|
Name |
Accession |
Description |
Interval |
E-value |
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
113-698 |
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: 832.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 113 WPKEDPLVRKRVGISLGLLAGSKLLTVCVPFLFKGAVDtmttlNMDTAPDAVLSAATALMLGYGIARASAAGFNELRNAV 192
Cdd:COG5265 27 LLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAID-----ALLSGAAALLVVPVGLLLAYGLLRLLSVLFGELRDAL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 193 FAKVAHHSIRKIASNVFLHLHNLDLAFHLNKQTGALSKTIDRGSRGINFVLSAMVFNIVPTIFELALVSSILGVKCGLAF 272
Cdd:COG5265 102 FARVTQRAVRRLALEVFRHLHALSLRFHLERQTGGLSRDIERGTKGIEFLLRFLLFNILPTLLEIALVAGILLVKYDWWF 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 273 AGVSMGCVGIYAAYTLSVTQWRTQFRVFMNQAENEAGNKAVDSLINYETVKYFNNEKYEAGCYNEVLKKYEAASLKTSSS 352
Cdd:COG5265 182 ALITLVTVVLYIAFTVVVTEWRTKFRREMNEADSEANTRAVDSLLNYETVKYFGNEAREARRYDEALARYERAAVKSQTS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 353 LALLNFGQNAIFSSALSLIMVLAAKEIAQGNMTVGDLVMVNALLFQLSIPLGFLGSVYREVRQALLDMRAMFTLMNVDSS 432
Cdd:COG5265 262 LALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 433 IQTAANAQPLFVdtTNSSIEFRNVSFEYEPGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGG 512
Cdd:COG5265 342 VADAPDAPPLVV--GGGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDG 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 513 QDISAVDLESLRKVIAVVPQDSVLFHNTIEHNIHYGNLSKSHAEVQNAARMADLHDSIMSWPGQYSTQVGERGLKLSGGE 592
Cdd:COG5265 420 QDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGE 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 593 KQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTRATSGRTSICIAHRLSTVKDADEILVLENGRVGERGTHSEL 672
Cdd:COG5265 500 KQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAEL 579
|
570 580
....*....|....*....|....*.
gi 45551502 673 LRQNGLYARLWETQTQQFDPSREINE 698
Cdd:COG5265 580 LAQGGLYAQMWARQQEEEEAEEALAA 605
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
101-689 |
1.41e-161 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 478.12 E-value: 1.41e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 101 SKDMLRAMMAYIWPkedplVRKRVGISLGLLAGSKLLTVCVPFLFKGAVDTMTTlnmdtapDAVLSAATALMLGYGIARA 180
Cdd:COG1132 5 PRKLLRRLLRYLRP-----YRGLLILALLLLLLSALLELLLPLLLGRIIDALLA-------GGDLSALLLLLLLLLGLAL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 181 SAAGFNELRNAVFAKVAHHSIRKIASNVFLHLHNLDLAFHLNKQTGALSKTIDRGSRGINFVLSAMVFNIVPTIFELALV 260
Cdd:COG1132 73 LRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 261 SSILGVKCGLaFAGVSMGCVGIYAAYTLSVTQWRTQFRVFMNQAENEAGNKAVDSLINYETVKYFNNEKYEAGCYNEVLK 340
Cdd:COG1132 153 LVVLFVIDWR-LALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 341 KYEAASLKTSSSLALLNFGQNAIFSSALSLIMVLAAKEIAQGNMTVGDLVMVNALLFQLSIPLGFLGSVYREVRQALLDM 420
Cdd:COG1132 232 ELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 421 RAMFTLMNVDSSIQTAANAQPLfvDTTNSSIEFRNVSFEYEPGKPIFRDLSFTIPAGKNVAIVggsgsgkssMVRLLFRF 500
Cdd:COG1132 312 ERIFELLDEPPEIPDPPGAVPL--PPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVgpsgsgkstLVNLLLRF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 501 FEPNSGKVLIGGQDISAVDLESLRKVIAVVPQDSVLFHNTIEHNIHYGNLSKSHAEVQNAARMADLHDSIMSWPGQYSTQ 580
Cdd:COG1132 390 YDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTV 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 581 VGERGLKLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTRATSGRTSICIAHRLSTVKDADEILVLEN 660
Cdd:COG1132 470 VGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDD 549
|
570 580
....*....|....*....|....*....
gi 45551502 661 GRVGERGTHSELLRQNGLYARLWETQTQQ 689
Cdd:COG1132 550 GRIVEQGTHEELLARGGLYARLYRLQFGE 578
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
127-423 |
4.73e-156 |
|
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: 453.11 E-value: 4.73e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 127 SLGLLAGSKLLTVCVPFLFKGAVDTMTTlnmdtAPDAVLSAATALMLGYGIARASAAGFNELRNAVFAKVAHHSIRKIAS 206
Cdd:cd18582 1 ALLLLVLAKLLNVAVPFLLKYAVDALSA-----PASALLAVPLLLLLAYGLARILSSLFNELRDALFARVSQRAVRRLAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 207 NVFLHLHNLDLAFHLNKQTGALSKTIDRGSRGINFVLSAMVFNIVPTIFELALVSSILGVKCGLAFAGVSMGCVGIYAAY 286
Cdd:cd18582 76 RVFRHLHSLSLRFHLSRKTGALSRAIERGTRGIEFLLRFLLFNILPTILELLLVCGILWYLYGWSYALITLVTVALYVAF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 287 TLSVTQWRTQFRVFMNQAENEAGNKAVDSLINYETVKYFNNEKYEAGCYNEVLKKYEAASLKTSSSLALLNFGQNAIFSS 366
Cdd:cd18582 156 TIKVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQALIISL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 45551502 367 ALSLIMVLAAKEIAQGNMTVGDLVMVNALLFQLSIPLGFLGSVYREVRQALLDMRAM 423
Cdd:cd18582 236 GLTAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFLGFVYREIRQSLIDMEKL 292
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
451-686 |
6.51e-133 |
|
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: 391.59 E-value: 6.51e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIAVV 530
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 531 PQDSVLFHNTIEHNIHYGNLSKSHAEVQNAARMADLHDSIMSWPGQYSTQVGERGLKLSGGEKQRVAIARAILKNTPILI 610
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45551502 611 FDEATSSLDSITEHNILQALTRATSGRTSICIAHRLSTVKDADEILVLENGRVGERGTHSELLRQNGLYARLWETQ 686
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
128-687 |
2.00e-120 |
|
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: 376.10 E-value: 2.00e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 128 LGLLAGskLLTVCVPFLFKGAVDT------MTTLNMdtapdavlsaataLMLGYGIARASAAGFNELRNAVFAKVAHHSI 201
Cdd:COG2274 164 ASLLIN--LLALATPLFTQVVIDRvlpnqdLSTLWV-------------LAIGLLLALLFEGLLRLLRSYLLLRLGQRID 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 202 RKIASNVFLHLHNLDLAFHLNKQTGALS---KTIDRGSRGINFVLSAMVFNIVPTIFELALVSSIlgvkcGLAFAGVSMG 278
Cdd:COG2274 229 LRLSSRFFRHLLRLPLSFFESRSVGDLAsrfRDVESIREFLTGSLLTALLDLLFVLIFLIVLFFY-----SPPLALVVLL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 279 CVGIYAAYTLSVTQW--RTQFRVFMNQAENEAgnKAVDSLINYETVKYFNNEKYEAGCYNEVLKKYEAASLKTSSSLALL 356
Cdd:COG2274 304 LIPLYVLLGLLFQPRlrRLSREESEASAKRQS--LLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 357 NFGQNAIFSSALSLIMVLAAKEIAQGNMTVGDLVMVNALLFQLSIPLGFLGSVYREVRQALLDMRAMFTLMNVDSSIQTA 436
Cdd:COG2274 382 STLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEG 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 437 ANAQPLfvDTTNSSIEFRNVSFEYEP-GKPIFRDLSFTIPAGKNVAIVggsgsgkssMVRLLFRFFEPNSGKVLIGGQDI 515
Cdd:COG2274 462 RSKLSL--PRLKGDIELENVSFRYPGdSPPVLDNISLTIKPGERVAIVgrsgsgkstLLKLLLGLYEPTSGRILIDGIDL 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 516 SAVDLESLRKVIAVVPQDSVLFHNTIEHNIHYGNLSKSHAEVQNAARMADLHDSIMSWPGQYSTQVGERGLKLSGGEKQR 595
Cdd:COG2274 540 RQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQR 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 596 VAIARAILKNTPILIFDEATSSLDSITEHNILQALTRATSGRTSICIAHRLSTVKDADEILVLENGRVGERGTHSELLRQ 675
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
570
....*....|..
gi 45551502 676 NGLYARLWETQT 687
Cdd:COG2274 700 KGLYAELVQQQL 711
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
451-683 |
6.54e-102 |
|
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: 311.47 E-value: 6.54e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEP-GKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIAV 529
Cdd:cd03251 1 VEFKNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 530 VPQDSVLFHNTIEHNIHYGNLSKSHAEVQNAARMADLHDSIMSWPGQYSTQVGERGLKLSGGEKQRVAIARAILKNTPIL 609
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45551502 610 IFDEATSSLDSITEHNILQALTRATSGRTSICIAHRLSTVKDADEILVLENGRVGERGTHSELLRQNGLYARLW 683
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
451-686 |
3.70e-98 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 302.15 E-value: 3.70e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEY--EPGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIA 528
Cdd:cd03249 1 IEFKNVSFRYpsRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 529 VVPQDSVLFHNTIEHNIHYGNLSKSHAEVQNAARMADLHDSIMSWPGQYSTQVGERGLKLSGGEKQRVAIARAILKNTPI 608
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45551502 609 LIFDEATSSLDSITEHNILQALTRATSGRTSICIAHRLSTVKDADEILVLENGRVGERGTHSELLRQNGLYARLWETQ 686
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
127-423 |
1.78e-96 |
|
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: 299.91 E-value: 1.78e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 127 SLGLLAGSKLLTVCVPFLFKGAVDTMTTlnmdtAPDAVLSAATALMLGYGIARASAAGFNELRNAVFAKVAHHSIRKIAS 206
Cdd:cd18560 1 SLLLLILGKACNVLAPLFLGRAVNALTL-----AKVKDLESAVTLILLYALLRFSSKLLKELRSLLYRRVQQNAYRELSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 207 NVFLHLHNLDLAFHLNKQTGALSKTIDRGSRGINFVLSAMVFNIVPTIFELALVSSILGVKCGLAFAGVSMGCVGIYAAY 286
Cdd:cd18560 76 KTFAHLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLELIVVSVVFAFHFGAWLALIVFLSVLLYGVF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 287 TLSVTQWRTQFRVFMNQAENEAGNKAVDSLINYETVKYFNNEKYEAGCYNEVLKKYEAASLKTSSSLALLNFGQNAIFSS 366
Cdd:cd18560 156 TIKVTEWRTKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLIIQL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 45551502 367 ALSLIMVLAAKEIAQGNMTVGDLVMVNALLFQLSIPLGFLGSVYREVRQALLDMRAM 423
Cdd:cd18560 236 GLTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSLTDMENL 292
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
106-686 |
4.66e-95 |
|
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: 305.86 E-value: 4.66e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 106 RAMMAYIWPKEDPLvRKRVGISLGLLAGSKLLTVCVPFLFKGAVDTmttlNMDTAPDAVLSAATALMLGYGIARASAAGF 185
Cdd:TIGR02204 3 LRPLAALWPFVRPY-RGRVLAALVALLITAAATLSLPYAVRLMIDH----GFSKDSSGLLNRYFAFLLVVALVLALGTAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 186 nelRNAVFAKVAHHSIRKIASNVFLHLHNLDLAFHLNKQTG-ALSK-TIDrgsrginfvlSAMVFNIVPTIFELALVSSI 263
Cdd:TIGR02204 78 ---RFYLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGeVVSRlTTD----------TTLLQSVIGSSLSMALRNAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 264 LGVKcGLA--------FAGVSMGCVGIYAAYTLSVTQWrtqFRVFMNQAEN---EAGNKAVDSLINYETVKYFNNEKYEA 332
Cdd:TIGR02204 145 MCIG-GLImmfitspkLTSLVLLAVPLVLLPILLFGRR---VRKLSRESQDriaDAGSYAGETLGAIRTVQAFGHEDAER 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 333 GCYN-EVLKKYEAASLKTSSSLALLNFGQNAIFSsALSLIMVLAAKEIAQGNMTVGDL--VMVNALLFQLSIplGFLGSV 409
Cdd:TIGR02204 221 SRFGgAVEKAYEAARQRIRTRALLTAIVIVLVFG-AIVGVLWVGAHDVIAGKMSAGTLgqFVFYAVMVAGSI--GTLSEV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 410 YREVRQALLDMRAMFTLMNVDSSIQTAANAQPLFVDTTnSSIEFRNVSFEY--EPGKPIFRDLSFTIPAGKNVAIVGGSG 487
Cdd:TIGR02204 298 WGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLR-GEIEFEQVNFAYpaRPDQPALDGLNLTVRPGETVALVGPSG 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 488 SGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIAVVPQDSVLFHNTIEHNIHYGNLSKSHAEVQNAARMADLH 567
Cdd:TIGR02204 377 AGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAH 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 568 DSIMSWPGQYSTQVGERGLKLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTRATSGRTSICIAHRLS 647
Cdd:TIGR02204 457 EFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLA 536
|
570 580 590
....*....|....*....|....*....|....*....
gi 45551502 648 TVKDADEILVLENGRVGERGTHSELLRQNGLYARLWETQ 686
Cdd:TIGR02204 537 TVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
106-686 |
2.42e-91 |
|
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: 295.86 E-value: 2.42e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 106 RAMMAYIWPKEDPLVRKRVGISLGLLAGSKLLTVCVPFLFKGAVDTMTTLnMDTAPDAVLsaatALMLGYGIARASAagf 185
Cdd:TIGR02203 3 RRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSV-LWWVPLVVI----GLAVLRGICSFVS--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 186 nelrNAVFAKVAHHSIRKIASNVFLHLHNLDLAFHLNKQTGALsktIDRGSRGINFVLSAMVFNIVPTIFELALVSSILG 265
Cdd:TIGR02203 75 ----TYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTL---LSRITFDSEQVASAATDAFIVLVRETLTVIGLFI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 266 VKCGLAFAgVSMGCVGIYAAYTLSVTQWRTQFRVF---MNQAENEAGNKAVDSLINYETVKYFNNEKYEAGCYNEVLKKY 342
Cdd:TIGR02203 148 VLLYYSWQ-LTLIVVVMLPVLSILMRRVSKRLRRIskeIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 343 EAASLKTSSSLALLNFGQNAIFSSALSLIMVLAAKEIAQGNMTVGDLVMVNALLFQLSIPLGFLGSVYREVRQALLDMRA 422
Cdd:TIGR02203 227 RRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAES 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 423 MFTLmnVDSSIQTAANAQPLfvDTTNSSIEFRNVSFEYEP-GKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFF 501
Cdd:TIGR02203 307 LFTL--LDSPPEKDTGTRAI--ERARGDVEFRNVTFRYPGrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 502 EPNSGKVLIGGQDISAVDLESLRKVIAVVPQDSVLFHNTIEHNIHYGNLSK-SHAEVQNAARMADLHDSIMSWPGQYSTQ 580
Cdd:TIGR02203 383 EPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQaDRAEIERALAAAYAQDFVDKLPLGLDTP 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 581 VGERGLKLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTRATSGRTSICIAHRLSTVKDADEILVLEN 660
Cdd:TIGR02203 463 IGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDD 542
|
570 580
....*....|....*....|....*.
gi 45551502 661 GRVGERGTHSELLRQNGLYARLWETQ 686
Cdd:TIGR02203 543 GRIVERGTHNELLARNGLYAQLHNMQ 568
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
451-677 |
3.21e-89 |
|
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: 278.34 E-value: 3.21e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIAVV 530
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 531 PQDSVLFHNTIEHNIHYGNLSKSHAEVQNAARMADLHDSIMSWPGQYSTQVGERGLKLSGGEKQRVAIARAILKNTPILI 610
Cdd:cd03254 83 LQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45551502 611 FDEATSSLDSITEHNILQALTRATSGRTSICIAHRLSTVKDADEILVLENGRVGERGTHSELLRQNG 677
Cdd:cd03254 163 LDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
183-686 |
5.06e-88 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 287.63 E-value: 5.06e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 183 AGFNELRNAVFAKVAHHSIR-------KIASNVFLHLHNLDLAFHLNKQTGALSKTIDRGSRG-----INFV---LSAMV 247
Cdd:PRK13657 63 AGFGLFNIIAGVLVARHADRlahrrrlAVLTEYFERIIQLPLAWHSQRGSGRALHTLLRGTDAlfglwLEFMrehLATLV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 248 --FNIVPTIF----ELALVSSILGVkcglafagvsmgcvgIYAAYTLSVTQwrtqfRVFMNQAENEAGN-----KAVDSL 316
Cdd:PRK13657 143 alVVLLPLALfmnwRLSLVLVVLGI---------------VYTLITTLVMR-----KTKDGQAAVEEHYhdlfaHVSDAI 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 317 INYETVKYFNNEKYEAGCYNEVLKKYEAASLKTSSSLALLNFGQNAifSSALSL--IMVLAAKEIAQGNMTVGDLVM--- 391
Cdd:PRK13657 203 GNVSVVQSYNRIEAETQALRDIADNLLAAQMPVLSWWALASVLNRA--ASTITMlaILVLGAALVQKGQLRVGEVVAfvg 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 392 -VNALLFQLSIPLGFLGSVYREVRQalldMRAMFTLMNVDSSIQTAANAQPLfvDTTNSSIEFRNVSFEYEPGKPIFRDL 470
Cdd:PRK13657 281 fATLLIGRLDQVVAFINQVFMAAPK----LEEFFEVEDAVPDVRDPPGAIDL--GRVKGAVEFDDVSFSYDNSRQGVEDV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 471 SFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIAVVPQDSVLFHNTIEHNIHYGNL 550
Cdd:PRK13657 355 SFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRP 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 551 SKSHAEVQNAARMADLHDSIMSWPGQYSTQVGERGLKLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQAL 630
Cdd:PRK13657 435 DATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAAL 514
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 45551502 631 TRATSGRTSICIAHRLSTVKDADEILVLENGRVGERGTHSELLRQNGLYARLWETQ 686
Cdd:PRK13657 515 DELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQ 570
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
118-677 |
1.00e-84 |
|
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: 278.18 E-value: 1.00e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 118 PLVRKRVGISLGLLAGSKLLTVCVPFLFKGAVDTMTtlnMDTAPDAVLSAATALMLGYGIARASAAGFNELRNAVFAKVA 197
Cdd:COG4988 13 RGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLI---IGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFRAAARV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 198 HHSIRKiasNVFLHLHNLDLAFHLNKQTGALSKTIdrgSRGI----NFV---LSAMVFNIVPTIFELALVSSIlGVKCGL 270
Cdd:COG4988 90 KRRLRR---RLLEKLLALGPAWLRGKSTGELATLL---TEGVealdGYFaryLPQLFLAALVPLLILVAVFPL-DWLSGL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 271 AFAG------VSMGCVGIYAAyTLSVTQWRTQFRVfmnqaeneaGNKAVDSLINYETVKYFNNEKYEAGCYNEVLKKYEA 344
Cdd:COG4988 163 ILLVtaplipLFMILVGKGAA-KASRRQWRALARL---------SGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 345 ASLKT-----SSSLALlnfgqnaIFSSALS--LIMVLAAKEIAQGNMTVGDLVMVnaLL-----FQlsiPLGFLGSVYRE 412
Cdd:COG4988 233 RTMKVlrvafLSSAVL-------EFFASLSiaLVAVYIGFRLLGGSLTLFAALFV--LLlapefFL---PLRDLGSFYHA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 413 VRQALLDMRAMFTLMNVDSSIQTAANAQPlfVDTTNSSIEFRNVSFEYEPGKPIFRDLSFTIPAGKNVAIVggsgsgkss 492
Cdd:COG4988 301 RANGIAAAEKIFALLDAPEPAAPAGTAPL--PAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVgpsgagkst 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 493 MVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIAVVPQDSVLFHNTIEHNIHYGNLSKSHAEVQNAARMADLHDSIMS 572
Cdd:COG4988 379 LLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAA 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 573 WPGQYSTQVGERGLKLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTRATSGRTSICIAHRLSTVKDA 652
Cdd:COG4988 459 LPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQA 538
|
570 580
....*....|....*....|....*
gi 45551502 653 DEILVLENGRVGERGTHSELLRQNG 677
Cdd:COG4988 539 DRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
119-687 |
9.14e-81 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 271.23 E-value: 9.14e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 119 LVRKRVGISLGLlagsKLLTVCVPFLFKGAVD------TMTTLNmdtapdaVLSAAtalMLGYGIARASAAGfneLRNAV 192
Cdd:TIGR01846 140 QFREVLLISLAL----QLFALVTPLLFQVVIDkvlvhrGLSTLS-------VLALA---MLAVAIFEPALGG---LRTYL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 193 FAKVAHHSIRKIASNVFLHLHNLDLAFHLNKQTGALSKTIDRGSRGINFVLSAMVFNIVPTIFELALVSSILGVKCGLAf 272
Cdd:TIGR01846 203 FAHLTSRIDVELGARLYRHLLGLPLGYFESRRVGDTVARVRELEQIRNFLTGSALTVVLDLLFVVVFLAVMFFYSPTLT- 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 273 aGVSMGCVGIYAAYTLSVTQwRTQFRVfMNQAENEAGNKA--VDSLINYETVKYFNNEKYEAGCYNEVLKKYEAASLKTS 350
Cdd:TIGR01846 282 -GVVIGSLVCYALLSVFVGP-ILRKRV-EDKFERSAAATSflVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVT 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 351 SSLALLNFGQNAIFSSALSLIMVLAAKEIAQGNMTVGDLVMVNALLFQLSIPLGFLGSVYREVRQALLDMRAMFTLMN-- 428
Cdd:TIGR01846 359 NLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILNsp 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 429 VDSSIQTAANAQPLfvdttNSSIEFRNVSFEYEPGKP-IFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGK 507
Cdd:TIGR01846 439 TEPRSAGLAALPEL-----RGAITFENIRFRYAPDSPeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQ 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 508 VLIGGQDISAVDLESLRKVIAVVPQDSVLFHNTIEHNIHYGNLSKSHAEVQNAARMADLHDSIMSWPGQYSTQVGERGLK 587
Cdd:TIGR01846 514 VLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGAN 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 588 LSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTRATSGRTSICIAHRLSTVKDADEILVLENGRVGERG 667
Cdd:TIGR01846 594 LSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESG 673
|
570 580
....*....|....*....|
gi 45551502 668 THSELLRQNGLYARLWETQT 687
Cdd:TIGR01846 674 RHEELLALQGLYARLWQQQS 693
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
98-682 |
5.30e-80 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 269.67 E-value: 5.30e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 98 EVTSKDMLRAMMAYIWPKedplvRKRVGISLGLLAGSKLLTVCVPFlFKGAVdtMTTLNMDTAPDAvLSAATALMLGYGI 177
Cdd:TIGR00958 142 QSETADLLFRLLGLSGRD-----WPWLISAFVFLTLSSLGEMFIPF-YTGRV--IDTLGGDKGPPA-LASAIFFMCLLSI 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 178 ARASAAGfneLRNAVFAKVAHHSIRKIASNVFLHLHNLDLAFHLNKQTGAL-----------SKTIdrgSRGINFVLSAM 246
Cdd:TIGR00958 213 ASSVSAG---LRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELtsrlssdtqtmSRSL---SLNVNVLLRNL 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 247 VFNIVPTIF------ELALVSSILgvkcgLAFAGVSMGCVGIYAAYTLSVTQwrtqfrvfmnQAENEAGNKAVDSLINYE 320
Cdd:TIGR00958 287 VMLLGLLGFmlwlspRLTMVTLIN-----LPLVFLAEKVFGKRYQLLSEELQ----------EAVAKANQVAEEALSGMR 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 321 TVKYFNNEKYEAGCYNEVLKkyEAASLKTSSSLALLNFGQNAIFSSALSLIMVLA--AKEIAQGNMTVGDLVmvNALLFQ 398
Cdd:TIGR00958 352 TVRSFAAEEGEASRFKEALE--ETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYygGQLVLTGKVSSGNLV--SFLLYQ 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 399 LSI--PLGFLGSVYREVRQALLDMRAMFTLMNVDSSIQTAANAQPLFVdttNSSIEFRNVSFEY--EPGKPIFRDLSFTI 474
Cdd:TIGR00958 428 EQLgeAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLNL---EGLIEFQDVSFSYpnRPDVPVLKGLTFTL 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 475 PAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIAVVPQDSVLFHNTIEHNIHYGNLSKSH 554
Cdd:TIGR00958 505 HPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPD 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 555 AEVQNAARMADLHDSIMSWPGQYSTQVGERGLKLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTRAt 634
Cdd:TIGR00958 585 EEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRA- 663
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 45551502 635 sGRTSICIAHRLSTVKDADEILVLENGRVGERGTHSELLRQNGLYARL 682
