGVV 591
Cdd:PRK13537 8 IDFRNVEKRYG-DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 592 PQDTPLFND-DIRHNI----RYGRLDASDAdveaaarAAKVDQIVQ--NLPQGYNTKVGErglmISGGEKQRLAVARLLL 664
Cdd:PRK13537 86 PQFDNLDPDfTVRENLlvfgRYFGLSAAAA-------RALVPPLLEfaKLENKADAKVGE----LSGGMKRRLTLARALV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 665 KNPSILFFDEATSALDSYTEtELMRNINANLLSEKRTAIFVAH------RLrtisdSDLIVVLQSGQVAEKGTHAELMDR 738
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQAR-HLMWERLRSLLARGKTILLTTHfmeeaeRL-----CDRLCVIEEGRKIAEGAPHALIES 228
|
.
gi 2274528008 739 K 739
Cdd:PRK13537 229 E 229
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
541-726 |
8.38e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 79.53 E-value: 8.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 541 TAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQ---DI-TKVSLESLRRHIGVVPQDTPLF-NDDIRHNIRYGrLDASD 615
Cdd:PRK11144 27 TAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAeKGICLPPEKRRIGYVFQDARLFpHYKVRGNLRYG-MAKSM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 616 ADveaaaraaKVDQIVQNLpqGYNTKVGERGLMISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELM------- 688
Cdd:PRK11144 106 VA--------QFDKIVALL--GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLpylerla 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 2274528008 689 RNINANLLsekrtaiFVAHRLRTISD-SDLIVVLQSGQV 726
Cdd:PRK11144 176 REINIPIL-------YVSHSLDEILRlADRVVVLEQGKV 207
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
524-738 |
8.87e-16 |
|
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: 76.41 E-value: 8.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 524 DRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRF--YKPQSGKIYIDGQDITKVSL-ESLRRHIGVVPQDTPLFnd 600
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPeERARLGIFLAFQYPPEI-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 601 dirhnirygrldasdadveaaaRAAKVDQIVQNLPQGYntkvgerglmiSGGEKQRLAVARLLLKNPSILFFDEATSALD 680
Cdd:cd03217 90 ----------------------PGVKNADFLRYVNEGF-----------SGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 681 sYTETELMRNINANLLSEKRTAIFVAHRLRTIS--DSDLIVVLQSGQVAEKGThAELMDR 738
Cdd:cd03217 137 -IDALRLVAEVINKLREEGKSVLIITHYQRLLDyiKPDRVHVLYDGRIVKSGD-KELALE 194
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
512-730 |
1.41e-15 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 76.42 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYH---------------------PDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIY 570
Cdd:cd03220 1 IELENVSKSYPtykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 571 IDGQDitkVSLesLRRHIGvvpqdtplFNDDI--RHNIR-YGRL-DASDADVEaaaraAKVDQIVQ--NLPQGYNTKVGE 644
Cdd:cd03220 81 VRGRV---SSL--LGLGGG--------FNPELtgRENIYlNGRLlGLSRKEID-----EKIDEIIEfsELGDFIDLPVKT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 645 rglmISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNINaNLLSEKRTAIFVAHRLRTISD-SDLIVVLQS 723
Cdd:cd03220 143 ----YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLR-ELLKQGKTVILVSHDPSSIKRlCDRALVLEK 217
|
....*..
gi 2274528008 724 GQVAEKG 730
Cdd:cd03220 218 GKIRFDG 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
530-730 |
1.75e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 80.28 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 530 NISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVS---LESLRRHIGVVPQDtPLFNDDIRHNI 606
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQD-PYASLDPRQTV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 607 RY---------GRLDASDADVEAAARAAKVDQIVQN---LPQGYntkvgerglmiSGGEKQRLAVARLLLKNPSILFFDE 674
Cdd:PRK10261 421 GDsimeplrvhGLLPGKAAAARVAWLLERVGLLPEHawrYPHEF-----------SGGQRQRICIARALALNPKVIIADE 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2274528008 675 ATSALDSYTETELMrNINANLLSEKRTA-IFVAHRLRTISD-SDLIVVLQSGQVAEKG 730
Cdd:PRK10261 490 AVSALDVSIRGQII-NLLLDLQRDFGIAyLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
522-683 |
2.03e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 76.66 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 522 HPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESlrrhiGVVPQDTPLFN-D 600
Cdd:PRK11248 11 YGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVVFQNEGLLPwR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 601 DIRHNIRYG-RLdasdADVEAAARAAKVDQIVQnlpqgyntKVGERGL------MISGGEKQRLAVARLLLKNPSILFFD 673
Cdd:PRK11248 86 NVQDNVAFGlQL----AGVEKMQRLEIAHQMLK--------KVGLEGAekryiwQLSGGQRQRVGIARALAANPQLLLLD 153
|
170
....*....|
gi 2274528008 674 EATSALDSYT 683
Cdd:PRK11248 154 EPFGALDAFT 163
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
512-683 |
2.18e-15 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 76.82 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPD---RPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESlrrhi 588
Cdd:COG4525 4 LTVRHVSVRYPGGgqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 589 GVVPQDTPLFN-DDIRHNIRYG-RLdasdADVEAAARAAKVDQIVQnlpqgyntKVGERGL---MI---SGGEKQRLAVA 660
Cdd:COG4525 79 GVVFQKDALLPwLNVLDNVAFGlRL----RGVPKAERRARAEELLA--------LVGLADFarrRIwqlSGGMRQRVGIA 146
|
170 180
....*....|....*....|...
gi 2274528008 661 RLLLKNPSILFFDEATSALDSYT 683
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDALT 169
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
524-689 |
3.39e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 74.91 E-value: 3.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 524 DRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGvvPQD--TPLFNdd 601
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNamKPALT-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 602 IRHNIRYGR--LDASDADVEAAARAAKVDQIvQNLPQGYntkvgerglmISGGEKQRLAVARLLLKNPSILFFDEATSAL 679
Cdd:PRK13539 90 VAENLEFWAafLGGEELDIAAALEAVGLAPL-AHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170
....*....|...
gi 2274528008 680 DSYTE---TELMR 689
Cdd:PRK13539 159 DAAAValfAELIR 171
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
512-708 |
3.61e-15 |
|
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: 79.41 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLF--------RFYKPQSGKIYIDGQDiTKVSLES 583
Cdd:TIGR00954 452 IKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKLFYVPQR-PYMTLGT 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 584 LRRHIgVVPqDTPlfnDDIRhnirygRLDASDADVEAAARAAKVDQIVQNlpQGYNTKVGERGLMISGGEKQRLAVARLL 663
Cdd:TIGR00954 531 LRDQI-IYP-DSS---EDMK------RRGLSDKDLEQILDNVQLTHILER--EGGWSAVQDWMDVLSGGEKQRIAMARLF 597
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2274528008 664 LKNPSILFFDEATSALDSYTET---ELMRNINANLLSekrtaifVAHR 708
Cdd:TIGR00954 598 YHKPQFAILDECTSAVSVDVEGymyRLCREFGITLFS-------VSHR 638
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
511-741 |
5.23e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 76.66 E-value: 5.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 511 EIRFENVTFGYHPDRPI----FSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKI---YIDGQDITKVSL-- 581
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEke 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 582 -------------------ESLRRHIGVVPQ--DTPLFNDDIRHNIRYGRLDASDADVEAAARAAKVDQIVqNLPQGYNT 640
Cdd:PRK13651 82 kvleklviqktrfkkikkiKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELV-GLDESYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 641 KvgeRGLMISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETElMRNINANLLSEKRTAIFVAHRL--------RTI 712
Cdd:PRK13651 161 R---SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKE-ILEIFDNLNKQGKTIILVTHDLdnvlewtkRTI 236
|
250 260 270
....*....|....*....|....*....|
gi 2274528008 713 sdsdlivVLQSGQVAEKG-THAELMDRKGL 741
Cdd:PRK13651 237 -------FFKDGKIIKDGdTYDILSDNKFL 259
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
527-726 |
5.28e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 79.00 E-value: 5.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 527 IFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKV---SLESLRR-HIGVVPQDTPLFND-D 601
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadALAQLRReHFGFIFQRYHLLSHlT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 602 IRHNIrygRLDASDADVEAAARAAKVDQIVQNLpqGYNTKVGERGLMISGGEKQRLAVARLLLKNPSILFFDEATSALDS 681
Cdd:PRK10535 103 AAQNV---EVPAVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDS 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2274528008 682 YTETELMrNINANLLSEKRTAIFVAHRLRTISDSDLIVVLQSGQV 726
Cdd:PRK10535 178 HSGEEVM-AILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
486-730 |
8.03e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 77.82 E-value: 8.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 486 MFNLENVNVAVKENADAPP-LKVTGGEIRFE------NVTFGYHPdrpIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLL 558
Cdd:PRK15134 256 LLNSEPSGDPVPLPEPASPlLDVEQLQVAFPirkgilKRTVDHNV---VVKNISFTLRPGETLGLVGESGSGKSTTGLAL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 559 FRFYKPQsGKIYIDGQDITKVS---LESLRRHIGVVPQD-----TPLFN--DDIRHNIRYGRLDASDADVEAaaraaKVD 628
Cdd:PRK15134 333 LRLINSQ-GEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDpnsslNPRLNvlQIIEEGLRVHQPTLSAAQREQ-----QVI 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 629 QIVQNL---PQGYNTKVGErglmISGGEKQRLAVARLLLKNPSILFFDEATSALDsytetelmRNINANLLS-------E 698
Cdd:PRK15134 407 AVMEEVgldPETRHRYPAE----FSGGQRQRIAIARALILKPSLIILDEPTSSLD--------KTVQAQILAllkslqqK 474
|
250 260 270
....*....|....*....|....*....|....
gi 2274528008 699 KRTA-IFVAHRLRTI-SDSDLIVVLQSGQVAEKG 730
Cdd:PRK15134 475 HQLAyLFISHDLHVVrALCHQVIVLRQGEVVEQG 508
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
503-727 |
1.38e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 76.98 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 503 PPLKVTGGEIRFE--NVTfgyhpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVS 580
Cdd:COG1129 246 PKRAAAPGEVVLEveGLS-----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRS 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 581 -LESLRRHIGVVPQD---TPLF-NDDIRHNI---------RYGRLD--ASDADVEAAARAAKV-----DQIVQNLpqgyn 639
Cdd:COG1129 321 pRDAIRAGIAYVPEDrkgEGLVlDLSIRENItlasldrlsRGGLLDrrRERALAEEYIKRLRIktpspEQPVGNL----- 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 640 tkvgerglmiSGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNINAnlLSEKRTAIFVahrlrtISD----- 714
Cdd:COG1129 396 ----------SGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRE--LAAEGKAVIV------ISSelpel 457
|
250
....*....|....*.
gi 2274528008 715 ---SDLIVVLQSGQVA 727
Cdd:COG1129 458 lglSDRILVMREGRIV 473
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
516-735 |
1.54e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 74.75 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 516 NVTFGYhPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRF------YKpQSGKIYIDGQDITKV-SLESLRRHI 588
Cdd:PRK14271 26 NLTLGF-AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMndkvsgYR-YSGDVLLGGRSIFNYrDVLEFRRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 589 GVVPQDTPLFNDDIRHNIRYGRLDASDADVEAAARAAKVDQIVQNLPQGYNTKVGERGLMISGGEKQRLAVARLLLKNPS 668
Cdd:PRK14271 104 GMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPE 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2274528008 669 ILFFDEATSALDSYTETELMRNINAnlLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQVAEKGTHAEL 735
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRS--LADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
515-707 |
1.55e-14 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 77.24 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 515 ENVTFGYhPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIyidgqditKVSLESlrrHIGVVPQD 594
Cdd:PRK15064 323 ENLTKGF-DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------KWSENA---NIGYYAQD 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 595 -TPLFNDDI------------RHN---IR--YGRLDASDADVeaaarAAKVdqivqnlpqgyntKVgerglmISGGEKQR 656
Cdd:PRK15064 391 hAYDFENDLtlfdwmsqwrqeGDDeqaVRgtLGRLLFSQDDI-----KKSV-------------KV------LSGGEKGR 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2274528008 657 LAVARLLLKNPSILFFDEATSALDsytetelMRNINA-NLLSEKR--TAIFVAH 707
Cdd:PRK15064 447 MLFGKLMMQKPNVLVMDEPTNHMD-------MESIESlNMALEKYegTLIFVSH 493
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
501-738 |
2.88e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 73.42 E-value: 2.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 501 DAPPLKVtggeirfENVTFGYHPdRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVS 580
Cdd:PRK11701 3 DQPLLSV-------RGLTKLYGP-RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 581 L----ESLRRHI-----GVVPQDT----------------PLFNDDIRHnirYGRLDASDAD----VEAAARaaKVDqiv 631
Cdd:PRK11701 75 LyalsEAERRRLlrtewGFVHQHPrdglrmqvsaggnigeRLMAVGARH---YGDIRATAGDwlerVEIDAA--RID--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 632 qNLPQGYntkvgerglmiSGGEKQRLAVARLLLKNPSILFFDEATSALDSYTET---ELMRNINANL-LSekrtAIFVAH 707
Cdd:PRK11701 147 -DLPTTF-----------SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQArllDLLRGLVRELgLA----VVIVTH 210
|
250 260 270
....*....|....*....|....*....|....
gi 2274528008 708 RL---RTISDSdlIVVLQSGQVAEKGthaeLMDR 738
Cdd:PRK11701 211 DLavaRLLAHR--LLVMKQGRVVESG----LTDQ 238
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
529-737 |
3.23e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 72.95 E-value: 3.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 529 SNISFAVPAGYKTAFVGPSGCGKSTifrLLFRF--YKPQSGKIYIDGQDITKVSLESLRRHIGVVPQ-DTPLFNDDIRHN 605
Cdd:COG4138 13 GPISAQVNAGELIHLIGPNGAGKST---LLARMagLLPGQGEILLNGRPLSDWSAAELARHRAYLSQqQSPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 606 IR-YGRLDASDADVEAAaraakVDQIVQNLpqGYNTKVGeRGLM-ISGGEKQRLAVARLLLK-----NPS--ILFFDEAT 676
Cdd:COG4138 90 LAlHQPAGASSEAVEQL-----LAQLAEAL--GLEDKLS-RPLTqLSGGEWQRVRLAAVLLQvwptiNPEgqLLLLDEPM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2274528008 677 SALDSYTETELMRninanLLSE----KRTAIFVAHRL-RTISDSDLIVVLQSGQVAEKGTHAELMD 737
Cdd:COG4138 162 NSLDVAQQAALDR-----LLRElcqqGITVVMSSHDLnHTLRHADRVWLLKQGKLVASGETAEVMT 222
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
183-480 |
3.71e-14 |
|
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: 73.70 E-value: 3.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 183 VALALALLVGGKLLNVQVPFFFKAIVDRlnqVVNAPLDMTNPNTVWVVagsaILGYGLARVGAAAFSELRNAVFANVAQQ 262
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDD---VLIQLGPGGNTSLLLLL----VLGLAGAYVLSALLGILRGRLLARLGER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 263 SIRRVARSVFTHLLALDLGWHLTRQTGGLTRAIDRGTKGISFLLTSIVFHIVPTALEISMVCGILSY--------KCGPS 334
Cdd:cd18563 74 ITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSlnwklallVLIPV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 335 FAAvtavtmaayAWFTIRttSW---RTRFRKeanAADNRAATTSV--DSLLNYEAVKYFNNEKHEIAKYDAALADYEKSS 409
Cdd:cd18563 154 PLV---------VWGSYF--FWkkiRRLFHR---QWRRWSRLNSVlnDTLPGIRVVKAFGQEKREIKRFDEANQELLDAN 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2274528008 410 IKVATSLAALNSGQNAIFSTSLTVMMLLAAQGVTNGTMSVGDLVMVNQLVFQLSLPLNFLGTVYRELRQSL 480
Cdd:cd18563 220 IRAEKLWATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRAL 290
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
523-737 |
4.11e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 75.85 E-value: 4.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 523 PDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLfRFYKPQ----SGKIYIDGqdiTKVSLESLRRHIGVVPQDTPLF 598
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNAL-AFRSPKgvkgSGSVLLNG---MPIDAKEMRAISAYVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 599 ND-------DIRHNIRYGRLDASDADVEaaaraaKVDQIVQ--NLPQGYNTKVGERGLM--ISGGEKQRLAVARLLLKNP 667
Cdd:TIGR00955 112 PTltvrehlMFQAHLRMPRRVTKKEKRE------RVDEVLQalGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDP 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2274528008 668 SILFFDEATSALDSYTETELMRNINaNLLSEKRTAIFVAHRlrtiSDSDL------IVVLQSGQVAEKGTHAELMD 737
Cdd:TIGR00955 186 PLLFCDEPTSGLDSFMAYSVVQVLK-GLAQKGKTIICTIHQ----PSSELfelfdkIILMAEGRVAYLGSPDQAVP 256
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
538-718 |
4.12e-14 |
|
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: 70.48 E-value: 4.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 538 GYKTAFVGPSGCGKSTIFRLLFRFYKPQSGK-IYIDGQDITKVSLESLRrhigvvpqdtplfnddirhnirygrldasda 616
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLL------------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 617 dveaaaraakvdqivqnlpqgyNTKVGERGLMISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNINANLL 696
Cdd:smart00382 51 ----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLL 108
|
170 180
....*....|....*....|....*.