Cdd:TIGR00958 664 -SRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
451-686 |
3.77e-79 |
|
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: 252.41 E-value: 3.77e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPGKP-IFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIAV 529
Cdd:cd03252 1 ITFEHVRFRYKPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 530 VPQDSVLFHNTIEHNIHYGNLSKSHAEVQNAARMADLHDSIMSWPGQYSTQVGERGLKLSGGEKQRVAIARAILKNTPIL 609
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45551502 610 IFDEATSSLDSITEHNILQALTRATSGRTSICIAHRLSTVKDADEILVLENGRVGERGTHSELLRQNGLYARLWETQ 686
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
322-686 |
5.71e-78 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 260.72 E-value: 5.71e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 322 VKYFNNEKYEAGCYNEVLKKYEAASLKTSSSLALLNFGQNAIFSSALSLIMVLAAKEIAQGNMTVGDLVMVNALLFQLSI 401
Cdd:PRK11176 217 VLIFGGQEVETKRFDKVSNRMRQQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMR 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 402 PLGFLGSVYREVRQALLDMRAMFTLMNvdssIQTAANAQPLFVDTTNSSIEFRNVSFEYePGK--PIFRDLSFTIPAGKN 479
Cdd:PRK11176 297 PLKSLTNVNAQFQRGMAACQTLFAILD----LEQEKDEGKRVIERAKGDIEFRNVTFTY-PGKevPALRNINFKIPAGKT 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 480 VAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIAVVPQDSVLFHNTIEHNIHYGNLSK-SHAEVQ 558
Cdd:PRK11176 372 VALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 559 NAARMADLHDSIMSWPGQYSTQVGERGLKLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTRATSGRT 638
Cdd:PRK11176 452 EAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRT 531
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 45551502 639 SICIAHRLSTVKDADEILVLENGRVGERGTHSELLRQNGLYARLWETQ 686
Cdd:PRK11176 532 SLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
340-684 |
2.77e-76 |
|
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: 255.85 E-value: 2.77e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 340 KKYEAASLKTSSSLALLNFGQNAIFSSALSLIMVLAAKEIAQGNMTVGDLVMVnAL----LFQLSIPLGFLGSVYREVRQ 415
Cdd:COG4987 226 ARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALL-VLaalaLFEALAPLPAAAQHLGRVRA 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 416 ALldmRAMFTLMNVDSSIQTAANAQPLfvdTTNSSIEFRNVSFEYEP-GKPIFRDLSFTIPAGKNVAIVggsgsgkssmV 494
Cdd:COG4987 305 AA---RRLNELLDAPPAVTEPAEPAPA---PGGPSLELEDVSFRYPGaGRPVLDGLSLTLPPGERVAIVgpsgsgkstlL 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 495 RLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIAVVPQDSVLFHNTIEHNIHYGNLSKSHAEVQNAARMADLHDSIMSWP 574
Cdd:COG4987 379 ALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALP 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 575 GQYSTQVGERGLKLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTRATSGRTSICIAHRLSTVKDADE 654
Cdd:COG4987 459 DGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDR 538
|
330 340 350
....*....|....*....|....*....|
gi 45551502 655 ILVLENGRVGERGTHSELLRQNGLYARLWE 684
Cdd:COG4987 539 ILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| ABC_6TM_ABCB6 |
cd18581 |
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, ... |
128-423 |
2.96e-75 |
|
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: 244.46 E-value: 2.96e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 128 LGLLAGSKLLTVCVPFLFKGAVDTMTtlnmDTAPDAVLSAATALMLGYGIAR------ASAAGF-NELRNAVFAKVAHHS 200
Cdd:cd18581 2 LLLLAAGRVVNVLVPILYKKIVDSLT----PDSADSPLAFPWALILLYVFLKflqgggSGSVGLlSNLRSFLWIPVQQFT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 201 IRKIASNVFLHLHNLDLAFHLNKQTGALSKTIDRGSRGINFVLSAMVFNIVPTIFELALVSSILGVKCGLAFAGVSMGCV 280
Cdd:cd18581 78 TREISVKLFAHLHSLSLRWHLSRKTGEVLRVMDRGTSSINSLLSYVLFNIGPTIADIIIAIIYFAIAFNPWFGLIVFVTM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 281 GIYAAYTLSVTQWRTQFRVFMNQAENEAGNKAVDSLINYETVKYFNNEKYEAGCYNEVLKKYEAASLKTSSSLALLNFGQ 360
Cdd:cd18581 158 ALYLILTIIITEWRTKFRREMNKLDNEKRAKAVDSLLNFETVKYYNAERFEVERYRRAIDDYQVAEWKSNASLNLLNTAQ 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45551502 361 NAIFSSALSLIMVLAAKEIAQGNMTVGDLVMVNALLFQLSIPLGFLGSVYREVRQALLDMRAM 423
Cdd:cd18581 238 NLIITIGLLAGSLLCAYFVVEGKLTVGDFVLFLTYIIQLYAPLNFFGTYYRMIQQSFIDMENM 300
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
451-662 |
4.93e-69 |
|
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: 223.41 E-value: 4.93e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPG-KPIFRDLSFTIPAGKNVAIVggsgsgkssMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIAV 529
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVgpsgsgkstLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 530 VPQDSVLFHNTIEHNIhygnlskshaevqnaarmadlhdsimswpgqystqvgerglkLSGGEKQRVAIARAILKNTPIL 609
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 45551502 610 IFDEATSSLDSITEHNILQALTRATSGRTSICIAHRLSTVKDADEILVLENGR 662
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
171-682 |
7.43e-69 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 239.08 E-value: 7.43e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 171 LMLGYGIARASAAGFNELRNAVFAKVAHHSIRKIASNVFLHLHNLDLAFHLNKQTGALSKTI---DRGSRGINFVLSAMV 247
Cdd:TIGR03796 196 LLLGMGLTALLQGVLTWLQLYYLRRLEIKLAVGMSARFLWHILRLPVRFFAQRHAGDIASRVqlnDQVAEFLSGQLATTA 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 248 FNIVPTIFELALV---SSILGVkCGLAFAGVSMGcvgiyaaytlsVTQWRTQFRVFMNQA----ENEAGNKAVDSLINYE 320
Cdd:TIGR03796 276 LDAVMLVFYALLMllyDPVLTL-IGIAFAAINVL-----------ALQLVSRRRVDANRRlqqdAGKLTGVAISGLQSIE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 321 TVKyfnnekyEAGCYNEVLKK---YEAASLKTSSSLALLN--FGQNAIFSSALS--LIMVLAAKEIAQGNMTVGDLVMVN 393
Cdd:TIGR03796 344 TLK-------ASGLESDFFSRwagYQAKLLNAQQELGVLTqiLGVLPTLLTSLNsaLILVVGGLRVMEGQLTIGMLVAFQ 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 394 ALLFQLSIPL----GFLGSvyrevrqaLLDMRAmfTLMNVDSSIQTAANaqPLFVDTTNSS------------IEFRNVS 457
Cdd:TIGR03796 417 SLMSSFLEPVnnlvGFGGT--------LQELEG--DLNRLDDVLRNPVD--PLLEEPEGSAatsepprrlsgyVELRNIT 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 458 FEYEP-GKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIAVVPQDSVL 536
Cdd:TIGR03796 485 FGYSPlEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFL 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 537 FHNTIEHNIHYGNLSKSHAEVQNAARMADLHDSIMSWPGQYSTQVGERGLKLSGGEKQRVAIARAILKNTPILIFDEATS 616
Cdd:TIGR03796 565 FEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATS 644
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45551502 617 SLDSITEHNILQALTRatSGRTSICIAHRLSTVKDADEILVLENGRVGERGTHSELLRQNGLYARL 682
Cdd:TIGR03796 645 ALDPETEKIIDDNLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARL 708
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
137-685 |
1.34e-66 |
|
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: 230.16 E-value: 1.34e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 137 LTVCVPFLFKGAVDTMTTlNMDTAPdavlsaATALMLGYGIarasaagFNELRNAVFAK----VAHHSIRKIASNVFLHL 212
Cdd:TIGR01192 34 ITIAEPILFGRIIDAISS-KSDVLP------TLALWAGFGV-------FNTIAYVLVAReadrLAHGRRATLLTEAFGRI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 213 HNLDLAFHLNKQTGALSKTIDRGSRGINFV--------LSAMV--FNIVPTIFELALVSSILgvkcglafagvsmgCVGI 282
Cdd:TIGR01192 100 ISMPLSWHQQRGTSNALHTLLRATETLFGLwlefmrqhLATFValFLLIPTAFAMDWRLSIV--------------LMVL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 283 YAAYTLsVTQWRTQfRVFMNQAENEAGNKAV-----DSLINYETVKYFNNEKYEAGCYNEVLKKYEAASLKTSSSLALLN 357
Cdd:TIGR01192 166 GILYIL-IAKLVMQ-RTKNGQAAVEHHYHNVfkhvsDSISNVSVVHSYNRIEAETSALKQFTNNLLSAQYPVLDWWALAS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 358 fGQNAIFSS-ALSLIMVLAAKEIAQGNMTVGDLV----MVNALLFQLSIPLGFLGSVYrEVRQALLDMRAMftlmnVDSS 432
Cdd:TIGR01192 244 -GLNRMASTiSMMCILVIGTVLVIKGELSVGEVIafigFANLLIGRLDQMSGFITQIF-EARAKLEDFFDL-----EDSV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 433 IQTAANAQPLFVDTTNSSIEFRNVSFEYEPGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGG 512
Cdd:TIGR01192 317 FQREEPADAPELPNVKGAVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 513 QDISAVDLESLRKVIAVVPQDSVLFHNTIEHNIHYGNLSKSHAEVQNAARMADLHDSIMSWPGQYSTQVGERGLKLSGGE 592
Cdd:TIGR01192 397 IDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 593 KQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTRATSGRTSICIAHRLSTVKDADEILVLENGRVGERGTHSEL 672
Cdd:TIGR01192 477 RQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQEL 556
|
570
....*....|...
gi 45551502 673 LRQNGLYARLWET 685
Cdd:TIGR01192 557 IQKDGRFYKLLRR 569
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
451-663 |
1.29e-60 |
|
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: 203.09 E-value: 1.29e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEY--EPGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIA 528
Cdd:cd03248 12 VKFQNVTFAYptRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 529 VVPQDSVLFHNTIEHNIHYGNLSKSHAEVQNAARMADLHDSIMSWPGQYSTQVGERGLKLSGGEKQRVAIARAILKNTPI 608
Cdd:cd03248 92 LVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 45551502 609 LIFDEATSSLDSITEHNILQALTRATSGRTSICIAHRLSTVKDADEILVLENGRV 663
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
450-668 |
6.89e-60 |
|
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: 200.80 E-value: 6.89e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 450 SIEFRNVSFEYEPG-KPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIA 528
Cdd:cd03244 2 DIEFKNVSLRYRPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 529 VVPQDSVLFHNTIEHNIHYGNLSkSHAEVQNAARMADLHDSIMSWPGQYSTQVGERGLKLSGGEKQRVAIARAILKNTPI 608
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLDPFGEY-SDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 609 LIFDEATSSLDSITEHNILQALTRATSGRTSICIAHRLSTVKDADEILVLENGRVGERGT 668
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
202-682 |
1.22e-57 |
|
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: 208.05 E-value: 1.22e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 202 RKIASNVFLHLHNLDLAFHLNKQTGALSKTIDRGSRGINfVLSAMVFNIVPTIFELALVSSILGVKCGLAFAgVSMGCVG 281
Cdd:TIGR01193 229 IDIILSYIKHLFELPMSFFSTRRTGEIVSRFTDASSIID-ALASTILSLFLDMWILVIVGLFLVRQNMLLFL-LSLLSIP 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 282 IYAAYTLSVtqwrtqFRVF--MNQAENEAG---NKAV-DSLINYETVKYFNNEkyeAGCYNEVLKKYEAAsLKTSSSLAL 355
Cdd:TIGR01193 307 VYAVIIILF------KRTFnkLNHDAMQANavlNSSIiEDLNGIETIKSLTSE---AERYSKIDSEFGDY-LNKSFKYQK 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 356 LNFGQNAIFS-SALSLIMVL---AAKEIAQGNMTVGDLVMVNALLFQLSIPLGFLGSVYREVRQALLDMRAMFTLMNVDS 431
Cdd:TIGR01193 377 ADQGQQAIKAvTKLILNVVIlwtGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDS 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 432 SIQTAANAQPLfvDTTNSSIEFRNVSFEYEPGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIG 511
Cdd:TIGR01193 457 EFINKKKRTEL--NNLNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLN 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 512 GQDISAVDLESLRKVIAVVPQDSVLFHNTIEHNIHYGNLSK-SHAEVQNAARMADLHDSIMSWPGQYSTQVGERGLKLSG 590
Cdd:TIGR01193 535 GFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKENvSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISG 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 591 GEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTRATSgRTSICIAHRLSTVKDADEILVLENGRVGERGTHS 670
Cdd:TIGR01193 615 GQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHD 693
|
490
....*....|..
gi 45551502 671 ELLRQNGLYARL 682
Cdd:TIGR01193 694 ELLDRNGFYASL 705
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
180-423 |
3.32e-56 |
|
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: 193.51 E-value: 3.32e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 180 ASAAGFNELRNAVFAKVAHHSIRKIASNVFLHLHNLDLAFHLNKQTGALSKTIDRGSrGINFVLSAMVFNIVPTIFELAL 259
Cdd:cd18583 48 QSGGGLGLLRSWLWIPVEQYSYRALSTAAFNHVMNLSMDFHDSKKSGEVLKAIEQGS-SINDLLEQILFQIVPMIIDLVI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 260 VSSILGVKCGLAFAGVsMGCVGI-YAAYTLSVTQWRTQFRVFMNQAENEAGNKAVDSLINYETVKYFNNEKYEAGCYNEV 338
Cdd:cd18583 127 AIVYLYYLFDPYMGLI-VAVVMVlYVWSTIKLTSWRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYREA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 339 LKKYEAASLKTSSSLALLNFGQNAIFSSALSLIMVLAAKEIAQGNMTVGDLVMVNALLFQLSIPLGFLGSVYREVRQALL 418
Cdd:cd18583 206 VKNYQKAERKYLFSLNLLNAVQSLILTLGLLAGCFLAAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDLI 285
|
....*
gi 45551502 419 DMRAM 423
Cdd:cd18583 286 DAERL 290
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
431-702 |
3.55e-56 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 201.09 E-value: 3.55e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 431 SSIQTAANAQPLFVDTTNSSIEFRNV------SFEYePG--KPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFE 502
Cdd:PRK10789 288 SRIRAMLAEAPVVKDGSEPVPEGRGEldvnirQFTY-PQtdHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFD 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 503 PNSGKVLIGGQDISAVDLESLRKVIAVVPQDSVLFHNTIEHNIHYGNLSKSHAEVQNAARMADLHDSIMSWPGQYSTQVG 582
Cdd:PRK10789 367 VSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVG 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 583 ERGLKLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTRATSGRTSICIAHRLSTVKDADEILVLENGR 662
Cdd:PRK10789 447 ERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGH 526
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 45551502 663 VGERGTHSELLRQNGLYARLWETQTQQ--FDPSREINEEVAA 702
Cdd:PRK10789 527 IAQRGNHDQLAQQSGWYRDMYRYQQLEaaLDDAPEIREEAVD 568
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
450-663 |
1.92e-54 |
|
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: 186.26 E-value: 1.92e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 450 SIEFRNVSFEYePGKPI--FRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVI 527
Cdd:cd03245 2 RIEFRNVSFSY-PNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 528 AVVPQDSVLFHNTIEHNIHYGNLSKSHAEVQNAARMADLHDSIMSWPGQYSTQVGERGLKLSGGEKQRVAIARAILKNTP 607
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 45551502 608 ILIFDEATSSLDSITEHNILQALTRATSGRTSICIAHRLSTVKDADEILVLENGRV 663
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
122-658 |
6.80e-50 |
|
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: 182.87 E-value: 6.80e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 122 KRVGISLGLLAG-SKLLTVCVPFLFKGAVDTmttLNMDTAPDAVLSAATALMLGYGIARASAAGFNELRNAVFAKVAHHS 200
Cdd:TIGR02857 2 RRALALLALLGVlGALLIIAQAWLLARVVDG---LISAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 201 IRKIASNVFLHLHNLDLAFhlnKQTGALSKTIDRG--------SRGINFVLSAMvfnIVPTIFELAL----VSSILGVKC 268
Cdd:TIGR02857 79 LRERLLEAVAALGPRWLQG---RPSGELATLALEGvealdgyfARYLPQLVLAV---IVPLAILAAVfpqdWISGLILLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 269 GLAFAGVSMGCVGiYAAYTLSVTQWRTQFRVfmnqaeneaGNKAVDSLINYETVKYFNNEKYEAGCYNEVLKKYEAASLK 348
Cdd:TIGR02857 153 TAPLIPIFMILIG-WAAQAAARKQWAALSRL---------SGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 349 TS-----SSLALLnfgqnaiFSSALSLIMVlaAKEIAQgNMTVGDLVMVNALL-------FQLsiPLGFLGSVYREVRQA 416
Cdd:TIGR02857 223 VLriaflSSAVLE-------LFATLSVALV--AVYIGF-RLLAGDLDLATGLFvlllapeFYL--PLRQLGAQYHARADG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 417 LLDMRAMFTLMnvDSSIQTAANAQPLFvDTTNSSIEFRNVSFEYEPGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRL 496
Cdd:TIGR02857 291 VAAAEALFAVL--DAAPRPLAGKAPVT-AAPASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNL 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 497 LFRFFEPNSGKVLIGGQDISAVDLESLRKVIAVVPQDSVLFHNTIEHNIHYGNLSKSHAEVQNAARMADLHDSIMSWPGQ 576
Cdd:TIGR02857 368 LLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQG 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 577 YSTQVGERGLKLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTRATSGRTSICIAHRLSTVKDADEIL 656
Cdd:TIGR02857 448 LDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIV 527
|
..
gi 45551502 657 VL 658
Cdd:TIGR02857 528 VL 529
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
402-689 |
1.33e-48 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 180.43 E-value: 1.33e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 402 PLGFLGSVYREVRQALLDMRAMFTLMNVDSSiQTAANAQPLFVDTTNSsIEFRNVS-FEYEpGKPIFRDLSFTIPAGKNV 480
Cdd:PRK11174 303 PLRDLGTFYHAKAQAVGAAESLVTFLETPLA-HPQQGEKELASNDPVT-IEAEDLEiLSPD-GKTLAGPLNFTLPAGQRI 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 481 AIVGGSGSGKSSMVRLLFRFFePNSGKVLIGGQDISAVDLESLRKVIAVVPQDSVLFHNTIEHNIHYGNLSKSHAEVQNA 560
Cdd:PRK11174 380 ALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQA 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 561 ARMADLHDSIMSWPGQYSTQVGERGLKLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTRATSGRTSI 640
Cdd:PRK11174 459 LENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTL 538
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 45551502 641 CIAHRLSTVKDADEILVLENGRVGERGTHSELLRQNGLYARLWETQTQQ 689
Cdd:PRK11174 539 MVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQEE 587
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
382-686 |
8.61e-47 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 175.29 E-value: 8.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 382 GNMTVGDLVMVNALLFQLSIPLGFLGSVYREVRQALLDMRAMFTLMnvDSSIQTAAN-AQPLfvdtTNSSIEFRNVSFEY 460
Cdd:PRK10790 277 GTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELM--DGPRQQYGNdDRPL----QSGRIDIDNVSFAY 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 461 EPGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIAVVPQDSVLFHNT 540
Cdd:PRK10790 351 RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADT 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 541 IEHNIHYG-NLSKSHA-EVQNAARMADLhdsIMSWPGQYSTQVGERGLKLSGGEKQRVAIARAILKNTPILIFDEATSSL 618
Cdd:PRK10790 431 FLANVTLGrDISEEQVwQALETVQLAEL---ARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANI 507
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45551502 619 DSITEHNILQALTRATSGRTSICIAHRLSTVKDADEILVLENGRVGERGTHSELLRQNGLYARLWETQ 686
Cdd:PRK10790 508 DSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQ 575
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
450-668 |
1.25e-45 |
|
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: 161.81 E-value: 1.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 450 SIEFRNVSFEYEPGKP-IFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIA 528
Cdd:cd03369 6 EIEVENLSVRYAPDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 529 VVPQDSVLFHNTIEHNI----HYgnlskSHAEVQNAARmadlhdsimswpgqystqVGERGLKLSGGEKQRVAIARAILK 604
Cdd:cd03369 86 IIPQDPTLFSGTIRSNLdpfdEY-----SDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45551502 605 NTPILIFDEATSSLDSITEHNILQALTRATSGRTSICIAHRLSTVKDADEILVLENGRVGERGT 668
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
446-684 |
3.70e-43 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 164.61 E-value: 3.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 446 TTNSSIEFRNVSFEYEPGK-PIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLR 524
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDQPqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 525 KVIAVVPQDSVLFHNTIEHNIHYGNLSKSHAEVQNAARMADLHDSIMSWPGqYSTQVGERGLKLSGGEKQRVAIARAILK 604
Cdd:PRK11160 414 QAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLEDDKG-LNAWLGEGGRQLSGGEQRRLGIARALLH 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 605 NTPILIFDEATSSLDSITEHNILQALTRATSGRTSICIAHRLSTVKDADEILVLENGRVGERGTHSELLRQNGLYARLWE 684
Cdd:PRK11160 493 DAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQ 572
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
451-663 |
1.08e-42 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 152.37 E-value: 1.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPGK-PIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIAV 529
Cdd:cd03246 1 LEVENVSFRYPGAEpPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 530 VPQDSVLFHNTIEHNIhygnlskshaevqnaarmadlhdsimswpgqystqvgerglkLSGGEKQRVAIARAILKNTPIL 609
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 45551502 610 IFDEATSSLDSITEHNILQALTRATS-GRTSICIAHRLSTVKDADEILVLENGRV 663
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
313-681 |
9.35e-42 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 164.05 E-value: 9.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 313 VDSLINYETVKYFNNEKYEAGCYNEVLKKYeaaslKTSSSLALLNFGQNAIFSSAlSLIMVLAAKEIAQGNMTVGDLVM- 391
Cdd:PTZ00265 1032 MNTVIIYGLEDYFCNLIEKAIDYSNKGQKR-----KTLVNSMLWGFSQSAQLFIN-SFAYWFGSFLIRRGTILVDDFMKs 1105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 392 VNALLFQLSIPlGFLGSVYREVRQALLDMRAMFTLMNVDSSIQTAANAQpLFVDTTN---SSIEFRNVSFEY--EPGKPI 466
Cdd:PTZ00265 1106 LFTFLFTGSYA-GKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGG-IRIKNKNdikGKIEIMDVNFRYisRPNVPI 1183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 467 FRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFE-------------------------------------------- 502
Cdd:PTZ00265 1184 YKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltke 1263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 503 ----------PNSGKVLIGGQDISAVDLESLRKVIAVVPQDSVLFHNTIEHNIHYGNLSKSHAEVQNAARMADLHDSIMS 572
Cdd:PTZ00265 1264 ggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIES 1343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 573 WPGQYSTQVGERGLKLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALT--RATSGRTSICIAHRLSTVK 650
Cdd:PTZ00265 1344 LPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdiKDKADKTIITIAHRIASIK 1423
|
410 420 430
....*....|....*....|....*....|....*..