gi 2274528008 697 ----SEKRTAIFVAHRLRTISDSDLI 718
Cdd:smart00382 109 lllkSEKNLTVILTTNDEKDLGPALL 134
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
515-726 |
5.02e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 72.79 E-value: 5.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 515 ENVTFGYHpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIyIDGQditkVSLESLRRHIGVVPQD 594
Cdd:PRK11247 16 NAVSKRYG-ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGT----APLAEAREDTRLMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 595 TPLFN-----DDI----RHNIRYGRLDASDAdveaaaraakvdqivqnlpQGYNTKVGERGLMISGGEKQRLAVARLLLK 665
Cdd:PRK11247 90 ARLLPwkkviDNVglglKGQWRDAALQALAA-------------------VGLADRANEWPAALSGGQKQRVALARALIH 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2274528008 666 NPSILFFDEATSALDSYTETElMRNINANLLSEKR-TAIFVAHRL-RTISDSDLIVVLQSGQV 726
Cdd:PRK11247 151 RPGLLLLDEPLGALDALTRIE-MQDLIESLWQQHGfTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
531-737 |
7.22e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 73.59 E-value: 7.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 531 ISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESL---RRHIGVVPQDtPLFNDDIRHNI- 606
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravRSDIQMIFQD-PLASLNPRMTIg 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 607 ---------RYGRLDASDADVEAAARAAKVDQivqnLPQGYNTKVGErglmISGGEKQRLAVARLLLKNPSILFFDEATS 677
Cdd:PRK15079 119 eiiaeplrtYHPKLSRQEVKDRVKAMMLKVGL----LPNLINRYPHE----FSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2274528008 678 ALDSYTETELMrninaNLLSEKR-----TAIFVAHRLRTISD-SDLIVVLQSGQVAEKGTHAELMD 737
Cdd:PRK15079 191 ALDVSIQAQVV-----NLLQQLQremglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYH 251
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
525-680 |
1.09e-13 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 70.47 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 525 RPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSlESLRRHI-------GVVPQDTPL 597
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQR-DEPHENIlylghlpGLKPELSAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 598 FNDDIRHNI-RYGRLDASDAdveaaaraakvdqivqnlpqgyNTKVGERGL------MISGGEKQRLAVARLLLKNPSIL 670
Cdd:TIGR01189 92 ENLHFWAAIhGGAQRTIEDA----------------------LAAVGLTGFedlpaaQLSAGQQRRLALARLWLSRRPLW 149
|
170
....*....|
gi 2274528008 671 FFDEATSALD 680
Cdd:TIGR01189 150 ILDEPTTALD 159
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
516-694 |
1.45e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 69.98 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 516 NVTFGYHpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKvSLESLRRHIGVVPQDT 595
Cdd:PRK13540 6 ELDFDYH-DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHRS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 596 PLF-NDDIRHNIRYgrldasdaDVEAAARAAKVDQIVQNLPQGY--NTKVGerglMISGGEKQRLAVARLLLKNPSILFF 672
Cdd:PRK13540 84 GINpYLTLRENCLY--------DIHFSPGAVGITELCRLFSLEHliDYPCG----LLSSGQKRQVALLRLWMSKAKLWLL 151
|
170 180
....*....|....*....|..
gi 2274528008 673 DEATSALDSYTETELMRNINAN 694
Cdd:PRK13540 152 DEPLVALDELSLLTIITKIQEH 173
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
527-683 |
1.99e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 70.61 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 527 IFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLES---LR-RHIGVVPQDTPLFND-D 601
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRnQKLGFIYQFHHLLPDfT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 602 IRHNIRYGRLDASDADVEAAARAAKVDQIVqnlpqGYNTKVGERGLMISGGEKQRLAVARLLLKNPSILFFDEATSALDS 681
Cdd:PRK11629 104 ALENVAMPLLIGKKKPAEINSRALEMLAAV-----GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDA 178
|
..
gi 2274528008 682 YT 683
Cdd:PRK11629 179 RN 180
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
186-453 |
2.26e-13 |
|
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: 71.44 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 186 ALALLVGGKLLNVQVPFFFKAIVDRLnqVVNAPLDMTNPNTVWVVAGSAILgyglarvgaAAFSELRNAVFANVAQQSIR 265
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTI--IKGGDLDVLNELALILLAIYLLQ---------SVFTFVRYYLFNIAGERIVA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 266 RVARSVFTHLLALDLGWHLTRQTGGLTRAIDRGTKGISFLLTSIVFHIVPTALEISMVCGIL---SYKCGPSFAAVTAVT 342
Cdd:cd18557 70 RLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILfilSWKLTLVLLLVIPLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 343 MAAYAWFTiRTTSWRTRFRKEANAADNRAATtsvDSLLNYEAVKYFNNEKHEIAKYDAALADYEKSSIKVATSLAALNSG 422
Cdd:cd18557 150 LIASKIYG-RYIRKLSKEVQDALAKAGQVAE---ESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGI 225
|
250 260 270
....*....|....*....|....*....|.
gi 2274528008 423 QNAIFSTSLTVMMLLAAQGVTNGTMSVGDLV 453
Cdd:cd18557 226 TSLLIYLSLLLVLWYGGYLVLSGQLTVGELT 256
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
526-737 |
2.59e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.16 E-value: 2.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 526 PIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKvsLESLRRH---IGVVPQDTPLF-NDD 601
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCAR--LTPAKAHqlgIYLVPQEPLLFpNLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 602 IRHNIRYGrLDASDADVEaaaraaKVDQIVQNLPQGYNTKVGERGLMISggEKQRLAVARLLLKNPSILFFDEATSALDS 681
Cdd:PRK15439 103 VKENILFG-LPKRQASMQ------KMKQLLAALGCQLDLDSSAGSLEVA--DRQIVEILRGLMRDSRILILDEPTASLTP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2274528008 682 YtETE-LMRNINAnLLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQVAEKGTHAELMD 737
Cdd:PRK15439 174 A-ETErLFSRIRE-LLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADLST 229
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
503-742 |
2.64e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 71.81 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 503 PPLKVTGGEI-RFENVTFGYHPDRP----IFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYID----G 573
Cdd:PRK13631 12 VPNPLSDDIIlRVKNLYCVFDEKQEnelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 574 QDITKVS------------LESLRRHIGVVPQ--DTPLFNDDIRHNIRYGRLDASDADVEAAARAAKvdqivqnlpqgYN 639
Cdd:PRK13631 92 DKKNNHElitnpyskkiknFKELRRRVSMVFQfpEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKF-----------YL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 640 TKVG------ERG-LMISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNInANLLSEKRTAIFVAHRLRTI 712
Cdd:PRK13631 161 NKMGlddsylERSpFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLI-LDAKANNKTVFVITHTMEHV 239
|
250 260 270
....*....|....*....|....*....|.
gi 2274528008 713 SD-SDLIVVLQSGQVAEKGTHAELMDRKGLY 742
Cdd:PRK13631 240 LEvADEVIVMDKGKILKTGTPYEIFTDQHII 270
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
515-736 |
2.74e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 70.31 E-value: 2.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 515 ENVTFGYHpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSL-ESLRRHIGVVPQ 593
Cdd:PRK10895 7 KNLAKAYK-GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 594 DTPLFND-----------DIRHNI-RYGRLDASDADVEAAARAAKVDQIVQNLpqgyntkvgerglmiSGGEKQRLAVAR 661
Cdd:PRK10895 86 EASIFRRlsvydnlmavlQIRDDLsAEQREDRANELMEEFHIEHLRDSMGQSL---------------SGGERRRVEIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2274528008 662 LLLKNPSILFFDEATSALDSYTETELMRNINaNLLSEKRTAIFVAHRLR-TISDSDLIVVLQSGQVAEKGTHAELM 736
Cdd:PRK10895 151 ALAANPKFILLDEPFAGVDPISVIDIKRIIE-HLRDSGLGVLITDHNVReTLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
497-748 |
2.82e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.89 E-value: 2.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 497 KENADAPPLKVTGGEIRFE--NVTfgyHPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQ 574
Cdd:PRK09700 249 RFNAMKENVSNLAHETVFEvrNVT---SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 575 DITKVS-LESLRRHIGVVPQ---DTPLF-NDDIRHNIR-------------YGRLDASD----ADVEAAARAAKVDQIVQ 632
Cdd:PRK09700 326 DISPRSpLDAVKKGMAYITEsrrDNGFFpNFSIAQNMAisrslkdggykgaMGLFHEVDeqrtAENQRELLALKCHSVNQ 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 633 NLPQgyntkvgerglmISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETE---LMRninaNLLSEKRTAIFVAHRL 709
Cdd:PRK09700 406 NITE------------LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEiykVMR----QLADDGKVILMVSSEL 469
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2274528008 710 -RTISDSDLIVVLQSGQVAEKGTH-AELMDRKGLYWDLWQA 748
Cdd:PRK09700 470 pEIITVCDRIAVFCEGRLTQILTNrDDMSEEEIMAWALPQE 510
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
512-726 |
3.61e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 70.50 E-value: 3.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPD----RPIFSNISFAVPAGyktAFV---GPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESL 584
Cdd:COG1101 2 LELKNLSKTFNPGtvneKRALDGLNLTIEEG---DFVtviGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 585 RRHIGVVPQDtPL----------------FNDDIRHNIRYGrLDASDADveaaARAAKVDQIVQNLPQGYNTKVGerglM 648
Cdd:COG1101 79 AKYIGRVFQD-PMmgtapsmtieenlalaYRRGKRRGLRRG-LTKKRRE----LFRELLATLGLGLENRLDTKVG----L 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 649 ISGGekQRLAVArLL---LKNPSILFFDEATSALDSYTETELMrNINANLLSEKR-TAIFVAHRLR-TISDSDLIVVLQS 723
Cdd:COG1101 149 LSGG--QRQALS-LLmatLTKPKLLLLDEHTAALDPKTAALVL-ELTEKIVEENNlTTLMVTHNMEqALDYGNRLIMMHE 224
|
...
gi 2274528008 724 GQV 726
Cdd:COG1101 225 GRI 227
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
186-480 |
4.04e-13 |
|
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: 70.59 E-value: 4.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 186 ALALLVGGKLLNVQVPFFFKAIVDrlnqVVNAPLDMTNPNTVWVvagsAILGYGLARvgaAAFSELRNAVFANVAQQSIR 265
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLID----AALGGGDTASLNQIAL----LLLGLFLLQ---AVFSFFRIYLFARVGERVVA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 266 RVARSVFTHLLALDLGWHLTRQTGGLT----------------------RAIDRGTKGISFL------LTSIVFHIVPTA 317
Cdd:cd18576 70 DLRKDLYRHLQRLPLSFFHERRVGELTsrlsndvtqiqdtltttlaeflRQILTLIGGVVLLffiswkLTLLMLATVPVV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 318 LEISMVCGilsykcgpsfaavtavtmaayawftirttswrTRFRKEANAA-DNRAATTSV--DSLLNYEAVKYFNNEKHE 394
Cdd:cd18576 150 VLVAVLFG--------------------------------RRIRKLSKKVqDELAEANTIveETLQGIRVVKAFTREDYE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 395 IAKYDAALADYEKSSIKVATSLAALNSGQNAIFSTSLTVMMLLAAQGVTNGTMSVGDLVMVNQLVFQLSLPLNFLGTVYR 474
Cdd:cd18576 198 IERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYG 277
|
....*.
gi 2274528008 475 ELRQSL 480
Cdd:cd18576 278 QLQKAL 283
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
510-707 |
4.54e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 72.68 E-value: 4.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 510 GEIRF--ENVTFGYhPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDgqdiTKVSLESLRRH 587
Cdd:PRK11147 316 GKIVFemENVNYQI-DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG----TKLEVAYFDQH 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 588 IGVV-PQDTplfnddIRHNIRYGRldasdADVEAAARAAKVDQIVQNL---PQGYNTKVgeRGLmiSGGEKQRLAVARLL 663
Cdd:PRK11147 391 RAELdPEKT------VMDNLAEGK-----QEVMVNGRPRHVLGYLQDFlfhPKRAMTPV--KAL--SGGERNRLLLARLF 455
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2274528008 664 LKNPSILFFDEATSALDsyTET-ELMRNINANLlseKRTAIFVAH 707
Cdd:PRK11147 456 LKPSNLLILDEPTNDLD--VETlELLEELLDSY---QGTVLLVSH 495
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
512-724 |
4.60e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.51 E-value: 4.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPDRPIfSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLE-SLRRHIGV 590
Cdd:PRK09700 6 ISMAGIGKSFGPVHAL-KSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 591 VPQDTPLFND-DIRHNIRYGRL-----------DASDADVEAAARAAKVDqivqnLPQGYNTKVGErgLMISggEKQRLA 658
Cdd:PRK09700 85 IYQELSVIDElTVLENLYIGRHltkkvcgvniiDWREMRVRAAMMLLRVG-----LKVDLDEKVAN--LSIS--HKQMLE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2274528008 659 VARLLLKNPSILFFDEATSALDSyTETELMRNINANLLSEKRTAIFVAHRLRTISD-SDLIVVLQSG 724
Cdd:PRK09700 156 IAKTLMLDAKVIIMDEPTSSLTN-KEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
512-738 |
8.63e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 70.64 E-value: 8.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKvsLESLRRHIGVV 591
Cdd:PRK11650 4 LKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNE--LEPADRDIAMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 592 PQDTPLF-NDDIRHNIRYG----RLDAS--DADVEAAARAAKVDQIVQNLPqgyntkvgeRGLmiSGGEKQRLAVARLLL 664
Cdd:PRK11650 82 FQNYALYpHMSVRENMAYGlkirGMPKAeiEERVAEAARILELEPLLDRKP---------REL--SGGQRQRVAMGRAIV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 665 KNPSILFFDEATSALDSytetEL---MRninanlLSEKR-------TAIFVAH-RLRTISDSDLIVVLQSGQVAEKGTHA 733
Cdd:PRK11650 151 REPAVFLFDEPLSNLDA----KLrvqMR------LEIQRlhrrlktTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPV 220
|
....*
gi 2274528008 734 ELMDR 738
Cdd:PRK11650 221 EVYEK 225
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
512-730 |
1.01e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.14 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLrrhIGVV 591
Cdd:PRK15056 7 IVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 592 PQDT------PLFNDDIRHNIRYGRLD----ASDADVEAAARA-AKVDQIVQNLPQgyntkVGErglmISGGEKQRLAVA 660
Cdd:PRK15056 84 PQSEevdwsfPVLVEDVVMMGRYGHMGwlrrAKKRDRQIVTAAlARVDMVEFRHRQ-----IGE----LSGGQKKRVFLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 661 RLLLKNPSILFFDEATSALDSYTETELMrNINANLLSEKRTAIFVAHRLRTISDSDLIVVLQSGQVAEKG 730
Cdd:PRK15056 155 RAIAQQGQVILLDEPFTGVDVKTEARII-SLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
530-736 |
2.06e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 68.28 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 530 NISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGVVPQDtPLFNDDIRHniRYG 609
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQD-PSTSLNPRQ--RIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 610 R-LDASDADVEAAARAAKVDQIVQNLPQgyntkVGERG-------LMISGGEKQRLAVARLLLKNPSILFFDEATSALDS 681
Cdd:PRK15112 108 QiLDFPLRLNTDLEPEQREKQIIETLRQ-----VGLLPdhasyypHMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2274528008 682 YTETELmrnINANL-LSEKR--TAIFVAHRLRTISD-SDLIVVLQSGQVAEKGTHAELM 736
Cdd:PRK15112 183 SMRSQL---INLMLeLQEKQgiSYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVL 238
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
525-731 |
2.20e-12 |
|
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: 71.20 E-value: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 525 RPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDItKVSLESLRRHIGVVPQDTPLFNDDI-- 602
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHLTva 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 603 RHNIRYGRLDASDADveaaARAAKVDQIVQNlpQGYNTKVGERGLMISGGEKQRLAVARLLLKNPSILFFDEATSALDSY 682
Cdd:TIGR01257 1022 EHILFYAQLKGRSWE----EAQLEMEAMLED--TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY 1095
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2274528008 683 TEtelmRNINANLLSEK--RTAIFVAHRLrtiSDSDL----IVVLQSGQVAEKGT 731
Cdd:TIGR01257 1096 SR----RSIWDLLLKYRsgRTIIMSTHHM---DEADLlgdrIAIISQGRLYCSGT 1143
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
510-726 |
2.47e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.96 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 510 GEIRFE--NVTfGYHPDRP---IFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQS-GKIYIDGQDIT-KVSLE 582
Cdd:PRK13549 256 GEVILEvrNLT-AWDPVNPhikRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPVKiRNPQQ 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 583 SLRRHIGVVPQD------TPLFndDIRHNI------RYGRLDASDADVEAAAraakVDQIVQNLpqgyntKVGERGLM-- 648
Cdd:PRK13549 335 AIAQGIAMVPEDrkrdgiVPVM--GVGKNItlaaldRFTGGSRIDDAAELKT----ILESIQRL------KVKTASPEla 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 649 ---ISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNINAnLLSEKRTAIFVAHRLRTI-SDSDLIVVLQSG 724
Cdd:PRK13549 403 iarLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQ-LVQQGVAIIVISSELPEVlGLSDRVLVMHEG 481
|
..
gi 2274528008 725 QV 726
Cdd:PRK13549 482 KL 483
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
530-725 |
2.89e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.96 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 530 NISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYkPQ---SGKIYIDGQDITKVSL-ESLRRHIGVVPQDTPLFND-DIRH 604
Cdd:PRK13549 23 NVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIrDTERAGIAIIHQELALVKElSVLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 605 NI-------RYGRLDASDADVEAAARAAKVdqivqNLPQGYNTKVGERGlmisGGEKQRLAVARLLLKNPSILFFDEATS 677
Cdd:PRK13549 102 NIflgneitPGGIMDYDAMYLRAQKLLAQL-----KLDINPATPVGNLG----LGQQQLVEIAKALNKQARLLILDEPTA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2274528008 678 ALdSYTETELMRNINANLLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQ 725
Cdd:PRK13549 173 SL-TESETAVLLDIIRDLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
512-738 |
3.47e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 67.03 E-value: 3.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVT---------------------FGYHPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIY 570
Cdd:COG1134 5 IEVENVSksyrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 571 IDGqditKVS--LEslrrhIGVVpqdtplFNDDI--RHNIR-YGR-LDASDADVEaaaraAKVDQIVQ--NLPQGYNTKV 642
Cdd:COG1134 85 VNG----RVSalLE-----LGAG------FHPELtgRENIYlNGRlLGLSRKEID-----EKFDEIVEfaELGDFIDQPV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 643 GerglMISGGEKQRLAVARLLLKNPSILFFDEATSALD------SYtetELMRninaNLLSEKRTAIFVAHRLRTISD-S 715
Cdd:COG1134 145 K----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDaafqkkCL---ARIR----ELRESGRTVIFVSHSMGAVRRlC 213
|
250 260
....*....|....*....|...
gi 2274528008 716 DLIVVLQSGQVAEKGTHAELMDR 738
Cdd:COG1134 214 DRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
508-726 |
4.17e-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: 69.47 E-value: 4.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 508 TGGEI-RFENVTfGYHPDRP---IFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQ-SGKIYIDGQDI-TKVSL 581
Cdd:TIGR02633 253 IGDVIlEARNLT-CWDVINPhrkRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVdIRNPA 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 582 ESLRRHIGVVPQD------TPLFNddIRHNIRYGRLD--ASDADVEAAARAAKVDQIVQNLpqgyNTKVGERGLMI---S 650
Cdd:TIGR02633 332 QAIRAGIAMVPEDrkrhgiVPILG--VGKNITLSVLKsfCFKMRIDAAAELQIIGSAIQRL----KVKTASPFLPIgrlS 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2274528008 651 GGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNINAnLLSEKRTAIFVAHRL-RTISDSDLIVVLQSGQV 726
Cdd:TIGR02633 406 GGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQ-LAQEGVAIIVVSSELaEVLGLSDRVLVIGEGKL 481
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
512-738 |
4.25e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 69.45 E-value: 4.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLL--FRFYKPQSGKI-----------YID-----G 573
Cdd:TIGR03269 1 IEVKNLTKKFD-GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIiyhvalcekcgYVErpskvG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 574 QDITKV--SLES---------------LRRHIGVVPQDT-PLFNDD------IR--HNIRYGRLDASDADVEAaaraakV 627
Cdd:TIGR03269 80 EPCPVCggTLEPeevdfwnlsdklrrrIRKRIAIMLQRTfALYGDDtvldnvLEalEEIGYEGKEAVGRAVDL------I 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 628 DQivqnlpqgynTKVGERGLMI----SGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNINANLLSEKRTAI 703
Cdd:TIGR03269 154 EM----------VQLSHRITHIardlSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMV 223
|
250 260 270
....*....|....*....|....*....|....*.
gi 2274528008 704 FVAHRLRTISD-SDLIVVLQSGQVAEKGTHAELMDR 738
Cdd:TIGR03269 224 LTSHWPEVIEDlSDKAIWLENGEIKEEGTPDEVVAV 259
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
525-729 |
5.64e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.14 E-value: 5.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 525 RPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITkvsleslrrhigvVPQDTPLFnDDIrh 604
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQ-------------FGREASLI-DAI-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 605 niryGRLDASDADVEAAARAAKVDqivqnlPQGYNTKVGErglmISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTE 684
Cdd:COG2401 107 ----GRKGDFKDAVELLNAVGLSD------AVLWLRRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2274528008 685 TELMRNINANLLSEKRTAIFVAHR---LRTISDSDLIVVLQSGQVAEK 729
Cdd:COG2401 173 KRVARNLQKLARRAGITLVVATHHydvIDDLQPDLLIFVGYGGVPEEK 220
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
398-674 |
6.49e-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: 68.67 E-value: 6.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 398 YDAALADYEKSSIKVATSLAALNSGQNAIFSTSLTVMMLLAAQGVTNGTMSVGDLVMVnqLVFqLSLPL-NFLGTV--YR 474
Cdd:COG4615 214 LQPTAERYRDLRIRADTIFALANNWGNLLFFALIGLILFLLPALGWADPAVLSGFVLV--LLF-LRGPLsQLVGALptLS 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 475 ELRQSLVDMETMFNLENVNVAVKENADAPPLKVTGGEIRFENVTFGYHP--DRPIFS--NISFAVPAGYKTAFVGPSGCG 550
Cdd:COG4615 291 RANVALRKIEELELALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGedGDEGFTlgPIDLTIRRGELVFIVGGNGSG 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 551 KSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGVVPQDTPLFnDDIrhnirYGRLDASDADveaaaraaKVDQI 630
Cdd:COG4615 371 KSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF-DRL-----LGLDGEADPA--------RAREL 436
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2274528008 631 VQNLpqGYNTKVGERG-----LMISGGEKQRLAVARLLLKNPSILFFDE 674
Cdd:COG4615 437 LERL--ELDHKVSVEDgrfstTDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
184-478 |
7.84e-12 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 67.15 E-value: 7.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 184 ALALALLVGGKLLNVQVPFFFKAIVDRL-----NQVVNAPLDMTNPNTVWVVAGSAILGYGLArVGAAAFSELRNAVFAN 258
Cdd:cd18564 2 ALALLALLLETALRLLEPWPLKVVIDDVlgdkpLPGLLGLAPLLGPDPLALLLLAAAALVGIA-LLRGLASYAGTYLTAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 259 VAQQSIRRVARSVFTHLLALDLGWHLTRQTGGL-TRAI-DRGTkgISFLLTSIVFHIVPTALE-ISMVC---------GI 326
Cdd:cd18564 81 VGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLlSRLTgDVGA--IQDLLVSGVLPLLTNLLTlVGMLGvmfwldwqlAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 327 LSYKCGPSFaavtavtmaayaWFTIRTTSWRTRFR-KEANAADNRAATTSVDSLLNYEAVKYFNNEKHEIAKYDAALADY 405
Cdd:cd18564 159 IALAVAPLL------------LLAARRFSRRIKEAsREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKS 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2274528008 406 EKSSIKVATSLAALNSGQNAIFSTSLTVMMLLAAQGVTNGTMSVGDLvmvnqLVFqlslpLNFLGTVYRELRQ 478
Cdd:cd18564 227 LRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDL-----LVF-----LAYLKNLYKPVRD 289
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
516-738 |
7.84e-12 |
|
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: 68.56 E-value: 7.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 516 NVTFG-YHPDRPIFSNISFAVPAGYKTAFVGPSGCGKS----TIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRR---- 586
Cdd:COG4172 13 SVAFGqGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 587 HIGVVPQD-----TPLFN--DDIRHNIR-YGRLDASDADveaaaraakvDQIVQNLpqgynTKVG----ERGL-----MI 649
Cdd:COG4172 93 RIAMIFQEpmtslNPLHTigKQIAEVLRlHRGLSGAAAR----------ARALELL-----ERVGipdpERRLdayphQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 650 SGGEKQRLAVARLLLKNPSILFFDEATSALDSYTET---ELMRNINAnllsEKRTAI-FVAHRL---RTISDSdlIVVLQ 722
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAqilDLLKDLQR----ELGMALlLITHDLgvvRRFADR--VAVMR 231
|
250
....*....|....*.
gi 2274528008 723 SGQVAEKGTHAELMDR 738
Cdd:COG4172 232 QGEIVEQGPTAELFAA 247
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
525-688 |
8.18e-12 |
|
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: 65.21 E-value: 8.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 525 RPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKV--SLESLRRHIGVVPQDTPLFNddI 602
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQrdSIARGLLYLGHAPGIKTTLS--V 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 603 RHNIRYGRLDASDADVEAAaraakVDQI----VQNLPQGYntkvgerglmISGGEKQRLAVARLLLKNPSILFFDEATSA 678
Cdd:cd03231 91 LENLRFWHADHSDEQVEEA-----LARVglngFEDRPVAQ----------LSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170
....*....|
gi 2274528008 679 LDSYTETELM 688
Cdd:cd03231 156 LDKAGVARFA 165
|
|
| cyc_pep_trnsptr |
TIGR01194 |
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ... |
402-726 |
1.78e-11 |
|
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake. [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]
Pssm-ID: 130262 [Multi-domain] Cd Length: 555 Bit Score: 67.29 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 402 LADYEKSSIKVATslAALNSGQnAIFSTSLTVMMLLAAQGVTNGTMSVGDLVMVnqlVFQLSLPLNFLGTVYRELRQSLV 481
Cdd:TIGR01194 226 IADLHIIEILIFI--AAENFGQ-LLFFLLIGCALFAAAMFASIDAAAISAFVLA---LLYIKGPLEMLVSALPILAQAQI 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 482 DMETMFNL-ENVN-------VAVKENADAPPLKVTGGEIRFENVTfgYHPDRPIFSN------ISFAVPAGYKTAFVGPS 547
Cdd:TIGR01194 300 ACQRLADFgERFNepepeleLSDADNVLLLAHDKSVDSIELKDVH--MNPKAPEGSEgfalgpIDLRIAQGDIVFIVGEN 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 548 GCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGVVPQDTPLFNDDIRHNIRYgrlDASDADVEAAARAAKV 627
Cdd:TIGR01194 378 GCGKSTLAKLFCGLYIPQEGEILLDGAAVSADSRDDYRDLFSAIFADFHLFDDLIGPDEGE---HASLDNAQQYLQRLEI 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 628 DQIVQNLPQGYNTKVGerglmISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNINANLLSEKRTAIFVAH 707
Cdd:TIGR01194 455 ADKVKIEDGGFSTTTA-----LSTGQQKRLALICAWLEDRPILLFDEWAADQDPAFKRFFYEELLPDLKRQGKTIIIISH 529
|
330
....*....|....*....