gi 45551502 651 DADEILVLEN-GRVGE----RGTHSELLR-QNGLYAR 681
Cdd:PTZ00265 1424 RSDKIVVFNNpDRTGSfvqaHGTHEELLSvQDGVYKK 1460
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
332-646 |
7.72e-41 |
|
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: 157.14 E-value: 7.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 332 AGCYNEVLKKYEAASL-------KTSSSLALLNFGQNAIFSSALSLIMVLAAKEIAQGNM---TVGDLVMVNALLFQLSI 401
Cdd:TIGR02868 209 SGALPAALAQVEEADReltraerRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLapvTLAVLVLLPLAAFEAFA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 402 PLGFLGSVYREVRQALldmRAMFTLMNVDSSIQTAANAQPLFVDTTNSSIEFRNVSFEYEPGKPIFRDLSFTIPAGKNVA 481
Cdd:TIGR02868 289 ALPAAAQQLTRVRAAA---ERIVEVLDAAGPVAEGSAPAAGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 482 IVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIAVVPQDSVLFHNTIEHNIHYGNLSKSHAEVQNAA 561
Cdd:TIGR02868 366 ILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAAL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 562 RMADLHDSIMSWPGQYSTQVGERGLKLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTRATSGRTSIC 641
Cdd:TIGR02868 446 ERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVL 525
|
....*
gi 45551502 642 IAHRL 646
Cdd:TIGR02868 526 ITHHL 530
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
451-667 |
3.84e-40 |
|
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: 145.15 E-value: 3.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEP-GKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDlESLRKVIAV 529
Cdd:cd03247 1 LSINNVSFSYPEqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 530 VPQDSVLFHNTIEHNIhygnlskshaevqnaarmadlhdsimswpgqystqvgerGLKLSGGEKQRVAIARAILKNTPIL 609
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 45551502 610 IFDEATSSLDSITEHNILQALTRATSGRTSICIAHRLSTVKDADEILVLENGRVGERG 667
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
450-675 |
1.11e-39 |
|
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: 154.14 E-value: 1.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 450 SIEFRNVSFEYePG--KPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVI 527
Cdd:COG4618 330 RLSVENLTVVP-PGskRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHI 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 528 AVVPQDSVLFHNTIEHNI-HYGNLSKshAEVQNAARMADLHDSIMSWPGQYSTQVGERGLKLSGGEKQRVAIARAILKNT 606
Cdd:COG4618 409 GYLPQDVELFDGTIAENIaRFGDADP--EKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDP 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 607 PILIFDEATSSLDSITEHNILQALTRA-TSGRTSICIAHRLSTVKDADEILVLENGRVGERGTHSELLRQ 675
Cdd:COG4618 487 RLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
451-679 |
4.60e-38 |
|
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: 152.79 E-value: 4.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPG-KPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIAV 529
Cdd:TIGR00957 1285 VEFRNYCLRYREDlDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITI 1364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 530 VPQDSVLFHNTIEHNIH-YGnlSKSHAEVQNAARMADLHDSIMSWPGQYSTQVGERGLKLSGGEKQRVAIARAILKNTPI 608
Cdd:TIGR00957 1365 IPQDPVLFSGSLRMNLDpFS--QYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKI 1442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45551502 609 LIFDEATSSLDSITEhNILQALTRAT-SGRTSICIAHRLSTVKDADEILVLENGRVGERGTHSELLRQNGLY 679
Cdd:TIGR00957 1443 LVLDEATAAVDLETD-NLIQSTIRTQfEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIF 1513
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
399-668 |
5.03e-38 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 152.49 E-value: 5.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 399 LSIPLGFLGSVY---------REVRQALLDMRAMFTLMNVDSSIQTAANAQPLfvdTTNSSIEFRNVSFEYEPGK--PIF 467
Cdd:PTZ00265 325 ISILLGVLISMFmltiilpniTEYMKSLEATNSLYEIINRKPLVENNDDGKKL---KDIKKIQFKNVRFHYDTRKdvEIY 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 468 RDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIG-GQDISAVDLESLRKVIAVVPQDSVLFHNTIEHNIH 546
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIK 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 547 Y------------------GNLSKSH---------------------------------------AEVQNAARMADLHDS 569
Cdd:PTZ00265 482 YslyslkdlealsnyynedGNDSQENknkrnscrakcagdlndmsnttdsneliemrknyqtikdSEVVDVSKKVLIHDF 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 570 IMSWPGQYSTQVGERGLKLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALT--RATSGRTSICIAHRLS 647
Cdd:PTZ00265 562 VSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLS 641
|
330 340
....*....|....*....|.
gi 45551502 648 TVKDADEILVLENGRVGERGT 668
Cdd:PTZ00265 642 TIRYANTIFVLSNRERGSTVD 662
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
451-675 |
6.32e-38 |
|
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: 140.93 E-value: 6.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPGKPIFRDLSFTIPAGKNVAIVggsgsgkssMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIAVV 530
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIgpngsgkstLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 531 PQ--DSVLFHNTIEHNIHYG--NLSKSHAEVQNAARMAdLhdsimswpgqysTQVGERGLK------LSGGEKQRVAIAR 600
Cdd:COG1122 81 FQnpDDQLFAPTVEEDVAFGpeNLGLPREEIRERVEEA-L------------ELVGLEHLAdrppheLSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45551502 601 AILKNTPILIFDEATSSLDSITEHNILQALTR-ATSGRTSICIAHRLSTVKD-ADEILVLENGRVGERGTHSELLRQ 675
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSD 224
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
451-663 |
3.18e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 135.33 E-value: 3.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEpGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIAVV 530
Cdd:COG4619 1 LELEGLSFRVG-GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 531 PQDSVLFHNTIEHNI----HYGNLSKSHAEVQNAARMADLHDSIMSWPgqystqVGErglkLSGGEKQRVAIARAILKNT 606
Cdd:COG4619 80 PQEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLGLPPDILDKP------VER----LSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45551502 607 PILIFDEATSSLDSITEHNILQALTR--ATSGRTSICIAH------RLstvkdADEILVLENGRV 663
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
450-677 |
2.06e-35 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 144.50 E-value: 2.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 450 SIEFRNVSFEYEPG-KPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIA 528
Cdd:PLN03130 1237 SIKFEDVVLRYRPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLG 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 529 VVPQDSVLFHNTIEHNIHYGNlSKSHAEVQNAARMADLHDSIMSWPGQYSTQVGERGLKLSGGEKQRVAIARAILKNTPI 608
Cdd:PLN03130 1317 IIPQAPVLFSGTVRFNLDPFN-EHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKI 1395
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45551502 609 LIFDEATSSLDSITEHNILQALTRATSGRTSICIAHRLSTVKDADEILVLENGRVGERGTHSELLRQNG 677
Cdd:PLN03130 1396 LVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
438-677 |
4.13e-35 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 143.58 E-value: 4.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 438 NAQPLFVDTTNSSIEFRNVSFEYEPG-KPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDIS 516
Cdd:PLN03232 1222 NNRPVSGWPSRGSIKFEDVHLRYRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVA 1301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 517 AVDLESLRKVIAVVPQDSVLFHNTIEHNIHYGNlSKSHAEVQNAARMADLHDSIMSWPGQYSTQVGERGLKLSGGEKQRV 596
Cdd:PLN03232 1302 KFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFS-EHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLL 1380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 597 AIARAILKNTPILIFDEATSSLDSITEHNILQALTRATSGRTSICIAHRLSTVKDADEILVLENGRVGERGTHSELLRQN 676
Cdd:PLN03232 1381 SLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRD 1460
|
.
gi 45551502 677 G 677
Cdd:PLN03232 1461 T 1461
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
451-674 |
1.64e-34 |
|
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: 131.47 E-value: 1.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEpGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDI---SAVDLESLRKVI 527
Cdd:cd03261 1 IELRGLTKSFG-GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglSEAELYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 528 AVVPQDSVLF-HNTIEHNI-----HYGNLSKShaEVQNAAR----MADLHDSIMSWPGQystqvgerglkLSGGEKQRVA 597
Cdd:cd03261 80 GMLFQSGALFdSLTVFENVafplrEHTRLSEE--EIREIVLekleAVGLRGAEDLYPAE-----------LSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 598 IARAILKNTPILIFDEATSSLDSITEHNILQ--ALTRATSGRTSICIAHRLSTVKD-ADEILVLENGRVGERGTHSELLR 674
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDliRSLKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
451-674 |
2.51e-34 |
|
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: 131.27 E-value: 2.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIAVV 530
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 531 PQDSVLF-HNTIEHNIhyGNLSK----SHAEVQNAAR--MADLHDSIMSWPGQYSTQvgerglkLSGGEKQRVAIARAIL 603
Cdd:cd03295 81 IQQIGLFpHMTVEENI--ALVPKllkwPKEKIRERADelLALVGLDPAEFADRYPHE-------LSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45551502 604 KNTPILIFDEATSSLDSITEHNILQALTR--ATSGRTSICIAHRL-STVKDADEILVLENGRVGERGTHSELLR 674
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRlqQELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
452-662 |
1.77e-33 |
|
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: 127.58 E-value: 1.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 452 EFRNVSFEYEPG-KPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIAVV 530
Cdd:cd03225 1 ELKNLSFSYPDGaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 531 PQ--DSVLFHNTIEHNIHYG--NLSKSHAEVQNAARmadlhdsimswpgQYSTQVGERGLK------LSGGEKQRVAIAR 600
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVAFGleNLGLPEEEIEERVE-------------EALELVGLEGLRdrspftLSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45551502 601 AILKNTPILIFDEATSSLDSITEHNILQALTR-ATSGRTSICIAHRLSTVKD-ADEILVLENGR 662
Cdd:cd03225 148 VLAMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
445-673 |
2.90e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 126.26 E-value: 2.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 445 DTTNSSIEFRNVSFEYEPG-KPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESL 523
Cdd:PRK13632 2 KNKSVMIKVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 524 RKVIAVVPQ--DSVLFHNTIEHNIHYGNLSKShaevQNAARMADLHDSimswpgqYSTQVG-ERGLK-----LSGGEKQR 595
Cdd:PRK13632 82 RKKIGIIFQnpDNQFIGATVEDDIAFGLENKK----VPPKKMKDIIDD-------LAKKVGmEDYLDkepqnLSGGQKQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 596 VAIARAILKNTPILIFDEATSSLDSITEHNILQALT--RATSGRTSICIAHRLSTVKDADEILVLENGRVGERGTHSELL 673
Cdd:PRK13632 151 VAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVdlRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
451-675 |
1.01e-31 |
|
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: 123.46 E-value: 1.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPGK---PIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKV- 526
Cdd:cd03258 2 IELKNVSKVFGDTGgkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 527 --IAVVPQDSVLFHN-TIEHNIHY----GNLSKSHAE--VQNAARMADLHDSIMSWPGQystqvgerglkLSGGEKQRVA 597
Cdd:cd03258 82 rrIGMIFQHFNLLSSrTVFENVALpleiAGVPKAEIEerVLELLELVGLEDKADAYPAQ-----------LSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 598 IARAILKNTPILIFDEATSSLDSITEHNILQALTR--ATSGRTSICIAHRLSTVKD-ADEILVLENGRVGERGTHSELLR 674
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFA 230
|
.
gi 45551502 675 Q 675
Cdd:cd03258 231 N 231
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
452-662 |
4.64e-31 |
|
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: 118.89 E-value: 4.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 452 EFRNVSFEYePGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIAVVP 531
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 532 QdsvlfhntiehnihygnlskshaevqnaarmadlhdsimswpgqystqvgerglkLSGGEKQRVAIARAILKNTPILIF 611
Cdd:cd00267 80 Q-------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 45551502 612 DEATSSLDSITEHNILQALTR-ATSGRTSICIAHRLSTVKDA-DEILVLENGR 662
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
451-667 |
5.97e-31 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 121.07 E-value: 5.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPGK---PIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVD---LESLR 524
Cdd:cd03257 2 LEVKNLSVSFPTGGgsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 525 KVIAVVPQDSVLFHN---TIEHNI------HYGNLSKSHAEVQNAARMADLHDSImSWPGQYSTQvgerglkLSGGEKQR 595
Cdd:cd03257 82 KEIQMVFQDPMSSLNprmTIGEQIaeplriHGKLSKKEARKEAVLLLLVGVGLPE-EVLNRYPHE-------LSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45551502 596 VAIARAILKNTPILIFDEATSSLDSITEHNILQALTRATS--GRTSICIAHRLSTVKD-ADEILVLENGRVGERG 667
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
451-685 |
1.26e-30 |
|
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: 121.17 E-value: 1.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPG-KPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIAV 529
Cdd:cd03288 20 IKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 530 VPQDSVLFHNTIEHNIHyGNLSKSHAEVQNAARMADLHDSIMSWPGQYSTQVGERGLKLSGGEKQRVAIARAILKNTPIL 609
Cdd:cd03288 100 ILQDPILFSGSIRFNLD-PECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSIL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45551502 610 IFDEATSSLDSITEhNILQALT-RATSGRTSICIAHRLSTVKDADEILVLENGRVGERGTHSELLRQ-NGLYARLWET 685
Cdd:cd03288 179 IMDEATASIDMATE-NILQKVVmTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQeDGVFASLVRT 255
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
451-678 |
1.74e-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: 121.00 E-value: 1.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPG-KPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVD-LESLRKVIA 528
Cdd:TIGR04520 1 IEVENVSFSYPESeKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEnLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 529 VVPQ--DSVLFHNTIEHNIHYG--NLSKSHAE----VQNAARMADLHDSIMSWPgqystqvgergLKLSGGEKQRVAIAR 600
Cdd:TIGR04520 81 MVFQnpDNQFVGATVEDDVAFGleNLGVPREEmrkrVDEALKLVGMEDFRDREP-----------HLLSGGQKQRVAIAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 601 AILKNTPILIFDEATSSLDSITEHNILQALT--RATSGRTSICIAHRLSTVKDADEILVLENGRVGERGT------HSEL 672
Cdd:TIGR04520 150 VLAMRPDIIILDEATSMLDPKGRKEVLETIRklNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTpreifsQVEL 229
|
....*.
gi 45551502 673 LRQNGL 678
Cdd:TIGR04520 230 LKEIGL 235
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
451-662 |
1.84e-30 |
|
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: 118.06 E-value: 1.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYePGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLES--LRKVIA 528
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 529 VVPQDSVLF-HNTIEHNIHYGnlskshaevqnaarmadlhdsimswpgqystqvgerglkLSGGEKQRVAIARAILKNTP 607
Cdd:cd03229 80 MVFQDFALFpHLTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 45551502 608 ILIFDEATSSLDSITEhNILQALTR---ATSGRTSICIAHRLSTV-KDADEILVLENGR 662
Cdd:cd03229 121 VLLLDEPTSALDPITR-REVRALLKslqAQLGITVVLVTHDLDEAaRLADRVVVLRDGK 178
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
451-673 |
3.44e-30 |
|
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: 119.76 E-value: 3.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYePGKPIFRDLSFTIPAGKNVAIVggsgsgkssMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIAVV 530
Cdd:COG1120 2 LEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLgpngsgkstLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 531 PQDSVL-FHNTIE---------HNIHYGNLSKS-HAEVQNAARMADLHDsimsWPGQYSTQvgerglkLSGGEKQRVAIA 599
Cdd:COG1120 81 PQEPPApFGLTVRelvalgrypHLGLFGRPSAEdREAVEEALERTGLEH----LADRPVDE-------LSGGERQRVLIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 600 RAILKNTPILIFDEATSSLDsITeH-----NILQALTRaTSGRTSICIAHrlstvkD-------ADEILVLENGRVGERG 667
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLD-LA-HqlevlELLRRLAR-ERGRTVVMVLH------DlnlaaryADRLVLLKDGRIVAQG 220
|
....*.
gi 45551502 668 THSELL 673
Cdd:COG1120 221 PPEEVL 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
451-674 |
4.32e-30 |
|
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: 118.93 E-value: 4.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEpGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVD---LESLRKVI 527
Cdd:COG1127 6 IEVRNLTKSFG-DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 528 AVVPQDSVLFHN-TIEHNI-----HYGNLSKshAEVQNAARMA----DLHDSIMSWPGQystqvgerglkLSGGEKQRVA 597
Cdd:COG1127 85 GMLFQGGALFDSlTVFENVafplrEHTDLSE--AEIRELVLEKlelvGLPGAADKMPSE-----------LSGGMRKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 598 IARAILKNTPILIFDEATSSLDSITEHNILQaL---TRATSGRTSICIAHRLSTVKD-ADEILVLENGRVGERGTHSELL 673
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDPITSAVIDE-LireLRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELL 230
|
.
gi 45551502 674 R 674
Cdd:COG1127 231 A 231
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
451-663 |
8.11e-30 |
|
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: 117.24 E-value: 8.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEpGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLEslRKVIAVV 530
Cdd:cd03259 1 LELKGLSKTYG-SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 531 PQDSVLF-HNTIEHNIHYG--NLSKSHAE----VQNAARMADLHDSIMSWPGQystqvgerglkLSGGEKQRVAIARAIL 603
Cdd:cd03259 78 FQDYALFpHLTVAENIAFGlkLRGVPKAEirarVRELLELVGLEGLLNRYPHE-----------LSGGQQQRVALARALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45551502 604 KNTPILIFDEATSSLDSITEHNI---LQALTRATsGRTSICIAHRLS-TVKDADEILVLENGRV 663
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLREELreeLKELQREL-GITTIYVTHDQEeALALADRIAVMNEGRI 209
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
451-672 |
9.47e-30 |
|
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: 117.67 E-value: 9.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPGKpIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRF-----FEPNSGKVLIGGQDISA--VDLESL 523
Cdd:cd03260 1 IELRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDldVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 524 RKVIAVVPQDSVLFHNTIEHNIHYG---NLSKSHAE----VQNAARMADLHDsimswpgqystQVGER--GLKLSGGEKQ 594
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGlrlHGIKLKEElderVEEALRKAALWD-----------EVKDRlhALGLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45551502 595 RVAIARAILKNTPILIFDEATSSLDSITEHNILQALTRATSGRTSICIAHRLSTVKD-ADEILVLENGRVGERGTHSEL 672
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
451-675 |
1.71e-29 |
|
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: 123.09 E-value: 1.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPG-KPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPN---SGKVLIGGQDISAVDLESLRKV 526
Cdd:COG1123 5 LEVRDLSVRYPGGdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 527 IAVVPQD--SVLFHNTIEHNIHYG--NLSKSHAE----VQNAARMADLHDSIMSWPGQystqvgerglkLSGGEKQRVAI 598
Cdd:COG1123 85 IGMVFQDpmTQLNPVTVGDQIAEAleNLGLSRAEararVLELLEAVGLERRLDRYPHQ-----------LSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 599 ARAILKNTPILIFDEATSSLDSITEHNILQALT--RATSGRTSICIAHRLSTVKD-ADEILVLENGRVGERGTHSELLRQ 675
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
451-662 |
2.07e-29 |
|
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: 115.64 E-value: 2.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPG----KPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQdisavdleslrkv 526
Cdd:cd03250 1 ISVEDASFTWDSGeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 527 IAVVPQDSVLFHNTIEHNIHYGNlSKSHAEVQNAARMADLHDSIMSWPGQYSTQVGERGLKLSGGEKQRVAIARAILKNT 606
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGK-PFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45551502 607 PILIFDEATSSLDS-----ITEHNILQALTRatsGRTSICIAHRLSTVKDADEILVLENGR 662
Cdd:cd03250 147 DIYLLDDPLSAVDAhvgrhIFENCILGLLLN---NKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
434-675 |
5.13e-29 |
|
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: 121.55 E-value: 5.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 434 QTAANAQPLfvdttnssIEFRNVSFEYE----PGKPIFRDLSFTIPAGKNVAIVGGSgsgkssMVRLLFRFFEPNSGKVL 509
Cdd:COG1123 252 PAAAAAEPL--------LEVRNLSKRYPvrgkGGVRAVDDVSLTLRRGETLGLVGESgsgkstLARLLLGLLRPTSGSIL 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 510 IGGQDISAV---DLESLRKVIAVVPQD--SVLF-HNTIEHNI-----HYGNLSKSHAE--VQNAARMADLHDSIMSW-PG 575
Cdd:COG1123 324 FDGKDLTKLsrrSLRELRRRVQMVFQDpySSLNpRMTVGDIIaeplrLHGLLSRAERRerVAELLERVGLPPDLADRyPH 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 576 QystqvgerglkLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALT--RATSGRTSICIAHRLSTVKD-A 652
Cdd:COG1123 404 E-----------LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYiA 472
|
250 260
....*....|....*....|...
gi 45551502 653 DEILVLENGRVGERGTHSELLRQ 675
Cdd:COG1123 473 DRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
451-663 |
2.00e-28 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 113.61 E-value: 2.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAV---DLESLRKVI 527
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 528 AVVPQD-SVLFHNTIEHNIHY-----GnlsKSHAEVQNAARMA----DLHDSIMSWPGQystqvgerglkLSGGEKQRVA 597
Cdd:COG2884 82 GVVFQDfRLLPDRTVYENVALplrvtG---KSRKEIRRRVREVldlvGLSDKAKALPHE-----------LSGGEQQRVA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45551502 598 IARAILKNTPILIFDEATSSLDSITEHNILQALTRATSGRTSICIA-HRLSTVKDADE-ILVLENGRV 663
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRL 215
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
467-616 |
7.12e-28 |
|
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: 109.66 E-value: 7.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 467 FRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIAVVPQDSVLF-HNTIEHNI 545
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45551502 546 HYGNLSKSHAEVQNAARMADLHDSiMSWPGQYSTQVGERGLKLSGGEKQRVAIARAILKNTPILIFDEATS 616
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEK-LGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
316-698 |
7.91e-28 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 120.47 E-value: 7.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 316 LINYETVKYFNNEK-YEA---GCYNEVLKKYEAASLKTSSSLALLNfgqnaifssalSLIMVLAAKEIAQGNMTVGDLVM 391
Cdd:PLN03232 486 LASMDTVKCYAWEKsFESriqGIRNEELSWFRKAQLLSAFNSFILN-----------SIPVVVTLVSFGVFVLLGGDLTP 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 392 VNAL----LFQ-LSIPLGFLGSVYREVRQALLDMRAMFTLMNVDSSIqtAANAQPLFVDTTNSSIEFRNVSFEYEPGKPI 466
Cdd:PLN03232 555 ARAFtslsLFAvLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEERI--LAQNPPLQPGAPAISIKNGYFSWDSKTSKPT 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 467 FRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPnsgkvliggQDISAVDLeslRKVIAVVPQDSVLFHNTIEHNIH 546
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH---------AETSSVVI---RGSVAYVPQVSWIFNATVRENIL 700
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 547 YGnlskSHAEVQNAARMADL----HDSIMsWPGQYSTQVGERGLKLSGGEKQRVAIARAILKNTPILIFDEATSSLDSIT 622
Cdd:PLN03232 701 FG----SDFESERYWRAIDVtalqHDLDL-LPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHV 775
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45551502 623 EHNILQALTR-ATSGRTSICIAHRLSTVKDADEILVLENGRVGERGTHSELLRQNGLYARLWEtQTQQFDPSREINE 698
Cdd:PLN03232 776 AHQVFDSCMKdELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLME-NAGKMDATQEVNT 851
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
124-417 |
8.19e-28 |
|
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: 113.80 E-value: 8.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 124 VGISLGLLAGSKLLTVCVPFLFKGAVDtmttlnmDTAPDAVLSAATALMLGYGIARASAAGFNELRNAVFAKVAHHSIRK 203
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLID-------DVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 204 IASNVFLHLHNLDLAFHLNKQTGALSKTIDRGSRGINFVLSAMVFNIVPTIFELALVSSIL---GVKcgLAFAGVSMgCV 280
Cdd:cd07346 74 LRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILfylNWK--LTLVALLL-LP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 281 GIYAAYTLSVTQWRTQFRVFMNQAEnEAGNKAVDSLINYETVKYFNNEKYEAGCYNEVLKKYEAASLKTSSSLALLNFGQ 360
Cdd:cd07346 151 LYVLILRYFRRRIRKASREVRESLA-ELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLI 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 45551502 361 NAIFSSALSLIMVLAAKEIAQGNMTVGDLVMVNALLFQLSIPLGFLGSVYREVRQAL 417
Cdd:cd07346 230 GLLTALGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQAL 286
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
452-663 |
2.25e-27 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 109.06 E-value: 2.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 452 EFRNVSFEYePGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIAVVP 531
Cdd:cd03214 1 EVENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 532 QdsvlfhntiehnihygnlskshaeVQNAARMADLHDSIMSwpgqystqvgerglKLSGGEKQRVAIARAILKNTPILIF 611
Cdd:cd03214 80 Q------------------------ALELLGLAHLADRPFN--------------ELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 45551502 612 DEATSSLD---SITEHNILQALTRATsGRTSICIAHRLS-TVKDADEILVLENGRV 663
Cdd:cd03214 122 DEPTSHLDiahQIELLELLRRLARER-GKTVVMVLHDLNlAARYADRVILLKDGRI 176
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
451-674 |
3.46e-27 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 110.66 E-value: 3.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPG---KPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVI 527
Cdd:COG1124 2 LEVRNLSVSYGQGgrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 528 AVVPQDSVL-FH--NTIEH------NIHygNLSKSHAEVQNAARMADLHDSIMS-WPGQystqvgerglkLSGGEKQRVA 597
Cdd:COG1124 82 QMVFQDPYAsLHprHTVDRilaeplRIH--GLPDREERIAELLEQVGLPPSFLDrYPHQ-----------LSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 598 IARAILKNTPILIFDEATSSLDSITEHNILQALT--RATSGRTSICIAHRLSTV-KDADEILVLENGRVGERGTHSELLR 674
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKdlREERGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVADLLA 228
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
450-672 |
4.39e-27 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 118.34 E-value: 4.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 450 SIEFRNVSFEYEPGKP-IFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIA 528
Cdd:PTZ00243 1308 SLVFEGVQMRYREGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFS 1387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 529 VVPQDSVLFHNTIEHNIHyGNLSKSHAEVQNAARMADLHDSIMSWPGQYSTQVGERGLKLSGGEKQRVAIARAILK-NTP 607
Cdd:PTZ00243 1388 MIPQDPVLFDGTVRQNVD-PFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSG 1466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45551502 608 ILIFDEATSSLDSITEHNILQALTRATSGRTSICIAHRLSTVKDADEILVLENGRVGERGTHSEL 672
Cdd:PTZ00243 1467 FILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
445-672 |
5.00e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 111.00 E-value: 5.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 445 DTTNSSIEFRNVSFEYEPGKPI-FRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESL 523
Cdd:PRK13648 2 EDKNSIIVFKNVSFQYQSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 524 RKVIAVVPQ--DSVLFHNTIEHNIHYG--NLSKSHAEVQNAARMAdLHDSIMSWPGQYSTQvgerglKLSGGEKQRVAIA 599
Cdd:PRK13648 82 RKHIGIVFQnpDNQFVGSIVKYDVAFGleNHAVPYDEMHRRVSEA-LKQVDMLERADYEPN------ALSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45551502 600 RAILKNTPILIFDEATSSLDSITEHNILQALTRATSGR--TSICIAHRLSTVKDADEILVLENGRVGERGTHSEL 672
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
447-675 |
7.51e-27 |
|
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: 110.43 E-value: 7.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 447 TNSSIEFRNVSFEYEPGKpIF--RDLSftiPAGKNvaivggsgsgksSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLR 524
Cdd:cd03294 34 TGQTVGVNDVSLDVREGE-IFviMGLS---GSGKS------------TLLRCINRLIEPTSGKVLIDGQDIAAMSRKELR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 525 KV----IAVVPQDSVLF-HNTIEHNIHYG------NLSKSHAEVQNAARMADLHDSIMSWPGQystqvgerglkLSGGEK 593
Cdd:cd03294 98 ELrrkkISMVFQSFALLpHRTVLENVAFGlevqgvPRAEREERAAEALELVGLEGWEHKYPDE-----------LSGGMQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 594 QRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTR--ATSGRTSICIAHRLS-TVKDADEILVLENGRVGERGTHS 670
Cdd:cd03294 167 QRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPE 246
|
....*
gi 45551502 671 ELLRQ 675
Cdd:cd03294 247 EILTN 251
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
451-663 |
2.01e-26 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 107.82 E-value: 2.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPGK---PIFRDLSFTIPAGKNVAIVggsgs---gkssMVRLLFRffePNSGKVLIGGQDISAVD---LE 521
Cdd:COG1136 5 LELRNLTKSYGTGEgevTALRGVSLSIEAGEFVAIVgpsgsgkstllnILGGLDR---PTSGEVLIDGQDISSLSereLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 522 SLR-KVIAVVPQdsvlFHN-----TIEHNI----HYGNLSKS--HAEVQNAARMADLHDSIMSWPGQystqvgerglkLS 589
Cdd:COG1136 82 RLRrRHIGFVFQ----FFNllpelTALENValplLLAGVSRKerRERARELLERVGLGDRLDHRPSQ-----------LS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45551502 590 GGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTR--ATSGRTSICIAHRLSTVKDADEILVLENGRV 663
Cdd:COG1136 147 GGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDGRI 222
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
446-675 |
2.68e-26 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 108.25 E-value: 2.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 446 TTNSSIEFRNVSFEYEpGKPIFRDLSFTIPAGKNVAIVggsgsgkssMVRLLFRFFEPNSGKVLIGGQDISAVdleslRK 525
Cdd:COG1121 2 MMMPAIELENLTVSYG-GRPVLEDVSLTIPPGEFVAIVgpngagkstLLKAILGLLPPTSGTVRLFGKPPRRA-----RR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 526 VIAVVPQdsvlfHNTIEHNI-----------HYGNLS-------KSHAEVQNA-AR--MADLHDsimswpgqysTQVGEr 584
Cdd:COG1121 76 RIGYVPQ-----RAEVDWDFpitvrdvvlmgRYGRRGlfrrpsrADREAVDEAlERvgLEDLAD----------RPIGE- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 585 glkLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTR-ATSGRTSICIAHRLSTVKD-ADEILVLeNGR 662
Cdd:COG1121 140 ---LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLL-NRG 215
|
250
....*....|...
gi 45551502 663 VGERGTHSELLRQ 675
Cdd:COG1121 216 LVAHGPPEEVLTP 228
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
394-685 |
3.54e-26 |
|
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: 115.43 E-value: 3.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 394 ALLFQLSIPLGFLGSVYREVRQALLDMRAMFTLMNVDSSIQTAANAQPLfVDTTNSSIEFRNVSFEYEPGKP-IFRDLSF 472
Cdd:TIGR00957 581 ALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTI-KPGEGNSITVHNATFTWARDLPpTLNGITF 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 473 TIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQdisavdleslrkvIAVVPQDSVLFHNTIEHNIHYG---N 549
Cdd:TIGR00957 660 SIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQAWIQNDSLRENILFGkalN 726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 550 LSKSHAEVQNAARMADLHdsimSWPGQYSTQVGERGLKLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQA 629
Cdd:TIGR00957 727 EKYYQQVLEACALLPDLE----ILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEH 802
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 45551502 630 LTRAT---SGRTSICIAHRLSTVKDADEILVLENGRVGERGTHSELLRQNGLYARLWET 685
Cdd:TIGR00957 803 VIGPEgvlKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRT 861
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
124-403 |
3.57e-26 |
|
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: 108.50 E-value: 3.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 124 VGISLGLLAGSKLLTVCVPFLFKGAVDTMTTLNmdtapDAVLSAATALMLGYGIARASAAGFNELRNAVFAKVAHHSIRK 203
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDG-----DPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 204 IASNVFLHLHNLDLAFHLNKQTGALSKTIDRGSRGINFVLSAMVFNIVPTIFELA---LVSSILGVKcgLAFAGVSMgcV 280
Cdd:pfam00664 76 LRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVggiIVMFYYGWK--LTLVLLAV--L 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 281 GIYAAYTLSVTQWRTQFRVFMNQAENEAGNKAVDSLINYETVKYFNNEKYEAGCYNEVLKKYEAASLKTSSSLALLNFGQ 360
Cdd:pfam00664 152 PLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGIT 231
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 45551502 361 NAIFSSALSLIMVLAAKEIAQGNMTVGDLVMVNALLFQLSIPL 403
Cdd:pfam00664 232 QFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
451-675 |
8.06e-26 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 106.30 E-value: 8.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYePGKPIFRDLSFTIP------------AGKNVAIvggsgsgkssmvRLLFRFFEPNSGKVLIGGQDISAv 518
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEpgeifgllgpngAGKTTTI------------RMLLGLLRPTSGEVRVLGEDVAR- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 519 DLESLRKVIAVVPQDSVLFHN-TIEHNIH-----YGnLSKSHAE--VQNAARMADLHDSImswpgqySTQVGerglKLSG 590
Cdd:COG1131 67 DPAEVRRRIGYVPQEPALYPDlTVRENLRffarlYG-LPRKEARerIDELLELFGLTDAA-------DRKVG----TLSG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 591 GEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTRATSGRTSICIA-HRLSTVKD-ADEILVLENGRVGERGT 668
Cdd:COG1131 135 GMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAERlCDRVAIIDKGRIVADGT 214
|
....*..
gi 45551502 669 HSELLRQ 675
Cdd:COG1131 215 PDELKAR 221
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
451-672 |
2.40e-25 |
|
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: 105.34 E-value: 2.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAV---DLESLRKVI 527
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgkALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 528 AVVPQDsvlfHNTIEH-----NIHYGNLSkSHAEVQNAARMADLHDSIMSWpgQYSTQVG------ERGLKLSGGEKQRV 596
Cdd:cd03256 81 GMIFQQ----FNLIERlsvleNVLSGRLG-RRSTWRSLFGLFPKEEKQRAL--AALERVGlldkayQRADQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45551502 597 AIARAILKNTPILIFDEATSSLDSITEHNILQALTRATS--GRTSICIAHRLSTVKD-ADEILVLENGRVGERGTHSEL 672
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
451-663 |
7.88e-25 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 101.71 E-value: 7.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYePGKPIFRDLSFTIPAGKNVAIVggsgsgkssMVRLLFRFFEPNSGKVLIGGQDISAvDLESLRKVIAVV 530
Cdd:cd03230 1 IEVRNLSKRY-GKKTALDDISLTVEKGEIYGLLgpngagkttLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 531 PQDSVLfhntiehnihYGNLSkshaevqnaarmadlhdsimswPGQYstqvgergLKLSGGEKQRVAIARAILKNTPILI 610
Cdd:cd03230 79 PEEPSL----------YENLT----------------------VREN--------LKLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 45551502 611 FDEATSSLDSITEHNILQALTRATS-GRTSICIAHRLSTVKD-ADEILVLENGRV 663
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKeGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
449-663 |
9.03e-25 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 102.24 E-value: 9.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 449 SSIEFRNVSFEYEPG-----KPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLL--FRFFEPNSGKVLIGGQDIsavDLE 521
Cdd:cd03213 2 VTLSFRNLTVTVKSSpsksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPL---DKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 522 SLRKVIAVVPQDSVLF-HNTIEHNIHYgnlskshaevqnAARMadlhdsimswpgqystqvgeRGLklSGGEKQRVAIAR 600
Cdd:cd03213 79 SFRKIIGYVPQDDILHpTLTVRETLMF------------AAKL--------------------RGL--SGGERKRVSIAL 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45551502 601 AILKNTPILIFDEATSSLDSITEHNILQALTR-ATSGRTSICIAHRLST--VKDADEILVLENGRV 663
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRV 190
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
451-675 |
1.11e-24 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 105.93 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPGKPIF---RDLSFTIPAGKNVAIVggsgsgkssMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKV- 526
Cdd:COG1135 2 IELENLSKTFPTKGGPVtalDDVSLTIEKGEIFGIIgysgagkstLIRCINLLERPTSGSVLVDGVDLTALSERELRAAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 527 --IAVVPQDSVLFHN-TIEHNIHY----GNLSKSHAEvqnaARMAD------LHDSIMSWPGQystqvgerglkLSGGEK 593
Cdd:COG1135 82 rkIGMIFQHFNLLSSrTVAENVALpleiAGVPKAEIR----KRVAEllelvgLSDKADAYPSQ-----------LSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 594 QRVAIARAiLKNTP-ILIFDEATSSLDSITEHNILQALTRATS--GRTSICIAHRLSTVKD-ADEILVLENGRVGERGTH 669
Cdd:COG1135 147 QRVGIARA-LANNPkVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGPV 225
|
....*.
gi 45551502 670 SELLRQ 675
Cdd:COG1135 226 LDVFAN 231
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
500-673 |
1.36e-24 |
|
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: 102.80 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 500 FFEPNSGKVLIGGQDISavDLESLRKVIAVVPQDSVLF-HNTIEHNIHYG------NLSKSHAEVQNAARMADLHDSIMS 572
Cdd:cd03299 48 FIKPDSGKILLNGKDIT--NLPPEKRDISYVPQNYALFpHMTVYKNIAYGlkkrkvDKKEIERKVLEIAEMLGIDHLLNR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 573 WPGqystqvgerglKLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTRA--TSGRTSICIAHRLSTVK 650
Cdd:cd03299 126 KPE-----------TLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIrkEFGVTVLHVTHDFEEAW 194
|
170 180
....*....|....*....|....
gi 45551502 651 D-ADEILVLENGRVGERGTHSELL 673
Cdd:cd03299 195 AlADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
451-663 |
1.82e-24 |
|
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: 101.84 E-value: 1.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEpGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISA--VDLESLRKVIA 528
Cdd:cd03262 1 IEIKNLHKSFG-DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 529 VVPQDSVLF-HNTIEHNIHYG-----NLSKSHAEvQNAARMAD---LHDSIMSWPGQystqvgerglkLSGGEKQRVAIA 599
Cdd:cd03262 80 MVFQQFNLFpHLTVLENITLApikvkGMSKAEAE-ERALELLEkvgLADKADAYPAQ-----------LSGGQQQRVAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45551502 600 RAILKNTPILIFDEATSSLDSITEHNILQALTR-ATSGRTSICIAHRLSTVKD-ADEILVLENGRV 663
Cdd:cd03262 148 RALAMNPKVMLFDEPTSALDPELVGEVLDVMKDlAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
449-663 |
2.37e-24 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 102.44 E-value: 2.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 449 SSIEFRNVSFEYEPGKPIFRDLSFTIPAGKNVAIVggsgsgkssMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKV-- 526
Cdd:COG3638 1 PMLELRNLSKRYPGGTPALDDVSLEIERGEFVALIgpsgagkstLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 527 -IAVVPQDsvlfHNTIE-----HNIHYGNLSK-----------SHAEVQNAARMADlhdsimswpgqystQVG------E 583
Cdd:COG3638 81 rIGMIFQQ----FNLVPrlsvlTNVLAGRLGRtstwrsllglfPPEDRERALEALE--------------RVGladkayQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 584 RGLKLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTRATS--GRTSICIAHRLSTVKD-ADEILVLEN 660
Cdd:COG3638 143 RADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDLARRyADRIIGLRD 222
|
...
gi 45551502 661 GRV 663
Cdd:COG3638 223 GRV 225
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
451-665 |
2.58e-24 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 102.86 E-value: 2.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPGK---PIFRDLSFTIPAGKNVAIVggsgsgkssmvrlLFR----FFEPNSGKVLIGGQDISAVDLEsl 523
Cdd:COG1116 8 LELRGVSKRFPTGGggvTALDDVSLTVAAGEFVALVgpsgc----gkstLLRliagLEKPTSGEVLVDGKPVTGPGPD-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 524 rkvIAVVPQDSVLF-HNTIEHNIHYG----NLSKS--HAEVQNAARMADLHDSIMSWPGQystqvgerglkLSGGEKQRV 596
Cdd:COG1116 82 ---RGVVFQEPALLpWLTVLDNVALGlelrGVPKAerRERARELLELVGLAGFEDAYPHQ-----------LSGGMRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 597 AIARAILKNTPILIFDEATSSLDSITE---HNILQALTRATsGRTSICIAH------RLstvkdADEILVLEN--GRVGE 665
Cdd:COG1116 148 AIARALANDPEVLLMDEPFGALDALTRerlQDELLRLWQET-GKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIVE 221
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
451-663 |
2.66e-24 |
|
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: 101.33 E-value: 2.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVD---LESLRKVI 527
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 528 AVVPQDS-VLFHNTIEHNIHYGN--LSKSHAEVQN----AARMADLHDSIMSWPGQystqvgerglkLSGGEKQRVAIAR 600
Cdd:cd03292 81 GVVFQDFrLLPDRNVYENVAFALevTGVPPREIRKrvpaALELVGLSHKHRALPAE-----------LSGGEQQRVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45551502 601 AILKNTPILIFDEATSSLDSITEHNILQALTRATSGRTSICIA-HRLSTVKDADE-ILVLENGRV 663
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVAtHAKELVDTTRHrVIALERGKL 214
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
451-675 |
4.42e-24 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 101.61 E-value: 4.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNV--SFEyepGKPIFRDLSFTIPAGKNVAIVggsgsgkssMVRLLFRFFEPNSGKVLIGGQDISA--VDLESLRKV 526
Cdd:COG1126 2 IEIENLhkSFG---DLEVLKGISLDVEKGEVVVIIgpsgsgkstLLRCINLLEEPDSGTITVDGEDLTDskKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 527 IAVVPQDSVLF-HNTIEHNIHYG-----NLSKSHAEvQNAARMAD---LHDSIMSWPGQystqvgerglkLSGGEKQRVA 597
Cdd:COG1126 79 VGMVFQQFNLFpHLTVLENVTLApikvkKMSKAEAE-ERAMELLErvgLADKADAYPAQ-----------LSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 598 IARAILKNTPILIFDEATSSLDSITEHNILQALTR-ATSGRTSICIAHRLSTVKD-ADEILVLENGRVGERGTHSELLRQ 675
Cdd:COG1126 147 IARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDlAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
451-666 |
1.04e-23 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 99.85 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPG---KPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVdleslRKVI 527
Cdd:cd03293 1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-----GPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 528 AVVPQDSVLF-HNTIEHNIHYG----NLSKSHA--EVQNAARMADLHDSIMSWPGQystqvgerglkLSGGEKQRVAIAR 600
Cdd:cd03293 76 GYVFQQDALLpWLTVLDNVALGlelqGVPKAEAreRAEELLELVGLSGFENAYPHQ-----------LSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45551502 601 AILKNTPILIFDEATSSLDSITEHNILQALTR--ATSGRTSICIAHRLS-TVKDADEILVLEN--GRVGER 666
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVAE 215
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
452-663 |
1.15e-23 |
|
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: 99.53 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 452 EFRNVSFEYePGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVdleslRKVIAVVP 531
Cdd:cd03235 1 EVEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 532 QDSVLFHN---TIE---------HNIHYGNLSKSHAEVQNAA----RMADLHDSimswpgqystQVGErglkLSGGEKQR 595
Cdd:cd03235 75 QRRSIDRDfpiSVRdvvlmglygHKGLFRRLSKADKAKVDEAlervGLSELADR----------QIGE----LSGGQQQR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 596 VAIARAILKNTPILIFDEATSSLDSITEHNILQALTR-ATSGRTSICIAHRLSTVKD-ADEILVLeNGRV 663
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLL-NRTV 209
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
447-678 |
2.19e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 100.58 E-value: 2.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 447 TNSSIEFRNVSFEYEPG--KPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLR 524
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 525 KVIAVVPQ--DSVLFHNTIEHNIHYG--NLSKSHAE----VQNAARMADLHDSIMSWPGqystqvgerglKLSGGEKQRV 596
Cdd:PRK13650 81 HKIGMVFQnpDNQFVGATVEDDVAFGleNKGIPHEEmkerVNEALELVGMQDFKEREPA-----------RLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 597 AIARAILKNTPILIFDEATSSLDSITEHNILQAL--TRATSGRTSICIAHRLSTVKDADEILVLENGRVGERGTHSELL- 673
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIkgIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFs 229
|
....*
gi 45551502 674 RQNGL 678
Cdd:PRK13650 230 RGNDL 234
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
450-675 |
3.33e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 100.12 E-value: 3.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 450 SIEFRNVSFEYEPGKPIFR----DLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDIS--AVDLESL 523
Cdd:PRK13637 2 SIKIENLTHIYMEGTPFEKkaldNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 524 RKVIAVVPQ--DSVLFHNTIEHNIHYG--NLSKSHAEVQNAARMAdlhdsiMSWPG-QYSTQVGERGLKLSGGEKQRVAI 598
Cdd:PRK13637 82 RKKVGLVFQypEYQLFEETIEKDIAFGpiNLGLSEEEIENRVKRA------MNIVGlDYEDYKDKSPFELSGGQKRRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 599 ARAILKNTPILIFDEATSSLDSITEHNILQALT--RATSGRTSICIAHRLSTV-KDADEILVLENGRVGERGTHSELLRQ 675
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGRDEILNKIKelHKEYNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
469-667 |
3.57e-23 |
|
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: 98.33 E-value: 3.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 469 DLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAvdLESLRKVIAVVPQDSVLF-HNTIEHNIHY 547
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTA--APPADRPVSMLFQENNLFaHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 548 GNLSKSHAEVQNAARMadlhDSIMSwpgqystQVGERGL------KLSGGEKQRVAIARAILKNTPILIFDEATSSLDSI 621
Cdd:cd03298 94 GLSPGLKLTAEDRQAI----EVALA-------RVGLAGLekrlpgELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 45551502 622 TEHNILQALT--RATSGRTSICIAHRLSTVKD-ADEILVLENGRVGERG 667
Cdd:cd03298 163 LRAEMLDLVLdlHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
451-663 |
4.96e-23 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 97.95 E-value: 4.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPGK---PIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDI---SAVDLESLR 524
Cdd:cd03255 1 IELKNLSKTYGGGGekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsklSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 525 -KVIAVVPQdsvlFHN-----TIEHNI----HYGNLSKSHAEVQ--NAARMADLHDSIMSWPGQystqvgerglkLSGGE 592
Cdd:cd03255 81 rRHIGFVFQ----SFNllpdlTALENVelplLLAGVPKKERRERaeELLERVGLGDRLNHYPSE-----------LSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45551502 593 KQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTR--ATSGRTSICIAHRLSTVKDADEILVLENGRV 663
Cdd:cd03255 146 QQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
450-709 |
2.35e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 103.28 E-value: 2.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 450 SIEFRNVSFEYEPG--KPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIggqdisavdlesLRKVI 527
Cdd:PLN03130 614 AISIKNGYFSWDSKaeRPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTV 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 528 AVVPQDSVLFHNTIEHNIHYGNLSKShAEVQNAARMADLHDSIMSWPGQYSTQVGERGLKLSGGEKQRVAIARAILKNTP 607
Cdd:PLN03130 682 AYVPQVSWIFNATVRDNILFGSPFDP-ERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSD 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 608 ILIFDEATSSLDSITEHNIL-QALTRATSGRTSICIAHRLSTVKDADEILVLENGRVGERGTHSELLRQNGLYARLWETQ 686
Cdd:PLN03130 761 VYIFDDPLSALDAHVGRQVFdKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMENA 840
|
250 260
....*....|....*....|...