gi 2274528008 708 RLRTISDSDLIVVLQSGQV 726
Cdd:TIGR01194 530 DDQYFELADQIIKLAAGCI 548
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
530-712 |
3.97e-11 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 63.89 E-value: 3.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 530 NISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRhIGVV------------PQDTPL 597
Cdd:cd03267 39 GISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRR-IGVVfgqktqlwwdlpVIDSFY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 598 FNDDIrhnirYgrldasdaDVEAAARAAKVDQIVQNLPQGYNTKVGERGLmiSGGEKQRLAVARLLLKNPSILFFDEATS 677
Cdd:cd03267 118 LLAAI-----Y--------DLPPARFKKRLDELSELLDLEELLDTPVRQL--SLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190
....*....|....*....|....*....|....*
gi 2274528008 678 ALDSYTETELMRNINANLLSEKRTAIFVAHRLRTI 712
Cdd:cd03267 183 GLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDI 217
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
183-470 |
4.56e-11 |
|
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: 64.43 E-value: 4.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 183 VALALALLVGGKLLNVQVPFFFKAIVDRlnqvvnaPLDMTNPNTVWVVAGsAILGYGLARvgaAAFSELRNAVFANVA-- 260
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDG-------PIAHGDRSALWPLVL-LLLALGVAE---AVLSFLRRYLAGRLSlg 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 261 -QQSIRRvarSVFTHLLALDLGWHLTRQTGGL-TRAI-DRGT-----KGISFLLTSIVFHIVPTA--LEISMVCGILSYK 330
Cdd:cd18543 70 vEHDLRT---DLFAHLQRLDGAFHDRWQSGQLlSRATsDLSLvqrflAFGPFLLGNLLTLVVGLVvmLVLSPPLALVALA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 331 CGPSFaavtavtmaayAWFTIRttsWRTRFRKEANAADNRAA--TTSVD-SLLNYEAVKYFNNEKHEIAKYDAALADYEK 407
Cdd:cd18543 147 SLPPL-----------VLVARR---FRRRYFPASRRAQDQAGdlATVVEeSVTGIRVVKAFGRERRELDRFEAAARRLRA 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2274528008 408 SSIKVATSLAALNSGQNAIFSTSLTVMMLLAAQGVTNGTMSVGDLVMVNQLVFQLSLPLNFLG 470
Cdd:cd18543 213 TRLRAARLRARFWPLLEALPELGLAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLG 275
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
512-724 |
5.71e-11 |
|
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: 62.26 E-value: 5.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTF---GYHPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLL-FRfyKPQ---SGKIYIDGQDITKvsleSL 584
Cdd:cd03232 4 LTWKNLNYtvpVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGR--KTAgviTGEILINGRPLDK----NF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 585 RRHIGVVPQ-DTPLFNDDIRHNIRYGrldasdadveaaaraakvdqivQNLpqgyntkvgeRGLmiSGGEKQRLAVARLL 663
Cdd:cd03232 78 QRSTGYVEQqDVHSPNLTVREALRFS----------------------ALL----------RGL--SVEQRKRLTIGVEL 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2274528008 664 LKNPSILFFDEATSALDSYTETELMRNINaNLLSEKRTAIFVAHR--LRTISDSDLIVVLQSG 724
Cdd:cd03232 124 AAKPSILFLDEPTSGLDSQAAYNIVRFLK-KLADSGQAILCTIHQpsASIFEKFDRLLLLKRG 185
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
512-709 |
6.15e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.59 E-value: 6.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFEN--VTFGyhpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQditkvslesLRrhIG 589
Cdd:PRK09544 5 VSLENvsVSFG---QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 590 VVPQDTPLFNDDIRHNIRYGRL--DASDADVEAAARAAKVDQIVQNLPQgyntkvgerglMISGGEKQRLAVARLLLKNP 667
Cdd:PRK09544 71 YVPQKLYLDTTLPLTVNRFLRLrpGTKKEDILPALKRVQAGHLIDAPMQ-----------KLSGGETQRVLLARALLNRP 139
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2274528008 668 SILFFDEATSALDSYTETELMRNINaNLLSEKRTAIF-VAHRL 709
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLID-QLRRELDCAVLmVSHDL 181
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
531-736 |
7.35e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.03 E-value: 7.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 531 ISFAVPAGYKTAFVGPSGCGKSTifrLLFRF--YKPQSGKIYIDGQDITKVSLESLRRHIG-VVPQDTPLFNDDIRHnir 607
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMagLLPGSGSIQFAGQPLEAWSAAELARHRAyLSQQQTPPFAMPVFQ--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 608 YgrLDASDAD-VEAAARAAKVDQIVQNLpqGYNTKVGERGLMISGGEKQRLAVARLLLK-----NPS--ILFFDEATSAL 679
Cdd:PRK03695 89 Y--LTLHQPDkTRTEAVASALNEVAEAL--GLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdiNPAgqLLLLDEPMNSL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2274528008 680 DSYTETELMRNINAnLLSEKRTAIFVAHRL-RTISDSDLIVVLQSGQVAEKGTHAELM 736
Cdd:PRK03695 165 DVAQQAALDRLLSE-LCQQGIAVVMSSHDLnHTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
524-736 |
1.06e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 65.29 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 524 DRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQS--GKIYIDGQDITKVSLeslrRHIGVVPQDTPLF-ND 600
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQIL----KRTGFVTQDDILYpHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 601 DIRHNIRYGRLDASDADVEAAARAAKVDQIVQNL--PQGYNTKVGE---RGlmISGGEKQRLAVARLLLKNPSILFFDEA 675
Cdd:PLN03211 156 TVRETLVFCSLLRLPKSLTKQEKILVAESVISELglTKCENTIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2274528008 676 TSALDSYTETELMRNInANLLSEKRTAIFVAHR--LRTISDSDLIVVLQSGQVAEKGTHAELM 736
Cdd:PLN03211 234 TSGLDATAAYRLVLTL-GSLAQKGKTIVTSMHQpsSRVYQMFDSVLVLSEGRCLFFGKGSDAM 295
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
524-735 |
1.12e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 64.73 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 524 DRPIFSNISFAVPAGYKTAFVGPSGCGKS----TIFRLLfrfykPQ------SGKIYIDGQDITKVSLESLRR----HIG 589
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLL-----PSppvvypSGDIRFHGESLLHASEQTLRGvrgnKIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 590 VVPQDtPLFNDDIRHNI-----------RYGRLDASDADVEAAARAAKVDQIVQNL---PQgyntkvgerglMISGGEKQ 655
Cdd:PRK15134 96 MIFQE-PMVSLNPLHTLekqlyevlslhRGMRREAARGEILNCLDRVGIRQAAKRLtdyPH-----------QLSGGERQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 656 RLAVARLLLKNPSILFFDEATSALDSYTET-------ELMRNINANLLsekrtaiFVAHRL---RTISDSdlIVVLQSGQ 725
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDVSVQAqilqllrELQQELNMGLL-------FITHNLsivRKLADR--VAVMQNGR 234
|
250
....*....|
gi 2274528008 726 VAEKGTHAEL 735
Cdd:PRK15134 235 CVEQNRAATL 244
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
516-680 |
1.61e-10 |
|
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: 64.19 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 516 NVTFGYHPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLfrfykpqSGkiyIDgQDITKVSLESLRRHIGVVPQDT 595
Cdd:TIGR03719 9 RVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AG---VD-KDFNGEARPQPGIKVGYLPQEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 596 PL-FNDDIRHNIRYG---------RLDA-------SDADVEA-AARAAKVDQIVQN------------------LPQGyN 639
Cdd:TIGR03719 78 QLdPTKTVRENVEEGvaeikdaldRFNEisakyaePDADFDKlAAEQAELQEIIDAadawdldsqleiamdalrCPPW-D 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2274528008 640 TKVGErglmISGGEKQRLAVARLLLKNPSILFFDEATSALD 680
Cdd:TIGR03719 157 ADVTK----LSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
521-730 |
1.84e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 62.17 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 521 YHPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQ-----SGKIYIDGQDI--TKVSLESLRRHIGVV-- 591
Cdd:PRK14267 13 YYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPIEVRREVGMVfq 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 592 -PQDTPLFN--DDIRHNIRYGRLDAS----DADVEAAARAAKVDQIVQNLPQGYNTKvgerglmISGGEKQRLAVARLLL 664
Cdd:PRK14267 93 yPNPFPHLTiyDNVAIGVKLNGLVKSkkelDERVEWALKKAALWDEVKDRLNDYPSN-------LSGGQRQRLVIARALA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2274528008 665 KNPSILFFDEATSALDSYTETELMRNINAnlLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQVAEKG 730
Cdd:PRK14267 166 MKPKILLMDEPTANIDPVGTAKIEELLFE--LKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVG 230
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
186-480 |
1.85e-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: 62.56 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 186 ALALLVGGKLLNVQVPFFfkaivdrLNQVVNAPLDMTNPNTVWvvagSAILGYGLARVGAAAFSELRNAVFANVAQQSIR 265
Cdd:cd18572 1 AFVFLVVAALSELAIPHY-------TGAVIDAVVADGSREAFY----RAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 266 RVARSVFTHLLALDLGWHLTRQTGGLT----------------------RAIDRGTKGISFL------LTSIVFHIVPTa 317
Cdd:cd18572 70 RLRRDLFRSLLRQDIAFFDATKTGELTsrltsdcqkvsdplstnlnvflRNLVQLVGGLAFMfslswrLTLLAFITVPV- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 318 leISMVCGIlsykcgpsfaavtavtmaaYAWFTiRTTSWRTRfrkEANAADNRAATtsvDSLLNYEAVKYFNNEKHEIAK 397
Cdd:cd18572 149 --IALITKV-------------------YGRYY-RKLSKEIQ---DALAEANQVAE---EALSNIRTVRSFATEEREARR 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 398 YDAALADYEKSSIKVAtSLAALNSGQNAIFSTSLTVMMLL-AAQGVTNGTMSVGDLVMVNQLVFQLSLPLNFLGTVYREL 476
Cdd:cd18572 201 YERALDKALKLSVRQA-LAYAGYVAVNTLLQNGTQVLVLFyGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSL 279
|
....
gi 2274528008 477 RQSL 480
Cdd:cd18572 280 MQAV 283
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
529-729 |
2.03e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.87 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 529 SNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDIT----KVSLESlrrHIGVVPQDTPLF-NDDIR 603
Cdd:PRK10762 21 SGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpKSSQEA---GIGIIHQELNLIpQLTIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 604 HNI--------RYGRLDASDADVEAAARAAKVdqivqNLPQGYNTKVGErglmISGGEKQRLAVARLLLKNPSILFFDEA 675
Cdd:PRK10762 98 ENIflgrefvnRFGRIDWKKMYAEADKLLARL-----NLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2274528008 676 TSALDSyTETE-LMRNINaNLLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQ-VAEK 729
Cdd:PRK10762 169 TDALTD-TETEsLFRVIR-ELKSQGRGIVYISHRLKEIFEiCDDVTVFRDGQfIAER 223
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
530-736 |
2.84e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 61.43 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 530 NISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITK-VSLESLRRHIGVVPQDTPLFND-DIRHNIR 607
Cdd:PRK11614 23 EVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKIMREAVAIVPEGRRVFSRmTVEENLA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 608 YGRLDAsdadvEAAARAAKVDQIVQNLPQGYNTKVGERGLMiSGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETEL 687
Cdd:PRK11614 103 MGGFFA-----ERDQFQERIKWVYELFPRLHERRIQRAGTM-SGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2274528008 688 MRNINAnlLSEKRTAIFVAHR--LRTISDSDLIVVLQSGQVAEKGTHAELM 736
Cdd:PRK11614 177 FDTIEQ--LREQGMTIFLVEQnaNQALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
527-728 |
3.82e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 60.56 E-value: 3.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 527 IFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLE---SLR-RHIGVVPQD---TPLFN 599
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQSfmlIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 600 ddIRHNIRYGRLDASDADVEAAaraakvDQIVQNLPQ-GYNTKVGERGLMISGGEKQRLAVARLLLKNPSILFFDEATSA 678
Cdd:PRK10584 105 --ALENVELPALLRGESSRQSR------NGAKALLEQlGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2274528008 679 LDSYTE---TELMRNINANLLSekrTAIFVAHRLRTISDSDLIVVLQSGQVAE 728
Cdd:PRK10584 177 LDRQTGdkiADLLFSLNREHGT---TLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
184-486 |
5.53e-10 |
|
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: 61.31 E-value: 5.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 184 ALALALLVGgkLLNVQVPFFFKAIVDRLnqvvnapLDMTNPNTVWVVAGSAILGYgLARVGaaaFSELRNAVFANVAQQS 263
Cdd:cd18570 7 ILLLSLLIT--LLGIAGSFFFQILIDDI-------IPSGDINLLNIISIGLILLY-LFQSL---LSYIRSYLLLKLSQKL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 264 IRRVARSVFTHLLALDLGWHLTRQTGGLT-RAIDrgTKGISFLLTSIVFHIVptaLEISMVC--GILSYKCGPSFAAVTA 340
Cdd:cd18570 74 DIRLILGYFKHLLKLPLSFFETRKTGEIIsRFND--ANKIREAISSTTISLF---LDLLMVIisGIILFFYNWKLFLITL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 341 VTMAAYAWFTIRTtswRTRFRKEANAA-DNRAATTS--VDSLLNYEAVKYFNNEKHEIAKYDAALADYEKSSIKVATsLA 417
Cdd:cd18570 149 LIIPLYILIILLF---NKPFKKKNREVmESNAELNSylIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGK-LS 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 418 ALNSGQNAIFSTSLTVMML-LAAQGVTNGTMSVGDLVMVNQLVFQLSLPLNFLGTVYRELRQSLVDMETM 486
Cdd:cd18570 225 NLQSSIKGLISLIGSLLILwIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
512-736 |
6.42e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 62.51 E-value: 6.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHP-DRPIF---SNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYI----DGQDITKVSLES 583
Cdd:TIGR03269 280 IKVRNVSKRYISvDRGVVkavDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 584 ---LRRHIGVVPQDTPLF-NDDIRHNI----------RYGRLDASDADVEAAARAAKVDQIVQNLPQgyntkvgerglMI 649
Cdd:TIGR03269 360 rgrAKRYIGILHQEYDLYpHRTVLDNLteaiglelpdELARMKAVITLKMVGFDEEKAEEILDKYPD-----------EL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 650 SGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNINANLLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQVAE 728
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVK 508
|
....*...
gi 2274528008 729 KGTHAELM 736
Cdd:TIGR03269 509 IGDPEEIV 516
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
538-721 |
6.70e-10 |
|
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: 62.49 E-value: 6.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 538 GYKTAFVGPSGCGKSTIFRLLFRFYKPQSGkIYIDGQDITKVslesLRRHIGVVPQD--TPLFNDDIR--HNIRYgrlda 613
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELKPNLG-DYDEEPSWDEV----LKRFRGTELQDyfKKLANGEIKvaHKPQY----- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 614 sdadveaaaraakVDQIvqnlPQGYNTKVG-------ERGLM-------------------ISGGEKQRLAVARLLLKNP 667
Cdd:COG1245 169 -------------VDLI----PKVFKGTVRellekvdERGKLdelaeklglenildrdiseLSGGELQRVAIAAALLRDA 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2274528008 668 SILFFDEATSALDSYTETELMRNINaNLLSEKRTAIFVAHRLrTISD--SDLIVVL 721
Cdd:COG1245 232 DFYFFDEPSSYLDIYQRLNVARLIR-ELAEEGKYVLVVEHDL-AILDylADYVHIL 285
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
183-481 |
7.18e-10 |
|
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: 60.90 E-value: 7.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 183 VALALALLVGGKLLNVQVPFFFKAIVDRLnqvvnapLDMTNPNTVWVVAGsAILGYGLARvGAAAFseLRNAVFANVAQQ 262
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDI-------FVEKDLEALLLVPL-AIIGLFLLR-GLASY--LQTYLMAYVGQR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 263 SIRRVARSVFTHLLALDLGWHLTRQTGGL-----------TRAIDRGTKG-----------------ISFLLTSIVFHIV 314
Cdd:cd18552 70 VVRDLRNDLFDKLLRLPLSFFDRNSSGDLisritndvnqvQNALTSALTVlvrdpltvigllgvlfyLDWKLTLIALVVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 315 PtaleismVCGILSYKCGpsfaavtavtmaayawftirttswrTRFRKEANAADNRAAT-TSV--DSLLNYEAVKYFNNE 391
Cdd:cd18552 150 P-------LAALPIRRIG-------------------------KRLRKISRRSQESMGDlTSVlqETLSGIRVVKAFGAE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 392 KHEIAKYDAALADYEKSSIKVATSLAALNSGQNAIFSTSLTVMMLLAAQGVTNGTMSVGDLVMVNQLVFQLSLPLNFLGT 471
Cdd:cd18552 198 DYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSN 277
|
330
....*....|
gi 2274528008 472 VYRELRQSLV 481
Cdd:cd18552 278 VNANLQRGLA 287
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
512-707 |
1.04e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.87 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKI---------YID---------- 572
Cdd:TIGR03719 323 IEAENLTKAFG-DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIeigetvklaYVDqsrdaldpnk 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 573 --------GQDITKV---SLESlRRHIGvvpqdtplfnddiRHNIRYGrldasdadveaaaraakvDQivqnlpqgyNTK 641
Cdd:TIGR03719 402 tvweeisgGLDIIKLgkrEIPS-RAYVG-------------RFNFKGS------------------DQ---------QKK 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2274528008 642 VGErglmISGGEKQRLAVARLLLKNPSILFFDEATSALDsyteTELMRNINANLLSEKRTAIFVAH 707
Cdd:TIGR03719 441 VGQ----LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD----VETLRALEEALLNFAGCAVVISH 498
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
524-680 |
1.37e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 58.66 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 524 DRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSlESLRR-------HIGVVPQDTP 596
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR-DEYHQdllylghQPGIKTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 597 LFNDDIRHNIRyGRLDAsdadveaaaraakvDQIVQNLpqgynTKVGERGLM------ISGGEKQRLAVARLLLKNPSIL 670
Cdd:PRK13538 92 LENLRFYQRLH-GPGDD--------------EALWEAL-----AQVGLAGFEdvpvrqLSAGQQRRVALARLWLTRAPLW 151
|
170
....*....|
gi 2274528008 671 FFDEATSALD 680
Cdd:PRK13538 152 ILDEPFTAID 161
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
183-484 |
1.39e-09 |
|
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: 60.09 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 183 VALALALLVGGKLLNVQVPFFFKAIVDrlNQVVNAPLDMtnpNTVWVVAgsaiLGYGLARVGAAAFSELRNAVFANVAQQ 262
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAID--DYIVPGQGDL---QGLLLLA----LLYLGLLLLSFLLQYLQTYLLQKLGQR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 263 SIRRVARSVFTHLLALDLGWHLTRQTGGL-TRAI-DrgTKGISFLLTSIVFHIVptaLEISMVCGILSykcgpsfaavta 340
Cdd:cd18544 72 IIYDLRRDLFSHIQRLPLSFFDRTPVGRLvTRVTnD--TEALNELFTSGLVTLI---GDLLLLIGILI------------ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 341 vtmaayAWFTIrttSWR---------------TR-FRKEANAA--DNRAATTSVDSLLNyEA------VKYFNNEKHEIA 396
Cdd:cd18544 135 ------AMFLL---NWRlalisllvlpllllaTYlFRKKSRKAyrEVREKLSRLNAFLQ-ESisgmsvIQLFNREKREFE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 397 KYDAALADYEKSSIKVATSLAALNSGQNAIFSTSLTVMMLLAAQGVTNGTMSVGDLVMVNQLVFQLSLPLNFLGTVYREL 476
Cdd:cd18544 205 EFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNIL 284
|
....*...