gi 45551502 687 TQQFDPSREINEEVAAKKTRGVA 709
Cdd:PLN03130 841 GKMEEYVEENGEEEDDQTSSKPV 863
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
455-664 |
3.54e-22 |
|
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: 95.02 E-value: 3.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 455 NVSFEYEPGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLeslRKVIAVVPQDS 534
Cdd:cd03226 4 NISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER---RKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 535 --VLFHNTIEHNIHYGN--LSKSHAEVQNAARMADLHDSIMSWPgqystqvgergLKLSGGEKQRVAIARAILKNTPILI 610
Cdd:cd03226 81 dyQLFTDSVREELLLGLkeLDAGNEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 45551502 611 FDEATSSLDSITEHNILQA-LTRATSGRTSICIAHRLSTVKD-ADEILVLENGRVG 664
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELiRELAAQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
451-671 |
3.57e-22 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 98.33 E-value: 3.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPGKPIF---RDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVD---LESLR 524
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhalNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekeLRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 525 KVIAVVPQD-SVLFHNTIEHNIHY----GNLSKshAEVQnaAR---------MADLHDSimsWPGQystqvgerglkLSG 590
Cdd:PRK11153 82 RQIGMIFQHfNLLSSRTVFDNVALplelAGTPK--AEIK--ARvtellelvgLSDKADR---YPAQ-----------LSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 591 GEKQRVAIARAiLKNTP-ILIFDEATSSLDSITEHNILQALTR--ATSGRTSICIAHRLSTVKD-ADEILVLENGRVGER 666
Cdd:PRK11153 144 GQKQRVAIARA-LASNPkVLLCDEATSALDPATTRSILELLKDinRELGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQ 222
|
....*
gi 45551502 667 GTHSE 671
Cdd:PRK11153 223 GTVSE 227
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
447-676 |
4.85e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 96.62 E-value: 4.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 447 TNSSIEFRNVSFEY-EPGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRK 525
Cdd:PRK13635 2 KEEIIRVEHISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 526 VIAVVPQ--DSVLFHNTIEHNIHYG--NLSKSHAE----VQNAARMADLHDSIMSWPGqystqvgerglKLSGGEKQRVA 597
Cdd:PRK13635 82 QVGMVFQnpDNQFVGATVQDDVAFGleNIGVPREEmverVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 598 IARAILKNTPILIFDEATSSLDSITEHNILQALTR--ATSGRTSICIAHRLSTVKDADEILVLENGRVGERGTHSELLRQ 675
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
.
gi 45551502 676 N 676
Cdd:PRK13635 231 G 231
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
450-663 |
5.99e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 96.44 E-value: 5.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 450 SIEFRNVSFEYEPGKPI----FRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISA----VDLE 521
Cdd:PRK13641 2 SIKFENVDYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPetgnKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 522 SLRKVIAVVPQ--DSVLFHNTIEHNIHYG--NLSKSHAEVQNAA----RMADLHDSIMSwpgqystqvgERGLKLSGGEK 593
Cdd:PRK13641 82 KLRKKVSLVFQfpEAQLFENTVLKDVEFGpkNFGFSEDEAKEKAlkwlKKVGLSEDLIS----------KSPFELSGGQM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45551502 594 QRVAIARAILKNTPILIFDEATSSLDSITEHNILQA-LTRATSGRTSICIAHRLSTVKD-ADEILVLENGRV 663
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLfKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKL 223
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
464-675 |
1.56e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 94.70 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 464 KPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIAVVPQ-----DSVLFH 538
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQhhltpEGITVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 539 NTIE-----HNIHYGNLS-KSHAEVQNAarMADLHdsimswpgqySTQVGERGL-KLSGGEKQRVAIARAILKNTPILIF 611
Cdd:PRK11231 95 ELVAygrspWLSLWGRLSaEDNARVNQA--MEQTR----------INHLADRRLtDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45551502 612 DEATSSLDsiTEHNI-LQALTR--ATSGRTSICIAHRLSTV-KDADEILVLENGRVGERGTHSE-----LLRQ 675
Cdd:PRK11231 163 DEPTTYLD--INHQVeLMRLMRelNTQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEvmtpgLLRT 233
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
451-676 |
4.80e-21 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 92.51 E-value: 4.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYepGKPIFRdLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDlESLRKViAVV 530
Cdd:COG3840 2 LRLDDLTYRY--GDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP-PAERPV-SML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 531 PQDSVLF-HNTIEHNIHYG-----NLSKS-HAEVQNAARMADLHDSIMSWPGQystqvgerglkLSGGEKQRVAIARAIL 603
Cdd:COG3840 77 FQENNLFpHLTVAQNIGLGlrpglKLTAEqRAQVEQALERVGLAGLLDRLPGQ-----------LSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45551502 604 KNTPILIFDEATSSLDSITEHNILQ---ALTRATsGRTSICIAHRLSTVKD-ADEILVLENGRVGERGTHSELLRQN 676
Cdd:COG3840 146 RKRPILLLDEPFSALDPALRQEMLDlvdELCRER-GLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGE 221
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
451-681 |
5.32e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 93.71 E-value: 5.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIAVV 530
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 531 PQ--DSVLFHNTIEHNIHYG--NLSKSHA----EVQNAARMADLHDsimswpgqYSTQVGERglkLSGGEKQRVAIARAI 602
Cdd:PRK13652 84 FQnpDDQIFSPTVEQDIAFGpiNLGLDEEtvahRVSSALHMLGLEE--------LRDRVPHH---LSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 603 LKNTPILIFDEATSSLDSITEHNILQALTR--ATSGRTSICIAHRLSTVKD-ADEILVLENGRVGERGTHSELLRQNGLY 679
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDlpETYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQPDLL 232
|
..
gi 45551502 680 AR 681
Cdd:PRK13652 233 AR 234
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
448-672 |
7.67e-21 |
|
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: 93.38 E-value: 7.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 448 NSSIEFRNVSFEyepGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQdisavdleslrkvI 527
Cdd:cd03291 37 DNNLFFSNLCLV---GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------I 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 528 AVVPQDSVLFHNTIEHNIHYGnLSKSHAEVQNAARMADLHDSIMSWPGQYSTQVGERGLKLSGGEKQRVAIARAILKNTP 607
Cdd:cd03291 101 SFSSQFSWIMPGTIKENIIFG-VSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDAD 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45551502 608 ILIFDEATSSLDSITEHNILQA-LTRATSGRTSICIAHRLSTVKDADEILVLENGRVGERGTHSEL 672
Cdd:cd03291 180 LYLLDSPFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
450-675 |
8.62e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 92.53 E-value: 8.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 450 SIEFRNVSFEYEpGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIAV 529
Cdd:PRK13548 2 MLEARNLSVRLG-GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 530 VPQDSVL-FHNTIEHNIHYGN--LSKSHAEVQNAARMAdlhdsiMswpgqysTQVGERGLK------LSGGEKQRVAIAR 600
Cdd:PRK13548 81 LPQHSSLsFPFTVEEVVAMGRapHGLSRAEDDALVAAA------L-------AQVDLAHLAgrdypqLSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 601 AIL------KNTPILIFDEATSSLDSITEHNILQALTRAT--SGRTSICIAHRLS-TVKDADEILVLENGRVGERGTHSE 671
Cdd:PRK13548 148 VLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAheRGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAE 227
|
....
gi 45551502 672 LLRQ 675
Cdd:PRK13548 228 VLTP 231
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
450-670 |
1.83e-20 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 91.23 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 450 SIEFRNVSFEYEpGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGG------QDISAVDLESL 523
Cdd:COG4161 2 SIQLKNINCFYG-SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 524 RKVIAVV-------PQDSVLfHNTIEHNIHYGNLSKSHA-----EVQNAARMADLHDSimsWPgqystqvgergLKLSGG 591
Cdd:COG4161 81 RQKVGMVfqqynlwPHLTVM-ENLIEAPCKVLGLSKEQArekamKLLARLRLTDKADR---FP-----------LHLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 592 EKQRVAIARAILKNTPILIFDEATSSLD-SITEH--NILQALtrATSGRTSICIAHRLSTV-KDADEILVLENGRVGERG 667
Cdd:COG4161 146 QQQRVAIARALMMEPQVLLFDEPTAALDpEITAQvvEIIREL--SQTGITQVIVTHEVEFArKVASQVVYMEKGRIIEQG 223
|
...
gi 45551502 668 THS 670
Cdd:COG4161 224 DAS 226
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
451-679 |
1.91e-20 |
|
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: 91.84 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEY-EPGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEpNSGKVLIGGQDISAVDLESLRKVIAV 529
Cdd:cd03289 3 MTVKDLTAKYtEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 530 VPQDSVLFHNTIEHNIH-YGNLSKShaEVQNAARMADLHDSIMSWPGQYSTQVGERGLKLSGGEKQRVAIARAILKNTPI 608
Cdd:cd03289 82 IPQKVFIFSGTFRKNLDpYGKWSDE--EIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45551502 609 LIFDEATSSLDSITEHNILQALTRATSGRTSICIAHRLSTVKDADEILVLENGRVGERGTHSELLRQNGLY 679
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
451-678 |
5.55e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 90.85 E-value: 5.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPGKPIFR----DLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISA----VDLES 522
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFERralyDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkknKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 523 LRKVIAVVPQ--DSVLFHNTIEHNIHYG--NLSKSHAEV-QNAARMADLhdsiMSWPGQYSTQvgeRGLKLSGGEKQRVA 597
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGpmNFGVSEEDAkQKAREMIEL----VGLPEELLAR---SPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 598 IARAILKNTPILIFDEATSSLDSITEHNILQALTR--ATSGRTSICIAHRLSTVKD-ADEILVLENGRVGERGT------ 668
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKlhKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTpreifa 235
|
250
....*....|
gi 45551502 669 HSELLRQNGL 678
Cdd:PRK13634 236 DPDELEAIGL 245
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
447-675 |
5.55e-20 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 92.08 E-value: 5.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 447 TNSSIEFRNVSFEYEpGKPIFRDLSFTIPAGKNVAIvggsgsgkssmvrL---------LFR----FFEPNSGKVLIGGQ 513
Cdd:COG3842 2 AMPALELENVSKRYG-DVTALDDVSLSIEPGEFVAL-------------LgpsgcgkttLLRmiagFETPDSGRILLDGR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 514 DISAVDLEslRKVIAVVPQDSVLF-HNTIEHNIHYG----NLSKS--HAEVQNAARMADLhdsimswPGQYSTQVGErgl 586
Cdd:COG3842 68 DVTGLPPE--KRNVGMVFQDYALFpHLTVAENVAFGlrmrGVPKAeiRARVAELLELVGL-------EGLADRYPHQ--- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 587 kLSGGEKQRVAIARAILKNTPILIFDEATSSLD-SITEH------NILQALtratsGRTSICIAHrlstvkD-------A 652
Cdd:COG3842 136 -LSGGQQQRVALARALAPEPRVLLLDEPLSALDaKLREEmreelrRLQREL-----GITFIYVTH------DqeealalA 203
|
250 260
....*....|....*....|...
gi 45551502 653 DEILVLENGRVGERGTHSELLRQ 675
Cdd:COG3842 204 DRIAVMNDGRIEQVGTPEEIYER 226
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
451-667 |
5.59e-20 |
|
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: 88.79 E-value: 5.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYePGKPIFRDLSFTIP-----------AGKNvaivggsgsgksSMVRLLFRFFEPNSGKVLIGGQDISAvD 519
Cdd:cd03264 1 LQLENLTKRY-GKKRALDGVSLTLGpgmygllgpngAGKT------------TLMRILATLTPPSSGTIRIDGQDVLK-Q 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 520 LESLRKVIAVVPQDSVLFHN--TIEHNIHYGNL-----SKSHAEVQNAARMADLHDSimswpgqYSTQVGerglKLSGGE 592
Cdd:cd03264 67 PQKLRRRIGYLPQEFGVYPNftVREFLDYIAWLkgipsKEVKARVDEVLELVNLGDR-------AKKKIG----SLSGGM 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45551502 593 KQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTRATSGRTSICIAHRLSTVKD-ADEILVLENGRVGERG 667
Cdd:cd03264 136 RRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
458-682 |
7.44e-20 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 95.23 E-value: 7.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 458 FEYEPgKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIggqdisavdleslRKVIAVVPQDSVLF 537
Cdd:PTZ00243 668 FELEP-KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA-------------ERSIAYVPQQAWIM 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 538 HNTIEHNIHYGNlSKSHAEVQNAARMADLHDSIMSWPGQYSTQVGERGLKLSGGEKQRVAIARAILKNTPILIFDEATSS 617
Cdd:PTZ00243 734 NATVRGNILFFD-EEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45551502 618 LDSITEHNILQALTR-ATSGRTSICIAHRLSTVKDADEILVLENGRVGERGTHSELLRQNgLYARL 682
Cdd:PTZ00243 813 LDAHVGERVVEECFLgALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS-LYATL 877
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
451-673 |
8.99e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 90.05 E-value: 8.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVD-LESLRKVIAV 529
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 530 VPQ--DSVLFHNTIEHNIHYG--NLSKSHAEVQNAARMADLHDSImswpGQYSTQVGErglKLSGGEKQRVAIARAILKN 605
Cdd:PRK13644 82 VFQnpETQFVGRTVEEDLAFGpeNLCLPPIEIRKRVDRALAEIGL----EKYRHRSPK---TLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45551502 606 TPILIFDEATSSLDSITEHNILQALTRA-TSGRTSICIAHRLSTVKDADEILVLENGRVGERGTHSELL 673
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
451-673 |
1.36e-19 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 88.61 E-value: 1.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPgKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDI--SAVDLESLRKVIA 528
Cdd:PRK09493 2 IEFKNVSKHFGP-TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 529 VVPQDSVLF-HNTIEHNIHYG-----NLSKSHAEVQNAARMAD--LHDSIMSWPGQystqvgerglkLSGGEKQRVAIAR 600
Cdd:PRK09493 81 MVFQQFYLFpHLTALENVMFGplrvrGASKEEAEKQARELLAKvgLAERAHHYPSE-----------LSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45551502 601 AILKNTPILIFDEATSSLDSITEHNILQAL-TRATSGRTSICIAHRLSTVKD-ADEILVLENGRVGERGTHSELL 673
Cdd:PRK09493 150 ALAVKPKLMLFDEPTSALDPELRHEVLKVMqDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
448-672 |
1.81e-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: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 448 NSSIEFRNVSFEyepGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQdisavdleslrkvI 527
Cdd:TIGR01271 426 DDGLFFSNFSLY---VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------I 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 528 AVVPQDSVLFHNTIEHNIHYGnLSKSHAEVQNAARMADLHDSIMSWPGQYSTQVGERGLKLSGGEKQRVAIARAILKNTP 607
Cdd:TIGR01271 490 SFSPQTSWIMPGTIKDNIIFG-LSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDAD 568
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45551502 608 ILIFDEATSSLDSITEHNILQA-LTRATSGRTSICIAHRLSTVKDADEILVLENGRVGERGTHSEL 672
Cdd:TIGR01271 569 LYLLDSPFTHLDVVTEKEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
450-670 |
2.11e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 88.15 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 450 SIEFRNVSFEYEPGKPIFrDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGG------QDISAVDLESL 523
Cdd:PRK11124 2 SIQLNGINCFYGAHQALF-DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 524 RKVIAVV-------PQDSVLfHNTIEHNIHYGNLSKSHA-----EVQNAARMADLHDSimsWPgqystqvgergLKLSGG 591
Cdd:PRK11124 81 RRNVGMVfqqynlwPHLTVQ-QNLIEAPCRVLGLSKDQAlaraeKLLERLRLKPYADR---FP-----------LHLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 592 EKQRVAIARAILKNTPILIFDEATSSLD-SITEH--NILQALtrATSGRTSICIAHRLSTV-KDADEILVLENGRVGERG 667
Cdd:PRK11124 146 QQQRVAIARALMMEPQVLLFDEPTAALDpEITAQivSIIREL--AETGITQVIVTHEVEVArKTASRVVYMENGHIVEQG 223
|
...
gi 45551502 668 THS 670
Cdd:PRK11124 224 DAS 226
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
451-675 |
3.68e-19 |
|
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: 86.91 E-value: 3.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEpGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDIsaVDLESLRKVIAVV 530
Cdd:cd03300 1 IELENVSKFYG-GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 531 PQDSVLF-HNTIEHNIHYG----NLSKS--HAEVQNAARMADLHDSIMSWPGQystqvgerglkLSGGEKQRVAIARAIL 603
Cdd:cd03300 78 FQNYALFpHLTVFENIAFGlrlkKLPKAeiKERVAEALDLVQLEGYANRKPSQ-----------LSGGQQQRVAIARALV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45551502 604 KNTPILIFDEATSSLDSITEHNILQALTR--ATSGRTSICIAHRLS---TVkdADEILVLENGRVGERGTHSELLRQ 675
Cdd:cd03300 147 NEPKVLLLDEPLGALDLKLRKDMQLELKRlqKELGITFVFVTHDQEealTM--SDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
469-674 |
3.76e-19 |
|
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: 89.79 E-value: 3.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 469 DLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGG---QDISA-VDLESLRKVIAVVPQDSVLF-HNTIEH 543
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKgIFLPPEKRRIGYVFQEARLFpHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 544 NIHYGnLSKSHAEVQNAArmadlHDSIMSWPGqYSTQVGERGLKLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITE 623
Cdd:TIGR02142 95 NLRYG-MKRARPSERRIS-----FERVIELLG-IGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 45551502 624 HNILQALTR--ATSGRTSICIAHRLSTVKD-ADEILVLENGRVGERGTHSELLR 674
Cdd:TIGR02142 168 YEILPYLERlhAEFGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
450-672 |
3.88e-19 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 87.01 E-value: 3.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 450 SIEFRNVSFEYePGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLEslRKVIAV 529
Cdd:cd03296 2 SIEVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 530 VPQDSVLF-HNTIEHNIHYGNLSKSHAEVQNAARMADLHDSI-----MSWPGQ-YSTQvgerglkLSGGEKQRVAIARAI 602
Cdd:cd03296 79 VFQHYALFrHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELlklvqLDWLADrYPAQ-------LSGGQRQRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45551502 603 LKNTPILIFDEATSSLDSITEHNILQALTRA--TSGRTSICIAHRLSTVKD-ADEILVLENGRVGERGTHSEL 672
Cdd:cd03296 152 AVEPKVLLLDEPFGALDAKVRKELRRWLRRLhdELHVTTVFVTHDQEEALEvADRVVVMNKGRIEQVGTPDEV 224
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
454-679 |
4.39e-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: 92.67 E-value: 4.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 454 RNVSFEY-EPGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEpNSGKVLIGGQDISAVDLESLRKVIAVVPQ 532
Cdd:TIGR01271 1221 QGLTAKYtEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQ 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 533 DSVLFHNTIEHNIH-YGNLSKShaEVQNAARMADLHDSIMSWPGQYSTQVGERGLKLSGGEKQRVAIARAILKNTPILIF 611
Cdd:TIGR01271 1300 KVFIFSGTFRKNLDpYEQWSDE--EIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLL 1377
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45551502 612 DEATSSLDSITEHNILQALTRATSGRTSICIAHRLSTVKDADEILVLENGRVGERGTHSELLRQNGLY 679
Cdd:TIGR01271 1378 DEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLF 1445
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
443-673 |
5.52e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 89.90 E-value: 5.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 443 FVDTTNSSIEFRNVsfeyepgkPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLES 522
Cdd:PRK09536 3 MIDVSDLSVEFGDT--------TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 523 LRKVIAVVPQD-SVLFHNTIEHNI------HYGNLSkSHAEVQNAARmadlhDSIMSWPGqySTQVGERGL-KLSGGEKQ 594
Cdd:PRK09536 75 ASRRVASVPQDtSLSFEFDVRQVVemgrtpHRSRFD-TWTETDRAAV-----ERAMERTG--VAQFADRPVtSLSGGERQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 595 RVAIARAILKNTPILIFDEATSSLDsiTEHNI--LQALTR-ATSGRTSICIAHRLS-TVKDADEILVLENGRVGERGTHS 670
Cdd:PRK09536 147 RVLLARALAQATPVLLLDEPTASLD--INHQVrtLELVRRlVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPA 224
|
...
gi 45551502 671 ELL 673
Cdd:PRK09536 225 DVL 227
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
468-673 |
1.24e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 88.55 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 468 RDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKV----IAVVPQDSVLF-HNTIE 542
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMpHMTVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 543 HNIHYG------NLSKSHAEVQNAARMADLHDSIMSWPGQystqvgerglkLSGGEKQRVAIARAILKNTPILIFDEATS 616
Cdd:PRK10070 125 DNTAFGmelagiNAEERREKALDALRQVGLENYAHSYPDE-----------LSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 617 SLDSITEHNILQALTR--ATSGRTSICIAHRL-STVKDADEILVLENGRVGERGTHSELL 673
Cdd:PRK10070 194 ALDPLIRTEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
449-701 |
2.28e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 87.05 E-value: 2.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 449 SSIEFRNVSFEYEpGKPIFRDLSFTIPAGKNVAIVggsgsgkssMVRLLFRFFEPNSGKVLIGGQDISavDLESLRKVIA 528
Cdd:COG3839 2 ASLELENVSKSYG-GVEALKDIDLDIEDGEFLVLLgpsgcgkstLLRMIAGLEDPTSGEILIGGRDVT--DLPPKDRNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 529 VVPQDSVLF-HNTIEHNIHYG----NLSKS--HAEVQNAARMADLHDSIMSWPGQystqvgerglkLSGGEKQRVAIARA 601
Cdd:COG3839 79 MVFQSYALYpHMTVYENIAFPlklrKVPKAeiDRRVREAAELLGLEDLLDRKPKQ-----------LSGGQRQRVALGRA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 602 ILKNTPILIFDEATSSLDS------ITEhniLQALTRATsGRTSICIAHrlstvkD-------ADEILVLENGRVgergt 668
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDAklrvemRAE---IKRLHRRL-GTTTIYVTH------DqveamtlADRIAVMNDGRI----- 212
|
250 260 270
....*....|....*....|....*....|....*...
gi 45551502 669 hsellrqnglyarlwetqtQQFDPSREI-----NEEVA 701
Cdd:COG3839 213 -------------------QQVGTPEELydrpaNLFVA 231
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
451-668 |
3.99e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 86.92 E-value: 3.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEpGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESlRKVIAVV 530
Cdd:PRK09452 15 VELRGISKSFD-GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN-RHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 531 pQDSVLF-HNTIEHNIHYG-NLSK-SHAE----VQNAARMADLHDSIMSWPGQystqvgerglkLSGGEKQRVAIARAIL 603
Cdd:PRK09452 93 -QSYALFpHMTVFENVAFGlRMQKtPAAEitprVMEALRMVQLEEFAQRKPHQ-----------LSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45551502 604 KNTPILIFDEATSSLD---SITEHNILQALTRaTSGRTSICIAH----RLSTvkdADEILVLENGRVGERGT 668
Cdd:PRK09452 161 NKPKVLLLDESLSALDyklRKQMQNELKALQR-KLGITFVFVTHdqeeALTM---SDRIVVMRDGRIEQDGT 228
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
371-666 |
4.82e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 88.33 E-value: 4.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 371 IMVLAAKEIAqGNMTVGDLVMVNALLFQLSIPLGFLGSVYrevrQALLDMRA----MFTLMNVDSSIQTAANAQPLFVDT 446
Cdd:COG4178 284 ILVAAPRYFA-GEITLGGLMQAASAFGQVQGALSWFVDNY----QSLAEWRAtvdrLAGFEEALEAADALPEAASRIETS 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 447 TNSSIEFRNVSFEYEPGKPIFRDLSFTIPAGKNVAIVGgsgsgkssmvrllfrffEPNSGKVLI----------GGQDIS 516
Cdd:COG4178 359 EDGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITG-----------------PSGSGKSTLlraiaglwpyGSGRIA 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 517 AVDLESlrkvIAVVPQDSVLFHNTIEHNIHYGNLSKSH--AEVQNAARMADLH------DSIMSWpgqysTQVgerglkL 588
Cdd:COG4178 422 RPAGAR----VLFLPQRPYLPLGTLREALLYPATAEAFsdAELREALEAVGLGhlaerlDEEADW-----DQV------L 486
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45551502 589 SGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTRATSGRTSICIAHRLSTVKDADEILVLENGRVGER 666
Cdd:COG4178 487 SLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGDGSWQL 564
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
448-678 |
6.10e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 84.85 E-value: 6.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 448 NSSIEFRNVSFEY-EPGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNS---GKVLIGGQDISAVDLESL 523
Cdd:PRK13640 3 DNIVEFKHVSFTYpDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 524 RKVIAVVPQ--DSVLFHNTIEHNIHYG--NLSKSHAE----VQNAARMADLHDSIMSWPgQYstqvgerglkLSGGEKQR 595
Cdd:PRK13640 83 REKVGIVFQnpDNQFVGATVGDDVAFGleNRAVPRPEmikiVRDVLADVGMLDYIDSEP-AN----------LSGGQKQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 596 VAIArAILKNTP-ILIFDEATSSLDSITEHNILQALT--RATSGRTSICIAHRLSTVKDADEILVLENGRVGERGT---- 668
Cdd:PRK13640 152 VAIA-GILAVEPkIIILDESTSMLDPAGKEQILKLIRklKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSpvei 230
|
250
....*....|..
gi 45551502 669 --HSELLRQNGL 678
Cdd:PRK13640 231 fsKVEMLKEIGL 242
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
451-675 |
9.56e-18 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 83.63 E-value: 9.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYePGKPIFRDLSFTIPAGKNVAIVggsgsgkssMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIAVV 530
Cdd:COG4559 2 LEAENLSVRL-GGRTLLDDVSLTLRPGELTAIIgpngagkstLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 531 PQDSVL-FHNTIEHNIHYG--NLSKSHAEVQNAARMAdlhdsiMSwpgqystQVGERGLK------LSGGEKQRVAIARA 601
Cdd:COG4559 81 PQHSSLaFPFTVEEVVALGraPHGSSAAQDRQIVREA------LA-------LVGLAHLAgrsyqtLSGGEQQRVQLARV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 602 IL------KNTP-ILIFDEATSSLDSITEHNILQALTR-ATSGRTSICIAHRLS-TVKDADEILVLENGRVGERGTHSEL 672
Cdd:COG4559 148 LAqlwepvDGGPrWLFLDEPTSALDLAHQHAVLRLARQlARRGGGVVAVLHDLNlAAQYADRILLLHQGRLVAQGTPEEV 227
|
...
gi 45551502 673 LRQ 675
Cdd:COG4559 228 LTD 230
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
451-675 |
1.22e-17 |
|
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: 84.33 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPGKPIFR---DLSFTIPAGKNVAIVGGS----GSGKSSMVRLLfrffEPN---SGKVLIGGQDISAVDL 520
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKavdGVSFDVRRGETLGLVGESgsgkSTLARAILGLL----PPPgitSGEILFDGEDLLKLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 521 ESLRKV----IAVVPQD--SVLfhN---TIEHNI-----HYGNLSKSHAEvQNAARMADL-----HDSIM-SWPGQystq 580
Cdd:COG0444 78 KELRKIrgreIQMIFQDpmTSL--NpvmTVGDQIaeplrIHGGLSKAEAR-ERAIELLERvglpdPERRLdRYPHE---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 581 vgerglkLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALT--RATSGRTSICIAHRLSTVKD-ADEILV 657
Cdd:COG0444 151 -------LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKdlQRELGLAILFITHDLGVVAEiADRVAV 223
|
250
....*....|....*...
gi 45551502 658 LENGRVGERGTHSELLRQ 675
Cdd:COG0444 224 MYAGRIVEEGPVEELFEN 241
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
458-661 |
1.24e-17 |
|
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: 82.38 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 458 FEYEPGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESL----RKVIAVVPQD 533
Cdd:cd03290 8 FSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 534 SVLFHNTIEHNIHYGN-LSKSHAEVQNAArmADLHDSIMSWPGQYSTQVGERGLKLSGGEKQRVAIARAILKNTPILIFD 612
Cdd:cd03290 88 PWLLNATVEENITFGSpFNKQRYKAVTDA--CSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 45551502 613 EATSSLD-SITEH----NILQALTraTSGRTSICIAHRLSTVKDADEILVLENG 661
Cdd:cd03290 166 DPFSALDiHLSDHlmqeGILKFLQ--DDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
451-663 |
1.27e-17 |
|
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: 80.55 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYePGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVD-LESLRKVIAV 529
Cdd:cd03216 1 LELRGITKRF-GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 530 VPQdsvlfhntiehnihygnlskshaevqnaarmadlhdsimswpgqystqvgerglkLSGGEKQRVAIARAILKNTPIL 609
Cdd:cd03216 80 VYQ-------------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 45551502 610 IFDEATSSLDSITEHNILQALTR-ATSGRTSICIAHRLSTVKD-ADEILVLENGRV 663
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRlRAQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
451-663 |
1.63e-17 |
|
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: 81.92 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYePGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISavDLESLRKVIAVV 530
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT--DLPPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 531 PQDSVLF-HNTIEHNIHYG----NLSKSH--AEVQNAARMADLHDSIMSWPGQystqvgerglkLSGGEKQRVAIARAIL 603
Cdd:cd03301 78 FQNYALYpHMTVYDNIAFGlklrKVPKDEidERVREVAELLQIEHLLDRKPKQ-----------LSGGQRQRVALGRAIV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45551502 604 KNTPILIFDEATSSLDSITEHNILQALTR--ATSGRTSICIAH-RLSTVKDADEILVLENGRV 663
Cdd:cd03301 147 REPKVFLMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
455-694 |
2.54e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 83.13 E-value: 2.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 455 NVSFEYEPGKPI-FRDL---SFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISA-----VDLESLRK 525
Cdd:PRK13645 11 NVSYTYAKKTPFeFKALnntSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkiKEVKRLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 526 VIAVVPQ--DSVLFHNTIEHNIHYG--NLSKSHAEVQNaaRMADLHDsIMSWPGQYstqVGERGLKLSGGEKQRVAIARA 601
Cdd:PRK13645 91 EIGLVFQfpEYQLFQETIEKDIAFGpvNLGENKQEAYK--KVPELLK-LVQLPEDY---VKRSPFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 602 ILKNTPILIFDEATSSLDSITEHNILQALTRATS--GRTSICIAHRLSTV-KDADEILVLENGRVGERGTHSELLRQNGL 678
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSPFEIFSNQEL 244
|
250
....*....|....*.
gi 45551502 679 YARLwetqtqQFDPSR 694
Cdd:PRK13645 245 LTKI------EIDPPK 254
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
445-621 |
2.64e-17 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 82.39 E-value: 2.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 445 DTTNSSIEFRNVSFEYEpGKPIFRDLSFTIPAGKNVAIvggsgsgkssM----------VRLLFRFFE--PN---SGKVL 509
Cdd:COG1117 6 STLEPKIEVRNLNVYYG-DKQALKDINLDIPENKVTAL----------IgpsgcgkstlLRCLNRMNDliPGarvEGEIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 510 IGGQDISA--VDLESLRKVIAVVPQDSVLFHNTIEHNIHYG-----NLSKSHAE--VQNAARMA--------DLHDSims 572
Cdd:COG1117 75 LDGEDIYDpdVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgIKSKSELDeiVEESLRKAalwdevkdRLKKS--- 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 45551502 573 wpgqystqvgerGLKLSGGEKQRVAIARAILKNTPILIFDEATSSLDSI 621
Cdd:COG1117 152 ------------ALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPI 188
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
451-673 |
5.56e-17 |
|
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: 80.56 E-value: 5.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYepGK-PIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLES-LRKVIA 528
Cdd:cd03224 1 LEVENLNAGY--GKsQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 529 VVPQDSVLFHN-TIEHNIHYGNLSKSHAEVQnaARMAD-------LHDsimswpgQYSTQVGErglkLSGGEKQRVAIAR 600
Cdd:cd03224 79 YVPEGRRIFPElTVEENLLLGAYARRRAKRK--ARLERvyelfprLKE-------RRKQLAGT----LSGGEQQMLAIAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45551502 601 AILKNTPILIFDEATSSLDSITEHNILQALTR-ATSGRTSICIAHRLSTVKD-ADEILVLENGRVGERGTHSELL 673
Cdd:cd03224 146 ALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRElRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELL 220
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
519-680 |
9.37e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 81.82 E-value: 9.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 519 DLESLRKVIAVVPQ--DSVLFHNTIEHNIHYG--NLSKSHAEvqnAARMADLHDSIMswpGQYSTQVGERGLKLSGGEKQ 594
Cdd:PRK13631 110 NFKELRRRVSMVFQfpEYQLFKDTIEKDIMFGpvALGVKKSE---AKKLAKFYLNKM---GLDDSYLERSPFGLSGGQKR 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 595 RVAIArAILKNTP-ILIFDEATSSLDSITEHNILQ-ALTRATSGRTSICIAHRLSTVKD-ADEILVLENGRVGERGTHSE 671
Cdd:PRK13631 184 RVAIA-GILAIQPeILIFDEPTAGLDPKGEHEMMQlILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYE 262
|
....*....
gi 45551502 672 LLRQNGLYA 680
Cdd:PRK13631 263 IFTDQHIIN 271
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
462-674 |
1.24e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 80.50 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 462 PGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLE---SLRKVIAVVPQDSVLFH 538
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAqrkAFRRDIQMVFQDSISAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 539 N---TIEHNI-----HYGNLSKSH--AEVQNAARMADLHDSIMS-WPGQystqvgerglkLSGGEKQRVAIARAILKNTP 607
Cdd:PRK10419 103 NprkTVREIIreplrHLLSLDKAErlARASEMLRAVDLDDSVLDkRPPQ-----------LSGGQLQRVCLARALAVEPK 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 608 ILIFDEATSSLDSITEHNILQALT--RATSGRTSICIAHRLSTV-KDADEILVLENGRVGERGTHSELLR 674
Cdd:PRK10419 172 LLILDEAVSNLDLVLQAGVIRLLKklQQQFGTACLFITHDLRLVeRFCQRVMVMDNGQIVETQPVGDKLT 241
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
454-668 |
1.24e-16 |
|
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: 84.68 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 454 RNVSFEYEP-GKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAvDLESLRKVIAVVPQ 532
Cdd:TIGR01257 932 KNLVKIFEPsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQ 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 533 DSVLFHN--TIEHNIHYGNL---SKSHAEVQNAARMAD--LHDsimswpgqystQVGERGLKLSGGEKQRVAIARAILKN 605
Cdd:TIGR01257 1011 HNILFHHltVAEHILFYAQLkgrSWEEAQLEMEAMLEDtgLHH-----------KRNEEAQDLSGGMQRKLSVAIAFVGD 1079
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45551502 606 TPILIFDEATSSLDSITEHNILQALTRATSGRTSICIAHRLSTVKD-ADEILVLENGRVGERGT 668
Cdd:TIGR01257 1080 AKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGT 1143
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
451-667 |
1.42e-16 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 79.33 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPGKPIF---RDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKvI 527
Cdd:cd03266 2 ITADALTKRFRDVKKTVqavDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR-L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 528 AVVPQDSVLFHN-TIEHNIHY-GNLS--KSHA------EVQNAARMADLHDsimswpgqystqvgERGLKLSGGEKQRVA 597
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYfAGLYglKGDEltarleELADRLGMEELLD--------------RRVGGFSTGMRQKVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45551502 598 IARAILKNTPILIFDEATSSLDSITEHNILQALTRATS-GRTSICIAHRLSTVKD-ADEILVLENGRVGERG 667
Cdd:cd03266 147 IARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
454-663 |
1.57e-16 |
|
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: 79.24 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 454 RNVSFEYEPGKP--------IFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPN---SGKVLIGGQDISAvdlES 522
Cdd:cd03234 2 RVLPWWDVGLKAknwnkyarILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKP---DQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 523 LRKVIAVVPQDSVLF-HNTIEHNIHYGNLSKSHAEVQNAAR--------MADLHDsimswpgqysTQVGERGLK-LSGGE 592
Cdd:cd03234 79 FQKCVAYVRQDDILLpGLTVRETLTYTAILRLPRKSSDAIRkkrvedvlLRDLAL----------TRIGGNLVKgISGGE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45551502 593 KQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTR-ATSGRTSICIAH--RLSTVKDADEILVLENGRV 663
Cdd:cd03234 149 RRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQlARRNRIVILTIHqpRSDLFRLFDRILLLSSGEI 222
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
450-675 |
1.91e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 80.21 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 450 SIEFRNVSFEYEPGKPI----FRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVD----LE 521
Cdd:PRK13646 2 TIRFDNVSYTYQKGTPYehqaIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 522 SLRKVIAVVPQ--DSVLFHNTIEHNIHYG--NLSKSHAEVQNAArmadlHDSIMSWpgQYSTQVGERG-LKLSGGEKQRV 596
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDTVEREIIFGpkNFKMNLDEVKNYA-----HRLLMDL--GFSRDVMSQSpFQMSGGQMRKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 597 AIARAILKNTPILIFDEATSSLDSITEHNILQALTR--ATSGRTSICIAHRLSTV-KDADEILVLENGRVGERGTHSELL 673
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELF 234
|
..
gi 45551502 674 RQ 675
Cdd:PRK13646 235 KD 236
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
448-673 |
2.18e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 80.14 E-value: 2.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 448 NSSIEFRNVSFEYEPGKPI--FRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRK 525
Cdd:PRK13642 2 NKILEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 526 VIAVVPQ--DSVLFHNTIEHNIHYG--NLSKSHAEVQNAARMADLHDSIMSWPGQYSTqvgerglKLSGGEKQRVAIARA 601
Cdd:PRK13642 82 KIGMVFQnpDNQFVGATVEDDVAFGmeNQGIPREEMIKRVDEALLAVNMLDFKTREPA-------RLSGGQKQRVAVAGI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45551502 602 ILKNTPILIFDEATSSLDSITEHNILQAL--TRATSGRTSICIAHRLSTVKDADEILVLENGRVGERGTHSELL 673
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIheIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
451-673 |
2.44e-16 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 79.36 E-value: 2.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEpGKPIFRDLSFTIPAGKNVAIVggsgsgkssMVRLLFRFFEPNSGKVL-IGGQDISAVDLESLRKVIAV 529
Cdd:COG1119 4 LELRNVTVRRG-GKTILDDISWTVKPGEHWAILgpngagkstLLSLITGDLPPTYGNDVrLFGERRGGEDVWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 530 V---------PQDSVL------FHNTIEHNIHYGNLSKSHA-EVQNAARMADLHDSimswpgQYSTqvgerglkLSGGEK 593
Cdd:COG1119 83 VspalqlrfpRDETVLdvvlsgFFDSIGLYREPTDEQRERArELLELLGLAHLADR------PFGT--------LSQGEQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 594 QRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTR--ATSGRTSICIAHRLSTVKDA-DEILVLENGRVGERGTHS 670
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKE 228
|
...
gi 45551502 671 ELL 673
Cdd:COG1119 229 EVL 231
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
448-676 |
3.60e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 79.39 E-value: 3.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 448 NSSIEFRNVSFEYEPGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVI 527
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 528 AVVPQ--DSVLFHNTIEHNIHYG--NLSKSHAEVQN-------AARMADLHDSimswPGQYstqvgerglkLSGGEKQRV 596
Cdd:PRK13647 82 GLVFQdpDDQVFSSTVWDDVAFGpvNMGLDKDEVERrveealkAVRMWDFRDK----PPYH----------LSYGQKKRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 597 AIARAILKNTPILIFDEATSSLD-----SITEhnILQALTRAtsGRTSICIAHRLSTVKD-ADEILVLENGRVGERGTHS 670
Cdd:PRK13647 148 AIAGVLAMDPDVIVLDEPMAYLDprgqeTLME--ILDRLHNQ--GKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKS 223
|
....*.
gi 45551502 671 ELLRQN 676
Cdd:PRK13647 224 LLTDED 229
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
451-675 |
4.02e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 79.35 E-value: 4.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDI--SAVDLESLRKVIA 528
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkyDKKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 529 VVPQ--DSVLFHNTIEHNIHYG--NLSKSHAEVQNAARMAdlhdsimswpgqySTQVGERGLK------LSGGEKQRVAI 598
Cdd:PRK13639 82 IVFQnpDDQLFAPTVEEDVAFGplNLGLSKEEVEKRVKEA-------------LKAVGMEGFEnkpphhLSGGQKKRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45551502 599 ARAILKNTPILIFDEATSSLDSITEHNILQALTRAT-SGRTSICIAHRLSTV-KDADEILVLENGRVGERGTHSELLRQ 675
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNkEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
451-672 |
5.08e-16 |
|
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: 77.55 E-value: 5.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPG-KPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAvDLESLRKVIAV 529
Cdd:cd03263 1 LQIRNLTKTYKKGtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 530 VPQDSVLFHN-TIEHNIHYGNLSKSHAEVQNAARMADLHDsIMSWPGQYSTQVGErglkLSGGEKQRVAIARAILKNTPI 608
Cdd:cd03263 80 CPQFDALFDElTVREHLRFYARLKGLPKSEIKEEVELLLR-VLGLTDKANKRART----LSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 609 LIFDEATSSLDSITEHNILQALTRATSGRTSICIAH------RLstvkdADEILVLENGRVGERGTHSEL 672
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHsmdeaeAL-----CDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
469-667 |
6.06e-16 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 77.34 E-value: 6.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 469 DLSFTIPAGKnVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQ---DIS-AVDLESLRKVIAVVPQDSVLF-HNTIEH 543
Cdd:cd03297 16 KIDFDLNEEV-TGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRkKINLPPQQRKIGLVFQQYALFpHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 544 NIHYGNLSKSHAEV-QNAARMADLHDSimswpgqysTQVGERG-LKLSGGEKQRVAIARAILKNTPILIFDEATSSLDSI 621
Cdd:cd03297 95 NLAFGLKRKRNREDrISVDELLDLLGL---------DHLLNRYpAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 45551502 622 TEHNILQALTRATS--GRTSICIAHRLSTV-KDADEILVLENGRVGERG 667
Cdd:cd03297 166 LRLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
503-666 |
1.68e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 79.68 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 503 PNSGKVLIGGQDISAVD-LESLRKVIAVVPQDSVLFHN-TIEHNIHYGNLSKS-----HAEVQNAAR--MADLHDSImsw 573
Cdd:COG1129 56 PDSGEILLDGEPVRFRSpRDAQAAGIAIIHQELNLVPNlSVAENIFLGREPRRgglidWRAMRRRARelLARLGLDI--- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 574 pgQYSTQVGErglkLSGGEKQRVAIARAILKNTPILIFDEATSSLDSiTEHNILQALTR--ATSGRTSICIAHRLSTVKD 651
Cdd:COG1129 133 --DPDTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTASLTE-REVERLFRIIRrlKAQGVAIIYISHRLDEVFE 205
|
170
....*....|....*..