gi 2274528008 477 RQSLVDME 484
Cdd:cd18544 285 QSAMASAE 292
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
511-674 |
1.56e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 61.14 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 511 EIRFENVTFGYHPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIGV 590
Cdd:PRK10522 322 TLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 591 VPQDTPLFNddirhnirygRL---DASDADVEAaaraakVDQIVQNLpqGYNTKVGERG-----LMISGGEKQRLAVARL 662
Cdd:PRK10522 402 VFTDFHLFD----------QLlgpEGKPANPAL------VEKWLERL--KMAHKLELEDgrisnLKLSKGQKKRLALLLA 463
|
170
....*....|..
gi 2274528008 663 LLKNPSILFFDE 674
Cdd:PRK10522 464 LAEERDILLLDE 475
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
538-721 |
1.82e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.98 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 538 GYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKiYIDGQDITKVslesLRRHIGVVPQD--TPLFNDDIR--HNIRYgrlda 613
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGELIPNLGD-YEEEPSWDEV----LKRFRGTELQNyfKKLYNGEIKvvHKPQY----- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 614 sdadveaaaraakVDQIvqnlPQGYNTKVG-------ERGLM-------------------ISGGEKQRLAVARLLLKNP 667
Cdd:PRK13409 169 -------------VDLI----PKVFKGKVRellkkvdERGKLdevverlglenildrdiseLSGGELQRVAIAAALLRDA 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2274528008 668 SILFFDEATSALDSYTETELMRNINAnlLSEKRTAIFVAHRLrTISD--SDLIVVL 721
Cdd:PRK13409 232 DFYFFDEPTSYLDIRQRLNVARLIRE--LAEGKYVLVVEHDL-AVLDylADNVHIA 284
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
502-735 |
2.17e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 58.85 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 502 APPLKVTGGEIRF------ENVTFGYHPDRpIFSNIsfavpagyktafvGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQD 575
Cdd:PRK11300 3 QPLLSVSGLMMRFggllavNNVNLEVREQE-IVSLI-------------GPNGAGKTTVFNCLTGFYKPTGGTILLRGQH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 576 ITKVSLESLRRHiGVVP--QDTPLFND----------DIRH---NIRYGRLDASD---ADVEAAARAAK-VDQIvqNLPQ 636
Cdd:PRK11300 69 IEGLPGHQIARM-GVVRtfQHVRLFREmtvienllvaQHQQlktGLFSGLLKTPAfrrAESEALDRAATwLERV--GLLE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 637 GYNTKVGErglmISGGEKQRLAVARLLLKNPSILFFDEATSALDSyTETELMRNINANLLSEKRTAI-FVAHRLRTISD- 714
Cdd:PRK11300 146 HANRQAGN----LAYGQQRRLEIARCMVTQPEILMLDEPAAGLNP-KETKELDELIAELRNEHNVTVlLIEHDMKLVMGi 220
|
250 260
....*....|....*....|.
gi 2274528008 715 SDLIVVLQSGQVAEKGTHAEL 735
Cdd:PRK11300 221 SDRIYVVNQGTPLANGTPEEI 241
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
535-721 |
2.51e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 58.53 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 535 VPA-GYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKiYIDGQDITKVslesLRRHIGVVPQD--TPLFNDDIRHNIRYGRL 611
Cdd:cd03236 22 VPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGK-FDDPPDWDEI----LDEFRGSELQNyfTKLLEGDVKVIVKPQYV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 612 D----ASDADV----EAAARAAKVDQIVQNLPQgynTKVGERGL-MISGGEKQRLAVARLLLKNPSILFFDEATSALDSY 682
Cdd:cd03236 97 DlipkAVKGKVgellKKKDERGKLDELVDQLEL---RHVLDRNIdQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2274528008 683 TETELMRNINaNLLSEKRTAIFVAHRLrTISD--SDLIVVL 721
Cdd:cd03236 174 QRLNAARLIR-ELAEDDNYVLVVEHDL-AVLDylSDYIHCL 212
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
544-731 |
2.89e-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: 58.57 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 544 VGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITkvsleslrrhigVVPQ----DTPLFNDDIRHNIRYGRLDASDADVE 619
Cdd:cd03237 31 LGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS------------YKPQyikaDYEGTVRDLLSSITKDFYTHPYFKTE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 620 AAARAaKVDQIV-QNLPQgyntkvgerglmISGGEKQRLAVARLLLKNPSILFFDEATSALDSytETELM--RNINANLL 696
Cdd:cd03237 99 IAKPL-QIEQILdREVPE------------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDV--EQRLMasKVIRRFAE 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 2274528008 697 SEKRTAIFVAHRLRTISD-SDLIVVLqSGQVAEKGT 731
Cdd:cd03237 164 NNEKTAFVVEHDIIMIDYlADRLIVF-EGEPSVNGV 198
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
523-683 |
4.20e-09 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 57.27 E-value: 4.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 523 PDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLL----FRFYKPqSGKIYIDGQDItKVSLESLRRHIGVVPQDtplf 598
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrtEGNVSV-EGDIHYNGIPY-KEFAEKYPGEIIYVSEE---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 599 nDDIRHNIRYGR-LDASdadveaaaRAAKVDQIVqnlpqgyntkvgeRGlmISGGEKQRLAVARLLLKNPSILFFDEATS 677
Cdd:cd03233 92 -DVHFPTLTVREtLDFA--------LRCKGNEFV-------------RG--ISGGERKRVSIAEALVSRASVLCWDNSTR 147
|
....*.
gi 2274528008 678 ALDSYT 683
Cdd:cd03233 148 GLDSST 153
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
530-725 |
4.84e-09 |
|
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: 59.45 E-value: 4.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 530 NISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYkPQ---SGKIYIDGQDITKVSL-ESLRRHIGVVPQDTPLFND----- 600
Cdd:TIGR02633 19 GIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIrDTERAGIVIIHQELTLVPElsvae 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 601 ------DIRHNIRYGRLDASDADVEAAARAAKVDQIVQNLPqgyntkVGERGlmisGGEKQRLAVARLLLKNPSILFFDE 674
Cdd:TIGR02633 98 niflgnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRP------VGDYG----GGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2274528008 675 ATSALdSYTETELMRNINANLLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQ 725
Cdd:TIGR02633 168 PSSSL-TEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQ 218
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
524-743 |
6.90e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 57.34 E-value: 6.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 524 DRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRF--YKPQSGKIYIDGQDITKVSLEsLRRHIGVV-----PQDTP 596
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLGIFlafqyPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 597 -LFNDD---IRHNIRYGRLDASDAD-VEAAARAAKVDQIVQNLPQGYNTKVGErGLmiSGGEKQRLAVARLLLKNPSILF 671
Cdd:CHL00131 98 gVSNADflrLAYNSKRKFQGLPELDpLEFLEIINEKLKLVGMDPSFLSRNVNE-GF--SGGEKKRNEILQMALLDSELAI 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2274528008 672 FDEATSALDSYTETELMRNINaNLLSEKRTAIFVAH--RLRTISDSDLIVVLQSGQVAEKG--THAELMDRKGLYW 743
Cdd:CHL00131 175 LDETDSGLDIDALKIIAEGIN-KLMTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGdaELAKELEKKGYDW 249
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
195-484 |
7.32e-09 |
|
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: 57.96 E-value: 7.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 195 LLNVQVPFFFKAIVDRlnqVVNAPldmtNPNTVWVVAGsAILGYGLARVgaaAFSELRNAVFANVAQQSIRRVARSVFTH 274
Cdd:cd18568 16 LLGLALPLFTQIILDR---VLVHK----NISLLNLILI-GLLIVGIFQI---LLSAVRQYLLDYFANRIDLSLLSDFYKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 275 LLALDLGWHLTRQTGGLTRAIDRGTKGISFLLTSIVFhivpTALEISMV--CGILSYKCGPSFAAVTAVTMAAYAWFTIR 352
Cdd:cd18568 85 LLSLPLSFFASRKVGDIITRFQENQKIRRFLTRSALT----TILDLLMVfiYLGLMFYYNLQLTLIVLAFIPLYVLLTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 353 TTSWRTRFRKEANAADNRAATTSVDSLLNYEAVKYFNNEKHEIAKYDAALADYEKSSIKVATSLAALNSGQNAIFSTSLT 432
Cdd:cd18568 161 SSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLGTI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2274528008 433 VMMLLAAQGVTNGTMSVGDLVMVNQLVFQLSLPLNFLGTVYRELRQSLVDME 484
Cdd:cd18568 241 AVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVE 292
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
385-472 |
1.12e-08 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 57.02 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 385 VKYFNNEKHEIAKYDAALADYEKSSIKVATSLAALNSGQNAIFSTSLTVMMLLAAQGVTNGTMSVGDLVMVNQLVFQLSL 464
Cdd:cd18548 191 IRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLVAFINYLMQILM 270
|
....*...
gi 2274528008 465 PLNFLGTV 472
Cdd:cd18548 271 SLMMLSMV 278
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
512-680 |
1.32e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 58.33 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYhPDRPI-FSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIY--------------IDGQDI 576
Cdd:PLN03073 509 ISFSDASFGY-PGGPLlFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFrsakvrmavfsqhhVDGLDL 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 577 TKVSLESLRRHIGVVPQDTplfnddIR-HNIRYGrldasdadveaaaraakvdqIVQNLP-QGYNTkvgerglmISGGEK 654
Cdd:PLN03073 588 SSNPLLYMMRCFPGVPEQK------LRaHLGSFG--------------------VTGNLAlQPMYT--------LSGGQK 633
|
170 180
....*....|....*....|....*.
gi 2274528008 655 QRLAVARLLLKNPSILFFDEATSALD 680
Cdd:PLN03073 634 SRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
187-480 |
3.04e-08 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 56.10 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 187 LALLVGGkLLNVQVPFFFKAIVDrlnQVVNAPLDMTNPNTVWVvaGSAILGYGLARVGAAAFSELRNAVFANVAQQSIRR 266
Cdd:cd18780 3 IALLVSS-GTNLALPYFFGQVID---AVTNHSGSGGEEALRAL--NQAVLILLGVVLIGSIATFLRSWLFTLAGERVVAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 267 VARSVFTHLLALDLGWHLTRQTGGLTRAIDRGTK--------GISFLLTSIV---------FHIVP--TALEISMVCGIL 327
Cdd:cd18780 77 LRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQvlqnavtvNLSMLLRYLVqiigglvfmFTTSWklTLVMLSVVPPLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 328 sykcgpsfaavtaVTMAAYAWFtIRTtswrtrFRKEANAADNRAATTSVDSLLNYEAVKYFNNEKHEIAKYDAALADYEK 407
Cdd:cd18780 157 -------------IGAVIYGKY-VRK------LSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYL 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2274528008 408 SSIKVATSLAALNSGQNAIFSTSLTVMMLLAAQGVTNGTMSVGDLVMVNQLVFQLSLPLNFLGTVYRELRQSL 480
Cdd:cd18780 217 LGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAV 289
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
521-680 |
3.98e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.67 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 521 YHPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDgQDITkvsleslrrhIGVVPQDTPLFND 600
Cdd:PRK11819 16 VPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPA-PGIK----------VGYLPQEPQLDPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 601 -DIRHNI------------RY---------------------GRL----DASDA-DVEAaaraaKVDQIVQ--NLPQGyN 639
Cdd:PRK11819 85 kTVRENVeegvaevkaaldRFneiyaayaepdadfdalaaeqGELqeiiDAADAwDLDS-----QLEIAMDalRCPPW-D 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2274528008 640 TKVGErglmISGGEKQRLAVARLLLKNPSILFFDEATSALD 680
Cdd:PRK11819 159 AKVTK----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
183-480 |
3.99e-08 |
|
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: 55.52 E-value: 3.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 183 VALALALLVGGKLLNVQVPFFFKAIVDRLNQvvnaplDMTNPNTVWVVAGSAILGyglarvgaAAFSELRNAVFANVAQQ 262
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSA------GGSSGGLLALLVALFLLQ--------AVLSALSSYLLGRTGER 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 263 SIRRVARSVFTHLLALDLGWHLTRQTGGL-TRAI-DrgTKGISFLLTSIVFHIVPTALeisMVCGILsykcgpsfaavta 340
Cdd:cd18551 67 VVLDLRRRLWRRLLRLPVSFFDRRRSGDLvSRVTnD--TTLLRELITSGLPQLVTGVL---TVVGAV------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 341 vtmaaYAWFTIrttSWR--------------------TRFRKEANAADNRAATTSVD---SLLNYEAVKYFNNEKHEIAK 397
Cdd:cd18551 129 -----VLMFLL---DWVltlvtlavvplafliilplgRRIRKASKRAQDALGELSAAlerALSAIRTVKASNAEERETKR 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 398 YDAALADYEKSSIKVATSLAALNSGQNAIFSTSLTVMMLLAAQGVTNGTMSVGDLV---MvnqLVFQLSLPLNFLGTVYR 474
Cdd:cd18551 201 GGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGVGGARVASGALTVGTLVaflL---YLFQLITPLSQLSSFFT 277
|
....*.