gi 45551502 652 -ADEILVLENGR-VGER 666
Cdd:COG1129 206 iADRVTVLRDGRlVGTG 222
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
451-675 |
1.69e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 77.47 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPGKPI----FRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAV----DLES 522
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFasraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTskqkEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 523 LRKVIAVVPQ--DSVLFHNTIEHNIHYG----NLSKSHAEVQNAARMADLHDSIMSWPgqystqvgERGLKLSGGEKQRV 596
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGpqnfGIPKEKAEKIAAEKLEMVGLADEFWE--------KSPFELSGGQMRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 597 AIARAILKNTPILIFDEATSSLDSITEHNILQALTRA-TSGRTSICIAHRLSTVKD-ADEILVLENGRVGERGTHSELLR 674
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQ 233
|
.
gi 45551502 675 Q 675
Cdd:PRK13643 234 E 234
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
505-673 |
2.41e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 79.71 E-value: 2.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 505 SGKVLIGGQdisAVDLESLRKVIAVVPQDSVLF-HNTIEHNIHYGNLSKSHAEVQNAARMADLHDSI--MSWPGQYSTQV 581
Cdd:TIGR00955 82 SGSVLLNGM---PIDAKEMRAISAYVQQDDLFIpTLTVREHLMFQAHLRMPRRVTKKEKRERVDEVLqaLGLRKCANTRI 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 582 GERGLK--LSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTR-ATSGRTSICIAHRLST--VKDADEIL 656
Cdd:TIGR00955 159 GVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGlAQKGKTIICTIHQPSSelFELFDKII 238
|
170
....*....|....*..
gi 45551502 657 VLENGRVGERGTHSELL 673
Cdd:TIGR00955 239 LMAEGRVAYLGSPDQAV 255
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
450-675 |
2.58e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 76.71 E-value: 2.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 450 SIEFRNVSFEYEPGKPIFR----DLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAV----DLE 521
Cdd:PRK13649 2 GINLQNVSYTYQAGTPFEGralfDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 522 SLRKVIAVVPQ--DSVLFHNTIEHNIHYG--NLSKSHAEVQNAAR----MADLHDSIMSwpgqystqvgERGLKLSGGEK 593
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEETVLKDVAFGpqNFGVSQEEAEALAReklaLVGISESLFE----------KNPFELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 594 QRVAIArAILKNTP-ILIFDEATSSLDSITEH---NILQALTRatSGRTSICIAHRLSTVKD-ADEILVLENGRVGERGT 668
Cdd:PRK13649 152 RRVAIA-GILAMEPkILVLDEPTAGLDPKGRKelmTLFKKLHQ--SGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
....*..
gi 45551502 669 HSELLRQ 675
Cdd:PRK13649 229 PKDIFQD 235
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
471-682 |
3.54e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 75.39 E-value: 3.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 471 SFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVdlESLRKVIAVVPQDSVLF-HNTIEHNIHYG- 548
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTT--PPSRRPVSMLFQENNLFsHLTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 549 --NLSKSHAEVQNAARMAD---LHDSIMSWPGQystqvgerglkLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITE 623
Cdd:PRK10771 97 npGLKLNAAQREKLHAIARqmgIEDLLARLPGQ-----------LSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45551502 624 HNILQALTRATSGR--TSICIAHRLStvkDADEI----LVLENGRVGERGTHSELLRQNGLYARL 682
Cdd:PRK10771 166 QEMLTLVSQVCQERqlTLLMVSHSLE---DAARIaprsLVVADGRIAWDGPTDELLSGKASASAL 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
436-675 |
8.77e-15 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 77.80 E-value: 8.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 436 AANAQPLfvdttnssIEFRNVSFEYEPGKPIFR----------DLSFTIPAGKNVAIVggsgs----gkssMVRLLfrff 501
Cdd:COG4172 269 PPDAPPL--------LEARDLKVWFPIKRGLFRrtvghvkavdGVSLTLRRGETLGLVgesgsgkstlglaLLRLI---- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 502 ePNSGKVLIGGQDISAVD---LESLRKVIAVVPQDSvlfhntiehnihYGNLS-------------KSHAEVQNAARMAD 565
Cdd:COG4172 337 -PSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP------------FGSLSprmtvgqiiaeglRVHGPGLSAAERRA 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 566 LHDSIMswpgqysTQVG-----------ErglkLSGGEKQRVAIARA-ILKntP-ILIFDEATSSLDSITEHNILQALTR 632
Cdd:COG4172 404 RVAEAL-------EEVGldpaarhryphE----FSGGQRQRIAIARAlILE--PkLLVLDEPTSALDVSVQAQILDLLRD 470
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 45551502 633 --ATSGRTSICIAHRLSTVKD-ADEILVLENGRVGERGTHSELLRQ 675
Cdd:COG4172 471 lqREHGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
451-673 |
9.96e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 75.27 E-value: 9.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQ--DISAVDLESLRKVIA 528
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 529 VVPQ--DSVLFHNTIEHNIHYG--NLSKSHAEVQNAAR-------MADLHDSIMSWpgqystqvgerglkLSGGEKQRVA 597
Cdd:PRK13636 86 MVFQdpDNQLFSASVYQDVSFGavNLKLPEDEVRKRVDnalkrtgIEHLKDKPTHC--------------LSFGQKKRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45551502 598 IARAILKNTPILIFDEATSSLDSITEHNILQAL--TRATSGRTSICIAHRLSTVK-DADEILVLENGRVGERGTHSELL 673
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLveMQKELGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
455-675 |
1.13e-14 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 77.42 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 455 NVSFEYEPG-KPIFRDLSFTIPAGKNVAIVGGS----GSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKV--- 526
Cdd:COG4172 13 SVAFGQGGGtVEAVKGVSFDIAAGETLALVGESgsgkSVTALSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRIrgn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 527 -IAVVPQD--SVLfhN---TIEHNI------HYGnLSKSHAEvqnaARMADLHDsimswpgqystQVG----ERGLK--- 587
Cdd:COG4172 93 rIAMIFQEpmTSL--NplhTIGKQIaevlrlHRG-LSGAAAR----ARALELLE-----------RVGipdpERRLDayp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 588 --LSGGEKQRVAIARAILkNTP-ILIFDEATSSLDSITEHNILQALT--RATSGRTSICIAHRLSTVKD-ADEILVLENG 661
Cdd:COG4172 155 hqLSGGQRQRVMIAMALA-NEPdLLIADEPTTALDVTVQAQILDLLKdlQRELGMALLLITHDLGVVRRfADRVAVMRQG 233
|
250
....*....|....
gi 45551502 662 RVGERGTHSELLRQ 675
Cdd:COG4172 234 EIVEQGPTAELFAA 247
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
436-672 |
1.99e-14 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 75.15 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 436 AANAQPLfvdttnssIEFRNVSFEYEPGKPIFR----------DLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNS 505
Cdd:COG4608 1 AAMAEPL--------LEVRDLKKHFPVRGGLFGrtvgvvkavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 506 GKVLIGGQDISAVDLESLRKV---IAVVPQD--SVLfhN---TIEH------NIHyGNLSKshAEVQnaARMADLHDsim 571
Cdd:COG4608 73 GEILFDGQDITGLSGRELRPLrrrMQMVFQDpyASL--NprmTVGDiiaeplRIH-GLASK--AERR--ERVAELLE--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 572 swpgqystQVGergLK----------LSGGEKQRVAIARAILKNTPILIFDEATSSLD-SITEH--NILQALtRATSGRT 638
Cdd:COG4608 143 --------LVG---LRpehadrypheFSGGQRQRIGIARALALNPKLIVCDEPVSALDvSIQAQvlNLLEDL-QDELGLT 210
|
250 260 270
....*....|....*....|....*....|....*
gi 45551502 639 SICIAHRLSTVKD-ADEILVLENGRVGERGTHSEL 672
Cdd:COG4608 211 YLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
446-675 |
2.13e-14 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 75.14 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 446 TTNSSIEFRNVSFEYepGK-PIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLEslR 524
Cdd:PRK11432 2 TQKNFVVLKNITKRF--GSnTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--Q 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 525 KVIAVVPQDSVLF-HNTIEHNIHYG----NLSKSH--AEVQNAARMADLhdsiMSWPGQYSTQVgerglklSGGEKQRVA 597
Cdd:PRK11432 78 RDICMVFQSYALFpHMSLGENVGYGlkmlGVPKEErkQRVKEALELVDL----AGFEDRYVDQI-------SGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 598 IARAILKNTPILIFDEATSSLDS---------ITEhniLQaltrATSGRTSICIAHRLS-TVKDADEILVLENGRVGERG 667
Cdd:PRK11432 147 LARALILKPKVLLFDEPLSNLDAnlrrsmrekIRE---LQ----QQFNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIG 219
|
....*...
gi 45551502 668 THSELLRQ 675
Cdd:PRK11432 220 SPQELYRQ 227
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
455-673 |
4.76e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 72.77 E-value: 4.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 455 NVS--FEYEPGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFE------PNSGKVLIGGQDISAVDLESLRKV 526
Cdd:PRK14246 12 NISrlYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 527 IAVVPQDSVLF-HNTIEHNIHYGnlSKSHAeVQNAARMADLHDSIMSWPGQYStQVGER----GLKLSGGEKQRVAIARA 601
Cdd:PRK14246 92 VGMVFQQPNPFpHLSIYDNIAYP--LKSHG-IKEKREIKKIVEECLRKVGLWK-EVYDRlnspASQLSGGQQQRLTIARA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45551502 602 ILKNTPILIFDEATSSLDSITEHNILQALTRATSGRTSICIAHRLSTV-KDADEILVLENGRVGERGTHSELL 673
Cdd:PRK14246 168 LALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIF 240
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
449-690 |
5.99e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 72.09 E-value: 5.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 449 SSIEFRNVSFEYEpGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVD--------L 520
Cdd:PRK11264 2 SAIEVKNLVKKFH-GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARslsqqkglI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 521 ESLRKVIAVVPQDSVLF-HNTIEHNIHYGNL-SKSHAEVQNAARMADLhdsimswpgqySTQVGERG------LKLSGGE 592
Cdd:PRK11264 81 RQLRQHVGFVFQNFNLFpHRTVLENIIEGPViVKGEPKEEATARAREL-----------LAKVGLAGketsypRRLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 593 KQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTR-ATSGRTSICIAHRLSTVKD-ADEILVLENGRVGERGTHS 670
Cdd:PRK11264 150 QQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAK 229
|
250 260
....*....|....*....|
gi 45551502 671 EllrqngLYARLWETQTQQF 690
Cdd:PRK11264 230 A------LFADPQQPRTRQF 243
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
451-644 |
6.80e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 74.10 E-value: 6.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEpGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVdlESLRKVIAVV 530
Cdd:PRK11607 20 LEIRNLTKSFD-GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV--PPYQRPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 531 PQDSVLF-HNTIEHNIHYGNLSKSHAEVQNAARMADLHDSImswpgQYSTQVGERGLKLSGGEKQRVAIARAILKNTPIL 609
Cdd:PRK11607 97 FQSYALFpHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLV-----HMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 45551502 610 IFDEATSSLDSI----TEHNILQALTRAtsGRTSICIAH 644
Cdd:PRK11607 172 LLDEPMGALDKKlrdrMQLEVVDILERV--GVTCVMVTH 208
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
126-407 |
9.91e-14 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 72.46 E-value: 9.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 126 ISLGLLAGSKLLTVCVPFLFKGAVDTMTTlnmDTAPDAVLSAAtALMLGYGIARAsaaGFNELRNAVFAKVAHHSIRKIA 205
Cdd:cd18542 3 LAILALLLATALNLLIPLLIRRIIDSVIG---GGLRELLWLLA-LLILGVALLRG---VFRYLQGYLAEKASQKVAYDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 206 SNVFLHLHNLDLAFHLNKQTGALsktIDRGS---RGINFVLSAMVFNIVPTIFELALVSSILG---VKcgLAFAGVSMGC 279
Cdd:cd18542 76 NDLYDHLQRLSFSFHDKARTGDL---MSRCTsdvDTIRRFLAFGLVELVRAVLLFIGALIIMFsinWK--LTLISLAIIP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 280 VGIYAAYTLSvTQWRTQFRVFMNQ--------AENEAGNKavdslinyeTVKYFNNEKYEAGCYNEVLKKYEAASLKTSS 351
Cdd:cd18542 151 FIALFSYVFF-KKVRPAFEEIREQegelntvlQENLTGVR---------VVKAFAREDYEIEKFDKENEEYRDLNIKLAK 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 45551502 352 SLALLNFGQNAIFSSALSLIMVLAAKEIAQGNMTVGDLVMVNALLFQLSIPLGFLG 407
Cdd:cd18542 221 LLAKYWPLMDFLSGLQIVLVLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLG 276
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
450-675 |
1.14e-13 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 72.87 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 450 SIEFRNVSFEYePGKPIFRDLSFTIPAGKNVAIvggsgsgkssmvrL---------LFR----FFEPNSGKVLIGGQDIs 516
Cdd:COG1118 2 SIEVRNISKRF-GSFTLLDDVSLEIASGELVAL-------------LgpsgsgkttLLRiiagLETPDSGRIVLNGRDL- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 517 AVDLESLRKVIAVVPQDSVLF-HNTIEHNIHYGNLSKSHAEVQNAARMADLHDSI-MSWPGQ-YSTQvgerglkLSGGEK 593
Cdd:COG1118 67 FTNLPPRERRVGFVFQHYALFpHMTVAENIAFGLRVRPPSKAEIRARVEELLELVqLEGLADrYPSQ-------LSGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 594 QRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTR--ATSGRTSICIAH------RLstvkdADEILVLENGRVGE 665
Cdd:COG1118 140 QRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRlhDELGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQ 214
|
250
....*....|
gi 45551502 666 RGTHSELLRQ 675
Cdd:COG1118 215 VGTPDEVYDR 224
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
463-664 |
1.28e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 71.25 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 463 GKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGgqdisAVDLESLRKVIAVVPQDSVLFH-NTI 541
Cdd:PRK11247 24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-----TAPLAEAREDTRLMFQDARLLPwKKV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 542 EHNIHYGNLSKSHAEVQNAARMADLHDSIMSWPGqystqvgerglKLSGGEKQRVAIARAILKNTPILIFDEATSSLDSI 621
Cdd:PRK11247 99 IDNVGLGLKGQWRDAALQALAAVGLADRANEWPA-----------ALSGGQKQRVALARALIHRPGLLLLDEPLGALDAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 45551502 622 TEHNILQALTR--ATSGRTSICIAHRLS-TVKDADEILVLENGRVG 664
Cdd:PRK11247 168 TRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKIG 213
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
411-662 |
1.76e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 72.17 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 411 REVRQALLDMRAMFTLMNVDSSIQTAANAQPLFVDTTnsSIEFRNVSFEYEpGKPIFRDLSFTIPAGKNVAIVGGSGSGK 490
Cdd:PRK13536 4 RAVAEEAPRRLELSPIERKHQGISEAKASIPGSMSTV--AIDLAGVSKSYG-DKAVVNGLSFTVASGECFGLLGPNGAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 491 SSMVRLLFRFFEPNSGKVLIGGQDISAvDLESLRKVIAVVPQ-DSVLFHNTIEHN-IHYGNLSKSHAEvQNAARMADLHD 568
Cdd:PRK13536 81 STIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQfDNLDLEFTVRENlLVFGRYFGMSTR-EIEAVIPSLLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 569 SimswpGQYSTQVGERGLKLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALtRA--TSGRTSICIAHRL 646
Cdd:PRK13536 159 F-----ARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERL-RSllARGKTILLTTHFM 232
|
250
....*....|....*..
gi 45551502 647 STVKD-ADEILVLENGR 662
Cdd:PRK13536 233 EEAERlCDRLCVLEAGR 249
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
451-675 |
1.87e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 71.27 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPG-----KPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDIS-AVDLESLR 524
Cdd:PRK13633 5 IKCKNVSYKYESNeesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSdEENLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 525 KVIAVVPQ--DSVLFHNTIEHNIHYG--NLSKSHAEVQnaARMADLHDSI-MSWPGQYSTQVgerglkLSGGEKQRVAIA 599
Cdd:PRK13633 85 NKAGMVFQnpDNQIVATIVEEDVAFGpeNLGIPPEEIR--ERVDESLKKVgMYEYRRHAPHL------LSGGQKQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45551502 600 RAILKNTPILIFDEATSSLDSITEHNILQALTR--ATSGRTSICIAHRLSTVKDADEILVLENGRVGERGTHSELLRQ 675
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
451-662 |
1.88e-13 |
|
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: 69.82 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEpGKPIFRDLSFTIPAGKNVAIvggsgsgkssmV-----------RLLFRFFEPNSGKVLIGGQDISAVD 519
Cdd:COG4133 3 LEAENLSCRRG-ERLLFSGLSFTLAAGEALAL-----------TgpngsgkttllRILAGLLPPSAGEVLWNGEPIRDAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 520 lESLRKVIAVVPQDSVLFHN-TIEHNIHY----GNLSKSHAEVQNAARMADLHDSIMSWPGQystqvgerglkLSGGEKQ 594
Cdd:COG4133 71 -EDYRRRLAYLGHADGLKPElTVRENLRFwaalYGLRADREAIDEALEAVGLAGLADLPVRQ-----------LSAGQKR 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45551502 595 RVAIARAILKNTPILIFDEATSSLDSITEHNILQALTRATSGRTSICIA-HRLSTVkDADEILVLENGR 662
Cdd:COG4133 139 RVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLEL-AAARVLDLGDFK 206
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
451-658 |
2.36e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 70.13 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEpGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIAVV 530
Cdd:PRK10247 8 LQLQNVGYLAG-DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 531 PQDSVLFHNTIehnihYGNLSKSHAEVQNAARMADLHDSIMSWpGQYSTQVGERGLKLSGGEKQRVAIARAILKNTPILI 610
Cdd:PRK10247 87 AQTPTLFGDTV-----YDNLIFPWQIRNQQPDPAIFLDDLERF-ALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 45551502 611 FDEATSSLDSITEHNILQALTRATS--GRTSICIAHRLSTVKDADEILVL 658
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHRYVReqNIAVLWVTHDKDEINHADKVITL 210
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
438-673 |
4.01e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.43 E-value: 4.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 438 NAQPLfVDTTNSSIEFRNVSFEYEpgkpIFRDLSFTIPAGKNVAIV----GGSGSGKSSMVRLLfrffePN------SGK 507
Cdd:PRK15134 1 MTQPL-LAIENLSVAFRQQQTVRT----VVNDVSLQIEAGETLALVgesgSGKSVTALSILRLL-----PSppvvypSGD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 508 VLIGGQDISAVDLESLRKV----IAVVPQDSVLFHNTIeHNIH---YGNLSKSHAEVQNAARMADLhdSIMSWPG--QYS 578
Cdd:PRK15134 71 IRFHGESLLHASEQTLRGVrgnkIAMIFQEPMVSLNPL-HTLEkqlYEVLSLHRGMRREAARGEIL--NCLDRVGirQAA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 579 TQVGERGLKLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALT--RATSGRTSICIAHRLSTVKD-ADEI 655
Cdd:PRK15134 148 KRLTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVRKlADRV 227
|
250
....*....|....*...
gi 45551502 656 LVLENGRVGERGTHSELL 673
Cdd:PRK15134 228 AVMQNGRCVEQNRAATLF 245
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
451-663 |
4.27e-13 |
|
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: 68.85 E-value: 4.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPgKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDleslRKVIAVV 530
Cdd:cd03269 1 LEVENVTKRFGR-VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 531 PQDSVLFHNT--IEHNIHYGNLSK-SHAEVQNaarmadlhdSIMSW-----PGQYSTQVGErglKLSGGEKQRVAIARAI 602
Cdd:cd03269 76 PEERGLYPKMkvIDQLVYLAQLKGlKKEEARR---------RIDEWlerleLSEYANKRVE---ELSKGNQQKVQFIAAV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45551502 603 LKNTPILIFDEATSSLDSITEHNILQALTR-ATSGRTSICIAHRLSTVKD-ADEILVLENGRV 663
Cdd:cd03269 144 IHDPELLILDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVEElCDRVLLLNKGRA 206
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
471-668 |
5.11e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 70.76 E-value: 5.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 471 SFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDI---SAVDLESLRKVIAVV---------PQDSV--- 535
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkaDPEAQKLLRQKIQIVfqnpygslnPRKKVgqi 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 536 ----LFHNTiehnihygNLSKSHAEVQNAARMAdlhdsimswpgqystQVGergLK----------LSGGEKQRVAIARA 601
Cdd:PRK11308 115 leepLLINT--------SLSAAERREKALAMMA---------------KVG---LRpehydryphmFSGGQRQRIAIARA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45551502 602 ILKNTPILIFDEATSSLD-SITEH--NILQALTRATsGRTSICIAHRLSTVKD-ADEILVLENGRVGERGT 668
Cdd:PRK11308 169 LMLDPDVVVADEPVSALDvSVQAQvlNLMMDLQQEL-GLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGT 238
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
450-694 |
7.42e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 69.30 E-value: 7.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 450 SIEFRNVSFEYEPGKpIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNS-----GKVLIGGQDI--SAVDLES 522
Cdd:PRK14258 7 AIKVNNLSFYYDTQK-ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 523 LRKVIAVVPQDSVLFHNTIEHNIHYG-NLSKSHAE------VQNAARMADLHDSImswpgqySTQVGERGLKLSGGEKQR 595
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNVAYGvKIVGWRPKleiddiVESALKDADLWDEI-------KHKIHKSALDLSGGQQQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 596 VAIARAILKNTPILIFDEATSSLD---SITEHNILQALtRATSGRTSICIAHRLSTVKDADEILVLENGRVGERGTHSEL 672
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDpiaSMKVESLIQSL-RLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENRIGQLVEF 237
|
250 260
....*....|....*....|..
gi 45551502 673 LRQNGLYARLWETQTQQFDPSR 694
Cdd:PRK14258 238 GLTKKIFNSPHDSRTREYVLSR 259
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
447-674 |
1.06e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 68.66 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 447 TNSSIEFRNVSFEYePGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKV 526
Cdd:PRK10575 8 SDTTFALRNVSFRV-PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 527 IAVVPQD-------SVLFHNTIEHNIHYGNLSK----SHAEVQNAARMADLhdsimswpgqysTQVGERGL-KLSGGEKQ 594
Cdd:PRK10575 87 VAYLPQQlpaaegmTVRELVAIGRYPWHGALGRfgaaDREKVEEAISLVGL------------KPLAHRLVdSLSGGERQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 595 RVAIARAILKNTPILIFDEATSSLDSITEHNILQALTRATSGR--TSICIAHRLS-TVKDADEILVLENGRVGERGTHSE 671
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAE 234
|
...