gi 2274528008 475 ELRQSL 480
Cdd:cd18551 278 QLQKAL 283
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
186-452 |
5.01e-08 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 55.21 E-value: 5.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 186 ALALLVGGKLLNVQVPFFFKAIVDRLNQVVNAPLDMT-NPNTVwvvagSAILGyGLARVGAAAFSeLRNAVFANVAQQSI 264
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDVASKESGDIEIFGlSLKTF-----ALALL-GVFVVGAAANF-GRVYLLRIAGERIV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 265 RRVARSVFTHLLALDLGWHLTRQTGGLT----------------------RAIDRGTKGISFL------LTSIVFHIVPT 316
Cdd:cd18573 74 ARLRKRLFKSILRQDAAFFDKNKTGELVsrlssdtsvvgksltqnlsdglRSLVSGVGGIGMMlyispkLTLVMLLVVPP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 317 ALEISMVCGILsykcgpsfaavtavtmaayawftIRTTSWRTRfrkeanaaDNRAATTSV--DSLLNYEAVKYFNNEKHE 394
Cdd:cd18573 154 IAVGAVFYGRY-----------------------VRKLSKQVQ--------DALADATKVaeERLSNIRTVRAFAAERKE 202
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2274528008 395 IAKYDAALADYEKSSIKVATSlaalnsgqNAIFSTS------LTVMMLLAAQG--VTNGTMSVGDL 452
Cdd:cd18573 203 VERYAKKVDEVFDLAKKEALA--------SGLFFGStgfsgnLSLLSVLYYGGslVASGELTVGDL 260
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
185-484 |
5.10e-08 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 55.29 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 185 LALALLVggKLLNVQVPFFFKAIVDRLnqvvnapLDMTNPNTVWVVAgsaiLGYGLARVGAAAFSELRNAVFANVAQQSI 264
Cdd:cd18782 8 LALSFVV--QLLGLANPLLFQVIIDKV-------LVQQDLATLYVIG----VVMLVAALLEAVLTALRTYLFTDTANRID 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 265 RRVARSVFTHLLALDLGWHLTRQTGGLTRAIDRGTKGISFL-------LTSIVFHIVPTA--LEISMVCGILSYKCGPSF 335
Cdd:cd18782 75 LELGGTIIDHLLRLPLGFFDKRPVGELSTRISELDTIRGFLtgtalttLLDVLFSVIYIAvlFSYSPLLTLVVLATVPLQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 336 AAVtavtmaayAWFTIRTTswRTRFRKeanAADNRAATTS--VDSLLNYEAVKYFNNEKHEIAKYDAALADYEKSSIKVA 413
Cdd:cd18782 155 LLL--------TFLFGPIL--RRQIRR---RAEASAKTQSylVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLT 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2274528008 414 TSLAALNSGQNAIFSTSLTVMMLLAAQGVTNGTMSVGDLVMVNQLVFQLSLPLNFLGTVYRELRQSLVDME 484
Cdd:cd18782 222 VLGTTSGSLSQFLNKLSSLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVSLE 292
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
183-481 |
6.90e-08 |
|
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: 54.80 E-value: 6.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 183 VALALALLVGGKLLNVQVPFFFKAIVDR--LNQvvNAPLdmtnpnTVWVVAGSAILGyglarVGAAAFSELRNAVFANVA 260
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDalPQG--DLGL------LVLLALGMVAVA-----VASALLGVVQTYLSARIG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 261 QQSIRRVARSVFTHLLALDLGWHLTRQTG-----------GLTRAIdrgTKGISFLLTSIVfhIVPTALeISMVcgILSY 329
Cdd:cd18550 68 QGVMYDLRVQLYAHLQRMSLAFFTRTRTGeiqsrlnndvgGAQSVV---TGTLTSVVSNVV--TLVATL-VAML--ALDW 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 330 KCG-------PSFaavtavtmaayAWFTIRTTSWR---TRFRKEANAADNRAA--TTSVD-SLLnyeaVKYFNNEKHEIA 396
Cdd:cd18550 140 RLAllslvllPLF-----------VLPTRRVGRRRrklTREQQEKLAELNSIMqeTLSVSgALL----VKLFGREDDEAA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 397 KYDAALADYEKSSIKVATSLAALNSGQNAIFSTSLTVMMLLAAQGVTNGTMSVGDLVMVNQLVFQLSLPLNFLGTVYREL 476
Cdd:cd18550 205 RFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDL 284
|
....*
gi 2274528008 477 RQSLV 481
Cdd:cd18550 285 MTSLA 289
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
512-731 |
7.52e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 54.25 E-value: 7.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHPDRPIFSnISFAVPAGYKTAFVGPSGCGKSTIFRLLfrfykpqSGKIYIDGQDITKVSL---------- 581
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHA-VDLNIHHGEMVALLGPSGSGKSTLLRHL-------SGLITGDKSAGSHIELlgrtvqregr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 582 -----ESLRRHIGVVPQDTPLFND-DIRHNIRYGRLDASD--ADVEAAARAAKVDQIVQNLpqgynTKVG------ERGL 647
Cdd:PRK09984 77 lardiRKSRANTGYIFQQFNLVNRlSVLENVLIGALGSTPfwRTCFSWFTREQKQRALQAL-----TRVGmvhfahQRVS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 648 MISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTE---TELMRNINANllsEKRTAIFVAHRLR-TISDSDLIVVLQS 723
Cdd:PRK09984 152 TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESArivMDTLRDINQN---DGITVVVTLHQVDyALRYCERIVALRQ 228
|
....*...
gi 2274528008 724 GQVAEKGT 731
Cdd:PRK09984 229 GHVFYDGS 236
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
530-742 |
7.87e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 54.71 E-value: 7.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 530 NISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVSLEsLRRHIGVV------------PQDTPL 597
Cdd:COG4586 40 DISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKE-FARRIGVVfgqrsqlwwdlpAIDSFR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 598 FNDDI--------RHNIRY--GRLDASDadveaaaraaKVDQIVQNLpqgyntkvgerglmiSGGEKQR--LAVArlLLK 665
Cdd:COG4586 119 LLKAIyripdaeyKKRLDElvELLDLGE----------LLDTPVRQL---------------SLGQRMRceLAAA--LLH 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 666 NPSILFFDEATSALDSYTET---ELMRNINAnllsEKRTAIFVA-HRLRTISD-SDLIVVLQSGQVAEKGTHAELMDRKG 740
Cdd:COG4586 172 RPKILFLDEPTIGLDVVSKEairEFLKEYNR----ERGTTILLTsHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFG 247
|
..
gi 2274528008 741 LY 742
Cdd:COG4586 248 PY 249
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
530-719 |
9.42e-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: 52.71 E-value: 9.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 530 NISFAVPAGYKTAFVGPSGCGKSTifrLLFRFYKPQSGKIYIDG----QDITKVSLESLRRHIGVvpqdtplfnddirhN 605
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKST---LVNEGLYASGKARLISFlpkfSRNKLIFIDQLQFLIDV--------------G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 606 IRYGRLDasdadveaaaraakvdQIVQNLpqgyntkvgerglmiSGGEKQRLAVARLLLKNP--SILFFDEATSALDSYT 683
Cdd:cd03238 76 LGYLTLG----------------QKLSTL---------------SGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQD 124
|
170 180 190
....*....|....*....|....*....|....*.
gi 2274528008 684 ETELMRNINaNLLSEKRTAIFVAHRLRTISDSDLIV 719
Cdd:cd03238 125 INQLLEVIK-GLIDLGNTVILIEHNLDVLSSADWII 159
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
638-689 |
1.51e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.11 E-value: 1.51e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2274528008 638 YNTKVGE---RGlmISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMR 689
Cdd:TIGR00956 198 RNTKVGNdfvRG--VSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIR 250
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
512-726 |
1.68e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.79 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYHpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIyidgqditkvsleSLRRHI--G 589
Cdd:PRK10636 313 LKMEKVSAGYG-DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI-------------GLAKGIklG 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 590 VVPQdtplfnddirHNIRYGRLDASDADVEAAARAAKVDQIVQNLPQGY---NTKVGERGLMISGGEKQRLAVARLLLKN 666
Cdd:PRK10636 379 YFAQ----------HQLEFLRADESPLQHLARLAPQELEQKLRDYLGGFgfqGDKVTEETRRFSGGEKARLVLALIVWQR 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2274528008 667 PSILFFDEATSALDSYtetelMRNINANLLSEKRTAIFVA----HRLRTISDsDLIVVlQSGQV 726
Cdd:PRK10636 449 PNLLLLDEPTNHLDLD-----MRQALTEALIDFEGALVVVshdrHLLRSTTD-DLYLV-HDGKV 505
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
502-695 |
1.80e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.54 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 502 APPLKVTGGeirfenVTFGYHpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKvsl 581
Cdd:PRK13543 8 APPLLAAHA------LAFSRN-EEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 582 eslrrhigvvpqdtplfNDDIRHNIRYGRLDASDADVEAAARAAKVDQI----VQNLPQGYNTKVGERGL------MISG 651
Cdd:PRK13543 78 -----------------GDRSRFMAYLGHLPGLKADLSTLENLHFLCGLhgrrAKQMPGSALAIVGLAGYedtlvrQLSA 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2274528008 652 GEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNINANL 695
Cdd:PRK13543 141 GQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHL 184
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
515-731 |
1.81e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.48 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 515 ENVTFGYHPDRPIFS---NISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQ----------DITKVSL 581
Cdd:PRK10261 16 ENLNIAFMQEQQKIAavrNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSEQSA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 582 ESLRR----HIGVVPQD-----TPLF--NDDIRHNIRYGR-LDASDADVEAAARaakVDQIvqNLPQGyNTKVGERGLMI 649
Cdd:PRK10261 96 AQMRHvrgaDMAMIFQEpmtslNPVFtvGEQIAESIRLHQgASREEAMVEAKRM---LDQV--RIPEA-QTILSRYPHQL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 650 SGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNINANLLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQVAE 728
Cdd:PRK10261 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEiADRVLVMYQGEAVE 249
|
...
gi 2274528008 729 KGT 731
Cdd:PRK10261 250 TGS 252
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
183-455 |
2.64e-07 |
|
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: 53.25 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 183 VALALALLVGGKLLNVQVPFFfkaivdRLNQVVNAPLDMTNPNTVWVVagsaILGyglarVGAAAFSELRNAVFANVAQQ 262
Cdd:cd18577 13 AALPLMTIVFGDLFDAFTDFG------SGESSPDEFLDDVNKYALYFV----YLG-----IGSFVLSYIQTACWTITGER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 263 SIRRVARSVFTHLLALDLGWHLTRQTGGLTRAIDRGTK----GIS----FLLTSIVFHIvpTALEISMVCG------ILS 328
Cdd:cd18577 78 QARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNliqdGIGeklgLLIQSLSTFI--AGFIIAFIYSwkltlvLLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 329 ykCGPSFAAVtavtmaayAWFTIRTTSwrtRFRKEANAADNRAATTSVDSLLNYEAVKYFNNEKHEIAKYDAALADYEKS 408
Cdd:cd18577 156 --TLPLIAIV--------GGIMGKLLS---KYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKA 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2274528008 409 SIKVATSLAALnsgqnaiFSTSLTVMMLLAAQG-------VTNGTMSVGDLVMV 455
Cdd:cd18577 223 GIKKGLVSGLG-------LGLLFFIIFAMYALAfwygsrlVRDGEISPGDVLTV 269
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
530-725 |
3.06e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.58 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 530 NISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDIT-KVSLESLRRHIGVVPQDTPLFND-DIRHNIR 607
Cdd:PRK10982 16 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQELNLVLQrSVMDNMW 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 608 YGRLDASDADVEAAARAAKVDQIVQNLPQGYNTKVGERGLMISggEKQRLAVARLLLKNPSILFFDEATSALdsyTETE- 686
Cdd:PRK10982 96 LGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVS--QMQMIEIAKAFSYNAKIVIMDEPTSSL---TEKEv 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2274528008 687 --LMRNINAnlLSEKRTAI-FVAHRLRTISD-SDLIVVLQSGQ 725
Cdd:PRK10982 171 nhLFTIIRK--LKERGCGIvYISHKMEEIFQlCDEITILRDGQ 211
|
|
| ABC_6TM_McjD_like |
cd18556 |
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ... |
201-481 |
3.13e-07 |
|
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: 52.64 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 201 PFFFKAIVDRLNQVVNAPLDMtnpntVWVVAGSAILGYGLARVGAAAF----SELRNavfanvaqQSIRRVARSVFTHLL 276
Cdd:cd18556 22 PVILAKITDLLTSSSSDSYNY-----IVVLAALYVITISATKLLGFLSlylqSSLRV--------ELIISISSSYFRYLY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 277 ALDLGWHLTRQTGGLTRAIDRGTKGISFLLTSIVFHIVPTALE--ISMVCGILS--YKCGPSFAAVTAVTMAAYAWFTIR 352
Cdd:cd18556 89 EQPKTFFVKENSGDITQRLNQASNDLYTLVRNLSTNILPPLLQliIAIVVILSSgdYFVAALFLLYAVLFVINNTIFTKK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 353 TTSWRTRFRKeanaADNRAATTSVDSLLNYEAVKYFNNEKHEIAKYDAAL-------ADYEKSSIKVATslaaLNSGQNA 425
Cdd:cd18556 169 IVSLRNDLMD----AGRKSYSLLTDSVKNIVAAKQNNAFDFLFKRYEATLtndrnsqKRYWKLTFKMLI----LNSLLNV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2274528008 426 IFSTSLTVMMLLaaqGVTNGTMSVGDLVMVNQLVFQLSLPLNFLGTVYRELRQSLV 481
Cdd:cd18556 241 ILFGLSFFYSLY---GVVNGQVSIGHFVLITSYILLLSTPIESLGNMLSELRQSVH 293
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
201-484 |
5.82e-07 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 52.12 E-value: 5.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 201 PFFFKAIVDRLnqVVNAPLDMTNpntvwvvagsaILGYGLARVGA--AAFSELRNAVFANVAQQ-----SIRrvarsVFT 273
Cdd:cd18588 22 PLFFQVIIDKV--LVHRSLSTLD-----------VLAIGLLVVALfeAVLSGLRTYLFSHTTNRidaelGAR-----LFR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 274 HLLALDLGWHLTRQTG-------------------GLTRAIDRGTKGI--------SFLLTSIVFHIVPtaleismVCGI 326
Cdd:cd18588 84 HLLRLPLSYFESRQVGdtvarvrelesirqfltgsALTLVLDLVFSVVflavmfyySPTLTLIVLASLP-------LYAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 327 LSYKCGPsfaavtavtmaayawftirttswrtRFRKEANAADNRAATTS---VDSLLNYEAVKYFNNEKHEIAKYDAALA 403
Cdd:cd18588 157 LSLLVTP-------------------------ILRRRLEEKFQRGAENQsflVETVTGIETVKSLAVEPQFQRRWEELLA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 404 DYEKSSIKVATSLAALNSGQNAIFSTSLTVMMLLAAQGVTNGTMSVGDLVMVNQLVFQLSLPLNFLGTVYRELRQSLVDM 483
Cdd:cd18588 212 RYVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLVMDGELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQAKVSV 291
|
.
gi 2274528008 484 E 484
Cdd:cd18588 292 E 292
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
512-685 |
9.82e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.04 E-value: 9.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFGYhPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKI---------YID---------- 572
Cdd:PRK11819 325 IEAENLSKSF-GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIkigetvklaYVDqsrdaldpnk 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 573 --------GQDITKV---SLESlRRHIGvvpqdtplfnddiRHNIRYGrldasdadveaaaraakvDQivqnlpqgyNTK 641
Cdd:PRK11819 404 tvweeisgGLDIIKVgnrEIPS-RAYVG-------------RFNFKGG------------------DQ---------QKK 442
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2274528008 642 VGerglMISGGEKQRLAVARLLLKNPSILFFDEATSALDsyTET 685
Cdd:PRK11819 443 VG----VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD--VET 480
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
649-731 |
1.14e-06 |
|
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: 49.49 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 649 ISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNINANLLSEKRTAIFVAHRLRTISD-SDLIVVLQsGQVA 727
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYlSDRIHVFE-GEPG 150
|
....
gi 2274528008 728 EKGT 731
Cdd:cd03222 151 VYGI 154
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
531-734 |
1.17e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.84 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 531 ISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVS-LESLRRHIGVVPQD------TPL--FNDD 601
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSpRDAIRAGIMLCPEDrkaegiIPVhsVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 602 I-----RHNIRYG-----RLDASDADVEAAARAAKV---DQIVQNLpqgyntkvgerglmiSGGEKQRLAVARLLLKNPS 668
Cdd:PRK11288 352 InisarRHHLRAGclinnRWEAENADRFIRSLNIKTpsrEQLIMNL---------------SGGNQQKAILGRWLSEDMK 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2274528008 669 ILFFDEATSALDSYTETELMrNINANLLSEKRTAIFVAHRL-RTISDSDLIVVLQSGQVAEKGTHAE 734
Cdd:PRK11288 417 VILLDEPTRGIDVGAKHEIY-NVIYELAAQGVAVLFVSSDLpEVLGVADRIVVMREGRIAGELAREQ 482
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
184-470 |
1.47e-06 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 50.87 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 184 ALALALLVGGKLLNVQVPFFFKAIVDRLNQvvnapldmtnpntvWVVAGSAILGYGLARVGAAAFSelrnAVFANVAQQS 263
Cdd:cd18541 2 LLGILFLILVDLLQLLIPRIIGRAIDALTA--------------GTLTASQLLRYALLILLLALLI----GIFRFLWRYL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 264 IRRVARSV--------FTHLLALDLGWHLTRQTGGL-TRAI-D----RGTKG--------ISFLLTSIVFHIVPTALEIS 321
Cdd:cd18541 64 IFGASRRIeydlrndlFAHLLTLSPSFYQKNRTGDLmARATnDlnavRMALGpgilylvdALFLGVLVLVMMFTISPKLT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 322 MVC-------GILSYKCGPSFaavtavtmaayawftirttswRTRFRK--EANAADNRAATTSVDSLlnyEAVKYFNNEK 392
Cdd:cd18541 144 LIAllplpllALLVYRLGKKI---------------------HKRFRKvqEAFSDLSDRVQESFSGI---RVIKAFVQEE 199
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2274528008 393 HEIAKYDAALADYEKSSIKVATSLAALNSGQNAIFSTSLTVMMLLAAQGVTNGTMSVGDLVMVNQLVFQLSLPLNFLG 470
Cdd:cd18541 200 AEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPMMALG 277
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
495-680 |
1.59e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.57 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 495 AVKENADAPPlkVTGGEIRFE--NVTfgYHPDRPI--FSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIY 570
Cdd:COG3845 241 EVLLRVEKAP--AEPGEVVLEveNLS--VRDDRGVpaLKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIR 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 571 IDGQDITKVSLESLRRH-IGVVPQD---TPLFND-DIRHNI-----------RYGRLDASDADveaaaraAKVDQIVQNL 634
Cdd:COG3845 317 LDGEDITGLSPRERRRLgVAYIPEDrlgRGLVPDmSVAENLilgryrrppfsRGGFLDRKAIR-------AFAEELIEEF 389
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2274528008 635 ---PQGYNTKVGerglMISGGEKQRLAVARLLLKNPSILFFDEATSALD 680
Cdd:COG3845 390 dvrTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLD 434
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
492-707 |
2.43e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.78 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 492 VNVAVKEnADAPPLKVTGGE----IRFENVTFGYHpDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYkPQ-- 565
Cdd:PRK10938 238 EGVQLPE-PDEPSARHALPAneprIVLNNGVVSYN-DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDH-PQgy 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 566 SGKIYIDGQdiTKVSLESL---RRHIGVVPQDTPL---FNDDIRHNIRYGRLDA-------SDAdveaaaRAAKVDQIVQ 632
Cdd:PRK10938 315 SNDLTLFGR--RRGSGETIwdiKKHIGYVSSSLHLdyrVSTSVRNVILSGFFDSigiyqavSDR------QQKLAQQWLD 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 633 NLpqGYNTKVGE---RGLmiSGGEkQRLA-VARLLLKNPSILFFDEATSALDSyTETELMRNINANLLSEKRTA-IFVAH 707
Cdd:PRK10938 387 IL--GIDKRTADapfHSL--SWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDP-LNRQLVRRFVDVLISEGETQlLFVSH 460
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
525-736 |
5.91e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 48.67 E-value: 5.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 525 RPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLF-RFYKPQ-------SGKIYIDGQDITKVSLESLRRHIGVVPQDT- 595
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAAq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 596 PLFNDDIR---------HNIRYGRLDASDADVEAAARAAKvdqivqnlpqGYNTKVGERGLMISGGEKQRLAVARLLLK- 665
Cdd:PRK13547 94 PAFAFSAReivllgrypHARRAGALTHRDGEIAWQALALA----------GATALVGRDVTTLSGGELARVQFARVLAQl 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 666 --------NPSILFFDEATSALDSYTETELMRNINANLLSEKRTAIFVAHRLRTIS-DSDLIVVLQSGQVAEKGTHAELM 736
Cdd:PRK13547 164 wpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAArHADRIAMLADGAIVAHGAPADVL 243
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
524-743 |
6.58e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 48.25 E-value: 6.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 524 DRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLF--RFYKPQSGKIYIDGQDITKVSLESlRRHIGVV-----PQDTP 596
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPED-RAGEGIFmafqyPVEIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 597 LFNDDI------------RHNIRYGRLDASDADVEaaaraaKVDQIvqNLPQGYNTKVGERGLmiSGGEKQRLAVARLLL 664
Cdd:PRK09580 92 GVSNQFflqtalnavrsyRGQEPLDRFDFQDLMEE------KIALL--KMPEDLLTRSVNVGF--SGGEKKRNDILQMAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 665 KNPSILFFDEATSALDSYTETELMRNINAnLLSEKRTAIFVAHRLRTIS--DSDLIVVLQSGQVAEKGTH--AELMDRKG 740
Cdd:PRK09580 162 LEPELCILDESDSGLDIDALKIVADGVNS-LRDGKRSFIIVTHYQRILDyiKPDYVHVLYQGRIVKSGDFtlVKQLEEQG 240
|
...
gi 2274528008 741 LYW 743
Cdd:PRK09580 241 YGW 243
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
544-741 |
1.01e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 49.01 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 544 VGPSGCGKSTIFRLLFRFYKPQSGKI-----------YIDG-QDITKVSLesLRRHIGVvPQDTPLFNDDIRHNIRYGRL 611
Cdd:COG1245 372 VGPNGIGKTTFAKILAGVLKPDEGEVdedlkisykpqYISPdYDGTVEEF--LRSANTD-DFGSSYYKTEIIKPLGLEKL 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 612 dasdadveaaaraakVDQIVQNLpqgyntkvgerglmiSGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNI 691
Cdd:COG1245 449 ---------------LDKNVKDL---------------SGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAI 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2274528008 692 NANLLSEKRTAIFVAHRLRTIsD--SDLIVVLqSGQVAEKGTHAELMD-RKGL 741
Cdd:COG1245 499 RRFAENRGKTAMVVDHDIYLI-DyiSDRLMVF-EGEPGVHGHASGPMDmREGM 549
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
650-731 |
1.15e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.18 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 650 SGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNINaNLLSEKRTA-IFVAHRLRTISDS-DLIVVLQSGQVA 727
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLN-ELKREFNTAiIMITHDLGVVAGIcDKVLVMYAGRTM 241
|
....
gi 2274528008 728 EKGT 731
Cdd:PRK09473 242 EYGN 245
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
524-691 |
1.98e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.18 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 524 DRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLfrfykpqSGKI---YIDGQDIT---KVSLESLRRHIGVVPQ-DTP 596
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVL-------AERVttgVITGGDRLvngRPLDSSFQRSIGYVQQqDLH 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 597 LFNDDIRHNIRYG---RLDASDADVEAAARAAKVDQIVQnLPQGYNTKVGERGLMISGGEKQRLAVARLLLKNP-SILFF 672
Cdd:TIGR00956 848 LPTSTVRESLRFSaylRQPKSVSKSEKMEYVEEVIKLLE-MESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPkLLLFL 926
|
170 180
....*....|....*....|..
gi 2274528008 673 DEATSALDSYTE---TELMRNI 691
Cdd:TIGR00956 927 DEPTSGLDSQTAwsiCKLMRKL 948
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
544-741 |
2.03e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.88 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 544 VGPSGCGKSTIFRLLFRFYKPQSGKIYIDgqdiTKVSLEslrrhigvvPQ----DTPLFNDDIRHNIRyGRLDASDADVE 619
Cdd:PRK13409 371 VGPNGIGKTTFAKLLAGVLKPDEGEVDPE----LKISYK---------PQyikpDYDGTVEDLLRSIT-DDLGSSYYKSE 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 620 aaaraakvdqIVQ--NLPQGYNTKVGErglmISGGEKQRLAVARLLLKNPSILFFDEATSALDS---YTETELMRNINAN 694
Cdd:PRK13409 437 ----------IIKplQLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrLAVAKAIRRIAEE 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2274528008 695 llsEKRTAIFVAHRLRTIsD--SDLIVVLqSGQVAEKGTHAELMD-RKGL 741
Cdd:PRK13409 503 ---REATALVVDHDIYMI-DyiSDRLMVF-EGEPGKHGHASGPMDmREGM 547
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
503-736 |
2.06e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.69 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 503 PPLKVTGGEIRFE--NVTfgyhpdRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVS 580
Cdd:PRK10762 247 PRLDKAPGEVRLKvdNLS------GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRS 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 581 -LESLRRHIGVVPQDTP----LFNDDIRHN-----IRY-----GRLDASDADveaaaraakvdQIVQNLPQGYNTKVGER 645
Cdd:PRK10762 321 pQDGLANGIVYISEDRKrdglVLGMSVKENmsltaLRYfsragGSLKHADEQ-----------QAVSDFIRLFNIKTPSM 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 646 GLMI---SGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNINaNLLSEKRTAIFVAHRL-RTISDSDLIVVL 721
Cdd:PRK10762 390 EQAIgllSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLIN-QFKAEGLSIILVSSEMpEVLGMSDRILVM 468
|
250 260
....*....|....*....|
gi 2274528008 722 QSGQV-----AEKGTHAELM 736
Cdd:PRK10762 469 HEGRIsgeftREQATQEKLM 488
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
512-680 |
2.41e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 46.62 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 512 IRFENVTFgyHPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKP----QSGKIYIDGQditKVSLESLR-R 586
Cdd:PRK10418 5 IELRNIAL--QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGK---PVAPCALRgR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 587 HIGVVPQD-----TPLFNddIRHNIR-----YGRLDASDADVEAAARAAKVDqiVQNLPQGYntkvgerGLMISGGEKQR 656
Cdd:PRK10418 80 KIATIMQNprsafNPLHT--MHTHARetclaLGKPADDATLTAALEAVGLEN--AARVLKLY-------PFEMSGGMLQR 148
|
170 180
....*....|....*....|....
gi 2274528008 657 LAVARLLLKNPSILFFDEATSALD 680
Cdd:PRK10418 149 MMIALALLCEAPFIIADEPTTDLD 172
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
470-708 |
2.54e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.92 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 470 GTVYRELRQSLVDMETMFNLENVNVAVKENADAPP----LKVTGGEIRFENVTfgYHPDRP--------------IFSNI 531
Cdd:PLN03140 822 GNNTREVAIQRMSNPEGLSKNRDSSLEAANGVAPKrgmvLPFTPLAMSFDDVN--YFVDMPaemkeqgvtedrlqLLREV 899
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 532 SFAVPAGYKTAFVGPSGCGKSTIFRLLfrfykpqSGKI---YIDGqDItKVS-----LESLRRHIGVVPQdtplfND--- 600
Cdd:PLN03140 900 TGAFRPGVLTALMGVSGAGKTTLMDVL-------AGRKtggYIEG-DI-RISgfpkkQETFARISGYCEQ-----NDihs 965
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 601 ---DIRHNIRYGRLDASDADVEAAARAAKVDQIVQ--NLPQGYNTKVGERGLM-ISGGEKQRLAVARLLLKNPSILFFDE 674
Cdd:PLN03140 966 pqvTVRESLIYSAFLRLPKEVSKEEKMMFVDEVMElvELDNLKDAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDE 1045
|
250 260 270
....*....|....*....|....*....|....
gi 2274528008 675 ATSALDSYTETELMRNINaNLLSEKRTAIFVAHR 708
Cdd:PLN03140 1046 PTSGLDARAAAIVMRTVR-NTVDTGRTVVCTIHQ 1078
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
183-453 |
3.52e-05 |
|
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: 46.33 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 183 VALALALLVGGKLLNVQVPFFFKAIVDRlnQVVNApldmtNPNTVWVVAGsailgYGLARVGAAAFSELRNAVFANVAQQ 262
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDS--GVRAG-----DLGVLLLAAA-----AYLAVVLAGWVAQRAQTRLTGRTGE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 263 SIRRVARS-VFTHLLALDLGWHlTRQTGGltRAIDRGTKGI----SFLLTSIVfhivPTALEISMVCGILSykcgpsfaa 337
Cdd:cd18546 69 RLLYDLRLrVFAHLQRLSLDFH-ERETSG--RIMTRMTSDIdalsELLQTGLV----QLVVSLLTLVGIAV--------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 338 vtavtmaayawfTIRTTSWR---------------TR-FRKEANAADNRAATTS-------VDSLLNYEAVKYFNNEKHE 394
Cdd:cd18546 133 ------------VLLVLDPRlalvalaalpplalaTRwFRRRSSRAYRRARERIaavnadlQETLAGIRVVQAFRRERRN 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2274528008 395 IAKYDAALADYEKSSIKVATSLAALNSGQNAIFSTSLTVMMLLAAQGVTNGTMSVGDLV 453
Cdd:cd18546 201 AERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAAGTLTVGVLV 259
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
183-479 |
4.47e-05 |
|
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: 46.24 E-value: 4.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 183 VALALALLVGGKLLNVQVPFFFKAIVDRLNQVVNAPLDMtNPNTVWVVAGSAILGYglarVGAAAFSELRNAVFANVAQQ 262
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGV-DFSGLLRILLLLLGLY----LLSALFSYLQNRLMARVSQR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 263 SIRRVARSVFTHLLALDLGWHLTRQTGGL----TRAIDRGTKGISFLLTSIVFHIV--------------PTALeISMVC 324
Cdd:cd18547 76 TVYDLRKDLFEKLQRLPLSYFDTHSHGDImsrvTNDVDNISQALSQSLTQLISSILtivgtlimmlyispLLTL-IVLVT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 325 GILSYkcgpsfaavtavtmaayawFTIRTTSWRTR--FRKEANAadnRAATTSV--DSLLNYEAVKYFNNEKHEIAKYDA 400
Cdd:cd18547 155 VPLSL-------------------LVTKFIAKRSQkyFRKQQKA---LGELNGYieEMISGQKVVKAFNREEEAIEEFDE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 401 ALADYEKSSIKvATSLAAL-NSGQNAIFSTSLTVMMLLAAQGVTNGTMSVGDLVMVNQLVFQLSLPLNFLGTVYRELrQS 479
Cdd:cd18547 213 INEELYKASFK-AQFYSGLlMPIMNFINNLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSL-QS 290
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
652-736 |
5.83e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 45.95 E-value: 5.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 652 GEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMR-----NINANLlsekrTAIFVAHRLRTISD-SDLIVVLQSGQ 725
Cdd:PRK15093 162 GECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRlltrlNQNNNT-----TILLISHDLQMLSQwADKINVLYCGQ 236
|
90
....*....|.
gi 2274528008 726 VAEKGTHAELM 736
Cdd:PRK15093 237 TVETAPSKELV 247
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
526-709 |
6.28e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 46.93 E-value: 6.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 526 PIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITkVSLESLRRHIGVVPQDTPLfnDDI--- 602
Cdd:TIGR01257 1953 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-TNISDVHQNMGYCPQFDAI--DDLltg 2029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 603 -RHNIRYGRLDASDADveaaaraaKVDQI----VQNLpqGYNTKVGERGLMISGGEKQRLAVARLLLKNPSILFFDEATS 677
Cdd:TIGR01257 2030 rEHLYLYARLRGVPAE--------EIEKVanwsIQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTT 2099
|
170 180 190
....*....|....*....|....*....|..
gi 2274528008 678 ALDSYTEtELMRNINANLLSEKRTAIFVAHRL 709
Cdd:TIGR01257 2100 GMDPQAR-RMLWNTIVSIIREGRAVVLTSHSM 2130
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
522-719 |
7.26e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.89 E-value: 7.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 522 HPDRPIFSNISFavPAGYKTAFVGPSGCGKSTIFR-----LLFRFYKPQSGKIYIDGQDITKVSLEslrrHIGVVPQdtp 596
Cdd:cd03227 7 FPSYFVPNDVTF--GEGSLTIITGPNGSGKSTILDaiglaLGGAQSATRRRSGVKAGCIVAAVSAE----LIFTRLQ--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 597 lfnddirhnirygrldasdadveaaaraakvdqivqnlpqgyntkvgerglmISGGEKQRLAVA---RLLLKNPSILF-F 672
Cdd:cd03227 78 ----------------------------------------------------LSGGEKELSALAlilALASLKPRPLYiL 105
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2274528008 673 DEATSALDSYTETELMRNINANLLsEKRTAIFVAHRLRTISDSDLIV 719
Cdd:cd03227 106 DEIDRGLDPRDGQALAEAILEHLV-KGAQVIVITHLPELAELADKLI 151
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
195-478 |
8.33e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 45.27 E-value: 8.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 195 LLNVQVPFFFKAIVDRLnqVVNAPLdmtnpNTVWVVAgsaiLGYGLARVGAAAFSELRNAVFANVAQQSIRRVARSVFTH 274
Cdd:cd18566 16 ILALATPLFILQVYDRV--IPNESI-----PTLQVLV----IGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 275 LLALDL--------GWHLTR---------QTGG--LTRAIDRGTKGIsFLLTSIVFH----IVPTALEIsmVCGILSYKC 331
Cdd:cd18566 85 LLSLPLsfferepsGAHLERlnsleqireFLTGqaLLALLDLPFVLI-FLGLIWYLGgklvLVPLVLLG--LFVLVAILL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 332 GPSFaavtavtmaayawftirttswRTRFrKEANAADNRAATTSVDSLLNYEAVKYFNNEKHEIAKYDAALADYEKSSIK 411
Cdd:cd18566 162 GPIL---------------------RRAL-KERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFK 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2274528008 412 VA-TSLAALNSGQnaIFSTSLTVMML-LAAQGVTNGTMSVGDLVMVNQLVFQLSLPLNFLGTVYRELRQ 478
Cdd:cd18566 220 VAkINAVAQTLGQ--LFSQVSMVAVVaFGALLVINGDLTVGALIACTMLSGRVLQPLQRAFGLWTRFQQ 286
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
347-453 |
1.75e-04 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 44.36 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 347 AWFTIRTT-SWRTRFRKeanaadNRAATTSV-----DSLLNYEAVKYFNNEKHEIAKYDAALADYEKSSIKVATSLAALN 420
Cdd:cd18549 156 IIFTIYFNkKMKKAFRR------VREKIGEInaqleDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYFF 229
|
90 100 110
....*....|....*....|....*....|....*
gi 2274528008 421 SGQNaiFSTSLTVMMLLAAQG--VTNGTMSVGDLV 453
Cdd:cd18549 230 SGMN--FFTNLLNLVVLVAGGyfIIKGEITLGDLV 262
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
183-472 |
1.83e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 44.48 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 183 VALALALLVGGKLLNVQVPFFFKAIVDR--------LNQVVNAPLDMTNPNTVWVVAGSAILGYglarVGAAAFSELRNA 254
Cdd:cd18565 1 LVLGLLASILNRLFDLAPPLLIGVAIDAvfngeasfLPLVPASLGPADPRGQLWLLGGLTVAAF----LLESLFQYLSGV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 255 VFANVAQQSIRRVARSVFTHLLALDLGWHLTRQTGGLTRA----IDRGTKGISFLLTSIVfHIVPTALEISMVCGILSYK 330
Cdd:cd18565 77 LWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVlnndVNQLERFLDDGANSII-RVVVTVLGIGAILFYLNWQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 331 cgpsfaavtavtmaaYAWFT-------IRTTSWRTRfRKEANAADNRAATTSVDSLLN-----YEAVKYFNNEKHEIAKY 398
Cdd:cd18565 156 ---------------LALVAllpvpliIAGTYWFQR-RIEPRYRAVREAVGDLNARLEnnlsgIAVIKAFTAEDFERERV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 399 DAALADYEKSSIKVATSLAALNSGQNAIFSTSLTVMMLLAAQGVTNG------TMSVGDLVMvnqLVF---QLSLPLNFL 469
Cdd:cd18565 220 ADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVLDGpplftgTLTVGTLVT---FLFytqRLLWPLTRL 296
|
...
gi 2274528008 470 GTV 472
Cdd:cd18565 297 GDL 299
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
528-727 |
2.11e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 44.66 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 528 FSNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYKPQSGKIYIDGQDITKVS-LESLRRHIGVVPQD---TPLFND-DI 602
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStAQRLARGLVYLPEDrqsSGLYLDaPL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 603 RHNI---RYGRL------DASDADVEAAARA-----AKVDQIVQNLpqgyntkvgerglmiSGGEKQRLAVARLLLKNPS 668
Cdd:PRK15439 359 AWNVcalTHNRRgfwikpARENAVLERYRRAlnikfNHAEQAARTL---------------SGGNQQKVLIAKCLEASPQ 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2274528008 669 ILFFDEATSALDSYTETELMRNINAnlLSEKRTAI-FVAHRLRTISD-SDLIVVLQSGQVA 727
Cdd:PRK15439 424 LLIVDEPTRGVDVSARNDIYQLIRS--IAAQNVAVlFISSDLEEIEQmADRVLVMHQGEIS 482
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
529-728 |
2.78e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.40 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 529 SNISFAVPAGYKTAFVGPSGCGKSTIFRLLFRFYkPQ---SGKIYIDGQ-----DITkvslESLRRHIGVVPQD---TPL 597
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEvcrfkDIR----DSEALGIVIIHQElalIPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 598 FNddIRHNI-------RYGRLDASDADVEAAARAAKVdqivqNLPQGYNTKVGERGLmisgGEKQRLAVARLLLKNPSIL 670
Cdd:NF040905 93 LS--IAENIflgneraKRGVIDWNETNRRARELLAKV-----GLDESPDTLVTDIGV----GKQQLVEIAKALSKDVKLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2274528008 671 FFDEATSAL---DSYTETELMRninaNLLSEKRTAIFVAHRLRTISD-SDLIVVLQSGQVAE 728
Cdd:NF040905 162 ILDEPTAALneeDSAALLDLLL----ELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
530-735 |
3.17e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 43.58 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 530 NISFAVPAGYKTAFVGPSGCGKS----TIFRLLFRFYKPQSGKIYIDGQDITKVSLESLRRHIG----VVPQDtPLFNDD 601
Cdd:PRK11022 25 RISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLVGaevaMIFQD-PMTSLN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 602 IRHNIRYgrldasdadveaaaraakvdQIVQNLP--QGYNTKV-GERGL--------------------MISGGEKQRLA 658
Cdd:PRK11022 104 PCYTVGF--------------------QIMEAIKvhQGGNKKTrRQRAIdllnqvgipdpasrldvyphQLSGGMSQRVM 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2274528008 659 VARLLLKNPSILFFDEATSALDSYTETELMRNINANLLSEKRTAIFVAHRLRTISDS-DLIVVLQSGQVAEKGTHAEL 735
Cdd:PRK11022 164 IAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAaHKIIVMYAGQVVETGKAHDI 241
|
|
| PHA03201 |
PHA03201 |
uracil DNA glycosylase; Provisional |
88-172 |
3.28e-04 |
|
uracil DNA glycosylase; Provisional
Pssm-ID: 165468 Cd Length: 318 Bit Score: 43.73 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 88 PTEPPKQSLSSSTTTPPQS--ASDNIVAASTPSPSASTPSARASTQPAAKKQPDG-------------DDPLGLN----A 148
Cdd:PHA03201 7 RSPSPPRRPSPPRPTPPRSpdASPEETPPSPPGPGAEPPPGRAAGPAAPRRRPRGcpagvtfsssappRPPLGLDdapaA 86
|
90 100
....*....|....*....|....*.
gi 2274528008 149 REKSLkeqrmvDWAIIRK--LVQYVW 172
Cdd:PHA03201 87 TPPPL------DWTEFRRrfLVGDAW 106
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
359-460 |
3.46e-04 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 43.24 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 359 RFRKEANAADNRAATTSV---DSLLNYEAVKYFNNEKHEIAKYDAALADYEKSSIKVATSLAALNSGQNAIFSTSLTVMM 435
Cdd:cd18575 159 RVRRLSRASQDRLADLSAfaeETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVL 238
|
90 100
....*....|....*....|....*
gi 2274528008 436 LLAAQGVTNGTMSVGDLVmvnQLVF 460
Cdd:cd18575 239 WLGAHDVLAGRMSAGELS---QFVF 260
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
503-680 |
4.31e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.62 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 503 PPLKVTGGEIRFE----NVTFGYHPDRPIFSNISFAVPAGYKTAFVGPSGCGKSTIFRLLF-RFY-KPQSGKIYIDGQ-- 574
Cdd:NF040905 247 PERTPKIGEVVFEvknwTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgRSYgRNISGTVFKDGKev 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 575 DITKVS----------LESlRRHIGVVpqdtplFNDDIRHNIRYGRLDA-SDADVEAAARAAKV---------------D 628
Cdd:NF040905 327 DVSTVSdaidaglayvTED-RKGYGLN------LIDDIKRNITLANLGKvSRRGVIDENEEIKVaeeyrkkmniktpsvF 399
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2274528008 629 QIVQNLpqgyntkvgerglmiSGGEKQRLAVARLLLKNPSILFFDEATSALD 680
Cdd:NF040905 400 QKVGNL---------------SGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
636-717 |
5.46e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 636 QGYNTKVGERGLM-----ISGGEKQ------RLAVARLLLKNPSILFFDEATSALDSYTETELMRNINANLL--SEKRTA 702
Cdd:PRK01156 784 QDFNITVSRGGMVegidsLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKdsSDIPQV 863
|
90
....*....|....*
gi 2274528008 703 IFVAHRLRTISDSDL 717
Cdd:PRK01156 864 IMISHHRELLSVADV 878
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
637-742 |
3.23e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.87 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 637 GYNTKVGErglmISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNINANLLSEKRTAIFVAHRLRTISDSD 716
Cdd:PRK10982 384 GHRTQIGS----LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITD 459
|
90 100 110
....*....|....*....|....*....|.
gi 2274528008 717 LIVVLQSGQVA-----EKGTHAELMDRKGLY 742
Cdd:PRK10982 460 RILVMSNGLVAgivdtKTTTQNEILRLASLH 490
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
183-453 |
6.75e-03 |
|
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: 39.37 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 183 VALALALLVggklLNVQVPFFFKAIVDrlnQVVNApldmTNPNTVWVVAgsaiLGYGLARVGAAAFSELRNAVFANVAQQ 262
Cdd:cd18567 8 LLLSLALEL----FALASPLYLQLVID---EVIVS----GDRDLLTVLA----IGFGLLLLLQALLSALRSWLVLYLSTS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 263 SIRRVARSVFTHLLALDLGWHLTRQTGG-LTR--AIDRgtkgISFLLTSivfHIVPTALEISMVCGILS----YkcGPSF 335
Cdd:cd18567 73 LNLQWTSNLFRHLLRLPLSYFEKRHLGDiVSRfgSLDE----IQQTLTT---GFVEALLDGLMAILTLVmmflY--SPKL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 336 AAVTAVTMAAYAwfTIRTTSWRtRFRK---EANAADNRAATTSVDSLLNYEAVKYFNNEKHEIAKYDAALADYEKSSIKV 412
Cdd:cd18567 144 ALIVLAAVALYA--LLRLALYP-PLRRateEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRL 220
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2274528008 413 ATSLAALNSGQNAIFSTSLTVMMLLAAQGVTNGTMSVGDLV 453
Cdd:cd18567 221 QRLQILFSAANGLLFGLENILVIYLGALLVLDGEFTVGMLF 261
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
530-731 |
6.79e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 39.13 E-value: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 530 NISFAVPAGYKTAFVGPSGCGKST-IFRLLfrfYKPQSGKIYIDGQDITKVSLESLRRHIG---VVPQD----TPLFN-- 599
Cdd:cd03271 13 NIDVDIPLGVLTCVTGVSGSGKSSlINDTL---YPALARRLHLKKEQPGNHDRIEGLEHIDkviVIDQSpigrTPRSNpa 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 600 ------DDIR-------HNIRYGR--LD-----ASDADV---------EAAARAAKVDQIVQNLPQ---GYnTKVGERGL 647
Cdd:cd03271 90 tytgvfDEIRelfcevcKGKRYNRetLEvrykgKSIADVldmtveealEFFENIPKIARKLQTLCDvglGY-IKLGQPAT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 648 MISGGEKQRLAVARLLLK---NPSILFFDEATSALDSYTETELMRNINAnLLSEKRTAIFVAHRLRTISDSDLIVVL--- 721
Cdd:cd03271 169 TLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQR-LVDKGNTVVVIEHNLDVIKCADWIIDLgpe 247
|
250
....*....|...
gi 2274528008 722 ---QSGQVAEKGT 731
Cdd:cd03271 248 ggdGGGQVVASGT 260
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
239-455 |
7.40e-03 |
|
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: 39.36 E-value: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 239 GLArVGAAAFSELRNAVFANVAQQSIRRVARSVFTHLLALDLGWH--LTRQTGGLTRAIDRGTKGISFLLTSIVFHIVpT 316
Cdd:cd18578 60 VLA-IVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFddPENSTGALTSRLSTDASDVRGLVGDRLGLIL-Q 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 317 ALeISMVCG-ILSYkcgpsfaavtavtmaAYAW-----------FTIRTTSWRTR----FRKEANAADNRAATTSVDSLL 380
Cdd:cd18578 138 AI-VTLVAGlIIAF---------------VYGWklalvglatvpLLLLAGYLRMRllsgFEEKNKKAYEESSKIASEAVS 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 381 NYEAVKYFNNEKHEIAKYDAALADYEKSSIKvatslAALNSGqnAIFSTSLTVMMLLAAQG-------VTNGTMSVGDLV 453
Cdd:cd18578 202 NIRTVASLTLEDYFLEKYEEALEEPLKKGLR-----RALISG--LGFGLSQSLTFFAYALAfwyggrlVANGEYTFEQFF 274
|
..
gi 2274528008 454 MV 455
Cdd:cd18578 275 IV 276
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
617-740 |
8.33e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 39.33 E-value: 8.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2274528008 617 DVEAAARAAKVDQIVQNLpqGYNTKVGERGLMISGGEKQRLAVARLLLKNPSILFFDEATSALDSYTETELMRNINAnLL 696
Cdd:NF000106 115 DLSRKDARARADELLERF--SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRS-MV 191
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2274528008 697 SEKRTAIFVAHRLRTISD-SDLIVVLQSGQVAEKGTHAELMDRKG 740
Cdd:NF000106 192 RDGATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| |