gi 45551502 672 LLR 674
Cdd:PRK10575 235 LMR 237
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
451-686 |
1.69e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 68.33 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPGKPIFR--------DLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLES 522
Cdd:COG4167 5 LEVRNLSKTFKYRTGLFRrqqfeavkPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 523 LRKVIAVVPQDSV----------------LFHNTiehnihygNLSkshaevqNAARMADLHDSImswpgqysTQVG---E 583
Cdd:COG4167 85 RCKHIRMIFQDPNtslnprlnigqileepLRLNT--------DLT-------AEEREERIFATL--------RLVGllpE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 584 RGL----KLSGGEKQRVAIARAILKNTPILIFDEATSSLD-----SITehNILQALtRATSGRTSICIAHRLSTVKD-AD 653
Cdd:COG4167 142 HANfyphMLSSGQKQRVALARALILQPKIIIADEALAALDmsvrsQII--NLMLEL-QEKLGISYIYVSQHLGIVKHiSD 218
|
250 260 270
....*....|....*....|....*....|....*
gi 45551502 654 EILVLENGRVGERGTHSELLR--QNGLYARLWETQ 686
Cdd:COG4167 219 KVLVMHQGEVVEYGKTAEVFAnpQHEVTKRLIESH 253
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
124-417 |
2.01e-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: 350007 [Multi-domain] Cd Length: 296 Bit Score: 68.31 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 124 VGISLGLLAGSKLLTVCVPFLFKGAVDTMTTLNmdtAPDAVLSAATALMLGYGIARASAAGFNELRNAVFAKVAHHSIRK 203
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDVLIQL---GPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 204 IASNVFLHLHNLDLAFHLNKQTGALsktIDRGSRGINFVLSAMVFNIVPTIFELALVSSILGVKC----GLA-FAGVSMG 278
Cdd:cd18563 78 LRRDLYEHLQRLSLSFFDKRQTGSL---MSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFslnwKLAlLVLIPVP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 279 CVGIyaaytLSVTQWRTQFRVFMNQAENEAGNKAV--DSLINYETVKYFNNEKYEAGCYNEVLKKYEAASLKTSSSLALL 356
Cdd:cd18563 155 LVVW-----GSYFFWKKIRRLFHRQWRRWSRLNSVlnDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATF 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45551502 357 NFGQNAIFSSALSLIMVLAAKEIAQGNMTVGDLVMVNALLFQLSIPLGFLGSVYREVRQAL 417
Cdd:cd18563 230 FPLLTFLTSLGTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRAL 290
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
446-676 |
3.28e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 67.48 E-value: 3.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 446 TTNSSIEFRNVSFEyEPGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVD---LES 522
Cdd:PRK11831 3 SVANLVDMRGVSFT-RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrLYT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 523 LRKVIAVVPQDSVLFHN-TIEHNIHYGnlSKSHAEVQNAArmadLHDSIMswpgQYSTQVGERGL------KLSGGEKQR 595
Cdd:PRK11831 82 VRKRMSMLFQSGALFTDmNVFDNVAYP--LREHTQLPAPL----LHSTVM----MKLEAVGLRGAaklmpsELSGGMARR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 596 VAIARAILKNTPILIFDEATSSLDSITEHNILQALTRATS--GRTSICIAHRLSTVKD-ADEILVLENGRVGERGTHSEl 672
Cdd:PRK11831 152 AALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQA- 230
|
....
gi 45551502 673 LRQN 676
Cdd:PRK11831 231 LQAN 234
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
466-690 |
6.04e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 66.53 E-value: 6.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 466 IFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAV-------------DLESLRKVIAVVPQ 532
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 533 DSVLF------HNTIEHNIHYGNLSKSHAEVQNAARMADLhdsimswpGQYSTQVGERGLKLSGGEKQRVAIARAILKNT 606
Cdd:PRK10619 100 HFNLWshmtvlENVMEAPIQVLGLSKQEARERAVKYLAKV--------GIDERAQGKYPVHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 607 PILIFDEATSSLDSITEHNILQALTR-ATSGRTSICIAHRLSTVKD-ADEILVLENGRVGERGTHSELLrQNGLYARLwe 684
Cdd:PRK10619 172 EVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLF-GNPQSPRL-- 248
|
....*.
gi 45551502 685 tqtQQF 690
Cdd:PRK10619 249 ---QQF 251
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
446-665 |
6.58e-12 |
|
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: 65.92 E-value: 6.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 446 TTNSSIEFRNVSFEY-EPGKP--IFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLES 522
Cdd:COG4181 4 SSAPIIELRGLTKTVgTGAGEltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 523 L----RKVIAVVPQDSVLFhntiehnihyGNLS-----------KSHAEVQNAAR-------MADLHDsimSWPGQystq 580
Cdd:COG4181 84 RarlrARHVGFVFQSFQLL----------PTLTalenvmlplelAGRRDARARARallervgLGHRLD---HYPAQ---- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 581 vgerglkLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQAL--TRATSGRTSICIAHRLSTVKDADEILVL 658
Cdd:COG4181 147 -------LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLfeLNRERGTTLVLVTHDPALAARCDRVLRL 219
|
....*..
gi 45551502 659 ENGRVGE 665
Cdd:COG4181 220 RAGRLVE 226
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
492-678 |
1.07e-11 |
|
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: 67.05 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 492 SMVRL---LFRffePNSGKVLIGG---QDISA-VDLESLRKVIAVVPQDSVLF-HNTIEHNIHYGnlsksHAEVQNAARM 563
Cdd:COG4148 40 TLLRAiagLER---PDSGRIRLGGevlQDSARgIFLPPHRRRIGYVFQEARLFpHLSVRGNLLYG-----RKRAPRAERR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 564 ADLhDSIMSW----------PGQystqvgerglkLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTRA 633
Cdd:COG4148 112 ISF-DEVVELlgighlldrrPAT-----------LSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 45551502 634 tSGRTSICI---AH------RLstvkdADEILVLENGRVGERGTHSELLRQNGL 678
Cdd:COG4148 180 -RDELDIPIlyvSHsldevaRL-----ADHVVLLEQGRVVASGPLAEVLSRPDL 227
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
588-660 |
1.25e-11 |
|
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: 63.33 E-value: 1.25e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45551502 588 LSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTRAtsGRTSICIAHRLSTVKDADEILVLEN 660
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL--GITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
451-676 |
1.29e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 66.26 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPGKPI----FRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLI-----------GGQDI 515
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkktKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 516 SAVDLE-------------SLRKVIAVVPQ--DSVLFHNTIEHNIHYGNLSK--SHAEVQNAAR----MADLHDSIMswp 574
Cdd:PRK13651 83 VLEKLViqktrfkkikkikEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMgvSKEEAKKRAAkyieLVGLDESYL--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 575 gqystqvgERG-LKLSGGEKQRVAIArAILKNTP-ILIFDEATSSLDSITEHNILQALTRA-TSGRTSICIAHRLSTV-K 650
Cdd:PRK13651 160 --------QRSpFELSGGQKRRVALA-GILAMEPdFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVlE 230
|
250 260
....*....|....*....|....*.
gi 45551502 651 DADEILVLENGRVGERGTHSELLRQN 676
Cdd:PRK13651 231 WTKRTIFFKDGKIIKDGDTYDILSDN 256
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
469-672 |
1.71e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 66.27 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 469 DLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDI---SAVDLESLRKVIAVVPQDSVLFHN---TIE 542
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmKDDEWRAVRSDIQMIFQDPLASLNprmTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 543 HNI------HYGNLSKSHAEVQNAARMAD---LHDSIMSWPGQYstqvgerglklSGGEKQRVAIARAILKNTPILIFDE 613
Cdd:PRK15079 119 EIIaeplrtYHPKLSRQEVKDRVKAMMLKvglLPNLINRYPHEF-----------SGGQCQRIGIARALILEPKLIICDE 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45551502 614 ATSSLD-SITEH--NILQALTRATsGRTSICIAHRLSTVKD-ADEILVLENGRVGERGTHSEL 672
Cdd:PRK15079 188 PVSALDvSIQAQvvNLLQQLQREM-GLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
506-668 |
2.17e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 64.80 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 506 GKVLIGGQDISA--VDLESLRKVIAVVPQDSVLFHNTIEHNIHYG---NLSKSHAE--VQNAARMADLHDSImswpgqyS 578
Cdd:PRK14243 70 GKVTFHGKNLYApdVDPVEVRRRIGMVFQKPNPFPKSIYDNIAYGariNGYKGDMDelVERSLRQAALWDEV-------K 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 579 TQVGERGLKLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTRATSGRTSICIAHRLSTVKDADEILVL 658
Cdd:PRK14243 143 DKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAF 222
|
170
....*....|
gi 45551502 659 ENGRVGERGT 668
Cdd:PRK14243 223 FNVELTEGGG 232
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
451-663 |
2.33e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 67.06 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPGK---PIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESL---- 523
Cdd:PRK10535 5 LELKDIRRSYPSGEeqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 524 RKVIAVVPQD-SVLFHNTIEHNIH----YGNLSKshAEVQNAARM----ADLHDSIMSWPGQystqvgerglkLSGGEKQ 594
Cdd:PRK10535 85 REHFGFIFQRyHLLSHLTAAQNVEvpavYAGLER--KQRLLRAQEllqrLGLEDRVEYQPSQ-----------LSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45551502 595 RVAIARAILKNTPILIFDEATSSLDSITEH---NILQALTRatSGRTSICIAHRLSTVKDADEILVLENGRV 663
Cdd:PRK10535 152 RVSIARALMNGGQVILADEPTGALDSHSGEevmAILHQLRD--RGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
451-672 |
2.58e-11 |
|
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: 66.75 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEpGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLL--FRFFEPNSGKVL------------------- 509
Cdd:TIGR03269 1 IEVKNLTKKFD-GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIyhvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 510 -----IGG----QDISAVDLE-----SLRKVIAVVPQ-------DSVLFHNTIE--HNIHYgnlsKSHAEVQNAARMADL 566
Cdd:TIGR03269 80 epcpvCGGtlepEEVDFWNLSdklrrRIRKRIAIMLQrtfalygDDTVLDNVLEalEEIGY----EGKEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 567 hdsimswpgqysTQVGER----GLKLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITE---HNILQALTRAtSGRTS 639
Cdd:TIGR03269 156 ------------VQLSHRithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAklvHNALEEAVKA-SGISM 222
|
250 260 270
....*....|....*....|....*....|....
gi 45551502 640 ICIAHRLSTVKD-ADEILVLENGRVGERGTHSEL 672
Cdd:TIGR03269 223 VLTSHWPEVIEDlSDKAIWLENGEIKEEGTPDEV 256
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
503-663 |
2.74e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 65.67 E-value: 2.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 503 PNSGKVLIGGQ---DI-SAVDLESLRKVIAVVPQDSVLF-HNTIEHNIHYGnLSKShaevqnaarMADLHDSIMSWPGQy 577
Cdd:PRK11144 50 PQKGRIVLNGRvlfDAeKGICLPPEKRRIGYVFQDARLFpHYKVRGNLRYG-MAKS---------MVAQFDKIVALLGI- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 578 stqvgERGLK-----LSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTRaTSGRTSICI---AHRLSTV 649
Cdd:PRK11144 119 -----EPLLDrypgsLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLER-LAREINIPIlyvSHSLDEI 192
|
170
....*....|....*
gi 45551502 650 -KDADEILVLENGRV 663
Cdd:PRK11144 193 lRLADRVVVLEQGKV 207
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
468-672 |
3.00e-11 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 63.54 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 468 RDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAvDLESLRKVIAVVPQDSVL------FHNTI 541
Cdd:cd03265 17 RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVddeltgWENLY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 542 EHNIHYG----NLSKSHAEVQNAARMADLHDSIMSwpgqystqvgerglKLSGGEKQRVAIARAILKNTPILIFDEATSS 617
Cdd:cd03265 96 IHARLYGvpgaERRERIDELLDFVGLLEAADRLVK--------------TYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 45551502 618 LDSITEHNI---LQALTRaTSGRTSICIAHRLSTVKD-ADEILVLENGRVGERGTHSEL 672
Cdd:cd03265 162 LDPQTRAHVweyIEKLKE-EFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
449-663 |
4.03e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.13 E-value: 4.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 449 SSIEFRNVSFEYEPGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISavdlESLRK-VI 527
Cdd:PRK15056 5 AGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKnLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 528 AVVPQDS-------VLFHNTIEHNiHYGNL-------SKSHAEVQNAARMADLHDsimswpgQYSTQVGErglkLSGGEK 593
Cdd:PRK15056 81 AYVPQSEevdwsfpVLVEDVVMMG-RYGHMgwlrrakKRDRQIVTAALARVDMVE-------FRHRQIGE----LSGGQK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45551502 594 QRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTR-ATSGRTSICIAHRLSTVKDADEILVLENGRV 663
Cdd:PRK15056 149 KRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRElRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTV 219
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
450-675 |
4.90e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 64.72 E-value: 4.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 450 SIEFRNVSFEYEPGKpIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESlRKViAV 529
Cdd:PRK10851 2 SIEIANIKKSFGRTQ-VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD-RKV-GF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 530 VPQDSVLF-HNTIEHNIHYG----------NLSKSHAEVQNAARMADLHDSIMSWPGQystqvgerglkLSGGEKQRVAI 598
Cdd:PRK10851 79 VFQHYALFrHMTVFDNIAFGltvlprrerpNAAAIKAKVTQLLEMVQLAHLADRYPAQ-----------LSGGQKQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 599 ARAILKNTPILIFDEATSSLDSITEHNILQALTRATS--GRTSICIAH-RLSTVKDADEILVLENGRVGERGTHSELLRQ 675
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEelKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQVWRE 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
451-675 |
5.91e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 65.47 E-value: 5.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEpGKPIFRDLSFTIPAGKNVAIVggsgsgkssMVRLLFRFFEPNSGKVLIGgqdisavdlESLRkvIAVV 530
Cdd:COG0488 316 LELEGLSKSYG-DKTLLDDLSLRIDRGDRIGLIgpngagkstLLKLLAGELEPDSGTVKLG---------ETVK--IGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 531 PQDSVLFH--NTIEHNIHYGNLSKSHAEVQN-AARM----ADLHdsimswpgqysTQVGerglKLSGGEKQRVAIARAIL 603
Cdd:COG0488 384 DQHQEELDpdKTVLDELRDGAPGGTEQEVRGyLGRFlfsgDDAF-----------KPVG----VLSGGEKARLALAKLLL 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45551502 604 KNTPILIFDEATSSLDSITehniLQALTRA---TSGrTSICIAH-R--LSTVkdADEILVLENGRVGER-GTHSELLRQ 675
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIET----LEALEEAlddFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVREYpGGYDDYLEK 520
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
452-663 |
6.13e-11 |
|
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: 61.68 E-value: 6.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 452 EFRNVSfeyepGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVD-LESLRKVIAVV 530
Cdd:cd03215 6 EVRGLS-----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 531 PQD---SVLFHN-TIEHNIHYGNLskshaevqnaarmadlhdsimswpgqystqvgerglkLSGGEKQRVAIARAILKNT 606
Cdd:cd03215 81 PEDrkrEGLVLDlSVAENIALSSL-------------------------------------LSGGNQQKVVLARWLARDP 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45551502 607 PILIFDEATSSLD--SITE-HNILQALTRAtsGRTSICIAHRLSTVKD-ADEILVLENGRV 663
Cdd:cd03215 124 RVLILDEPTRGVDvgAKAEiYRLIRELADA--GKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
128-417 |
9.75e-11 |
|
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: 63.35 E-value: 9.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 128 LGLLAGSKLLTVCVPFLFKGAVDTMTTlnmDTAPDAVLSAATALMLGYGIArasaAGFNELRNAVFAKVAHHSIRKIASN 207
Cdd:cd18557 2 LLFLLISSAAQLLLPYLIGRLIDTIIK---GGDLDVLNELALILLAIYLLQ----SVFTFVRYYLFNIAGERIVARLRRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 208 VFLHLHNLDLAFHLNKQTGALsktIDRGSRGINFVLSAMVFNIVPTIFELALVSSILGVKCGLAF--AGVSMGCVGIYAA 285
Cdd:cd18557 75 LFSSLLRQEIAFFDKHKTGEL---TSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWklTLVLLLVIPLLLI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 286 YTLSVTQWRTQFRVFMNQAENEAGNKAVDSLINYETVKYFNNEKYEAGCYNEVLKKYEAASLKTSSSLALLNFGQNAIFS 365
Cdd:cd18557 152 ASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIY 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 45551502 366 SALSLIMVLAAKEIAQGNMTVGDLVMVNALLFQLSIPLGFLGSVYREVRQAL 417
Cdd:cd18557 232 LSLLLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKAL 283
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
505-666 |
1.09e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.57 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 505 SGKVLIGGQDISAVDL-ESLRKVIAVVPQDSVLFHN-TIEHNIHYGNlskshaEVqnaarmadLHDSIMSWPGQYS---- 578
Cdd:PRK13549 61 EGEIIFEGEELQASNIrDTERAGIAIIHQELALVKElSVLENIFLGN------EI--------TPGGIMDYDAMYLraqk 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 579 ------------TQVGErglkLSGGEKQRVAIARAILKNTPILIFDEATSSL-DSITEH--NILQALTRatSGRTSICIA 643
Cdd:PRK13549 127 llaqlkldinpaTPVGN----LGLGQQQLVEIAKALNKQARLLILDEPTASLtESETAVllDIIRDLKA--HGIACIYIS 200
|
170 180
....*....|....*....|....*
gi 45551502 644 HRLSTVKD-ADEILVLENGR-VGER 666
Cdd:PRK13549 201 HKLNEVKAiSDTICVIRDGRhIGTR 225
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
449-672 |
1.43e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 63.51 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 449 SSIEFRNVSFEYEpGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISavDLESLRKVIA 528
Cdd:PRK11000 2 ASVTLRNVTKAYG-DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN--DVPPAERGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 529 VVPQDSVLF-HNTIEHNIHYG----NLSKSHAE--VQNAARMADLhdsimswpgqysTQVGERGLK-LSGGEKQRVAIAR 600
Cdd:PRK11000 79 MVFQSYALYpHLSVAENMSFGlklaGAKKEEINqrVNQVAEVLQL------------AHLLDRKPKaLSGGQRQRVAIGR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45551502 601 AILKNTPILIFDEATSSLDSITEHNILQALTRATS--GRTSICIAH-RLSTVKDADEILVLENGRVGERGTHSEL 672
Cdd:PRK11000 147 TLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
451-663 |
1.48e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 61.81 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAV---DLESLRKVI 527
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrEVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 528 AVVPQDS-VLFHNTIEHN------IHYGNLSKSHAEVQNAARMADLHDSIMSWPgqystqvgergLKLSGGEKQRVAIAR 600
Cdd:PRK10908 82 GMIFQDHhLLMDRTVYDNvaipliIAGASGDDIRRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45551502 601 AILKNTPILIFDEATSSLDSITEHNILQALTRATS-GRTSICIAHRLSTVKDAD-EILVLENGRV 663
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATHDIGLISRRSyRMLTLSDGHL 215
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
127-417 |
1.52e-10 |
|
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: 62.50 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 127 SLGLLAGSKLLTVCVPFLFKGAVDTMTTLNmDTAPdavLSAATALMLGYGIARAsaaGFNELRNAVFAKVAHHSIRKIAS 206
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAALGGG-DTAS---LNQIALLLLGLFLLQA---VFSFFRIYLFARVGERVVADLRK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 207 NVFLHLHNLDLAFHLNKQTGALSKtidRGSRGINFVLSAMVFNIVptifelALVSSILGVKCGLAFAGV-----SMGCVG 281
Cdd:cd18576 74 DLYRHLQRLPLSFFHERRVGELTS---RLSNDVTQIQDTLTTTLA------EFLRQILTLIGGVVLLFFiswklTLLMLA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 282 IYAAYTLSVTQWRTQFRVFMNQAEN---EAGNKAVDSLINYETVKYFNNEKYEAGCYNEVLKKYEAASLKTSSSLALLNF 358
Cdd:cd18576 145 TVPVVVLVAVLFGRRIRKLSKKVQDelaEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSS 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45551502 359 GQNAIFSSALSLIMVLAAKEIAQGNMTVGDLVMVnaLLFQLSI--PLGFLGSVYREVRQAL 417
Cdd:cd18576 225 FIIFLLFGAIVAVLWYGGRLVLAGELTAGDLVAF--LLYTLFIagSIGSLADLYGQLQKAL 283
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
449-673 |
2.52e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 61.47 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 449 SSIEFRNVSFEYEPGKpIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFE--PN---SGKVLIGGQDISAVDLESL 523
Cdd:PRK14247 2 NKIEIRDLKVSFGQVE-VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 524 RKVIAVVPQDSVLFHN-TIEHNIHYG----NLSKSHAEVQNAARMAdlHDSIMSWPgQYSTQVGERGLKLSGGEKQRVAI 598
Cdd:PRK14247 81 RRRVQMVFQIPNPIPNlSIFENVALGlklnRLVKSKKELQERVRWA--LEKAQLWD-EVKDRLDAPAGKLSGGQQQRLCI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45551502 599 ARAILKNTPILIFDEATSSLDSITEHNILQALTRATSGRTSICIAH-RLSTVKDADEILVLENGRVGERGTHSELL 673
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREVF 233
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
455-674 |
3.85e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 62.95 E-value: 3.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 455 NVSFEYEPGK-PIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKV-------------LIGGQDISAVDL 520
Cdd:PRK10261 19 NIAFMQEQQKiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqVIELSEQSAAQM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 521 ESLRKV-IAVVPQDSVLFHN---TIEHNI------HYGnLSKSHAEVQnAARMADL-----HDSIMS-WPGQystqvger 584
Cdd:PRK10261 99 RHVRGAdMAMIFQEPMTSLNpvfTVGEQIaesirlHQG-ASREEAMVE-AKRMLDQvripeAQTILSrYPHQ-------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 585 glkLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQaLTRATSGRTS---ICIAHRLSTVKD-ADEILVLEN 660
Cdd:PRK10261 169 ---LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQ-LIKVLQKEMSmgvIFITHDMGVVAEiADRVLVMYQ 244
|
250
....*....|....
gi 45551502 661 GRVGERGTHSELLR 674
Cdd:PRK10261 245 GEAVETGSVEQIFH 258
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
449-666 |
4.87e-10 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 60.65 E-value: 4.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 449 SSIEFRNVSFEYEPG---KPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESlrk 525
Cdd:COG4525 2 SMLTVRHVSVRYPGGgqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 526 viAVVPQDSVLF--HNTIEhNIHYG------NLSKSHAEVQNAARMADLHDsimswpgqystqVGERGL-KLSGGEKQRV 596
Cdd:COG4525 79 --GVVFQKDALLpwLNVLD-NVAFGlrlrgvPKAERRARAEELLALVGLAD------------FARRRIwQLSGGMRQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 597 AIARAILKNTPILIFDEATSSLDSITEHNILQALTR--ATSGRTSICIAHrlstvkDADEILVLEN---------GRVGE 665
Cdd:COG4525 144 GIARALAADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH------SVEEALFLATrlvvmspgpGRIVE 217
|
.
gi 45551502 666 R 666
Cdd:COG4525 218 R 218
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
452-662 |
6.64e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 62.24 E-value: 6.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 452 EFRNVSFEYePGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDI---SAVDleSLRKVIA 528
Cdd:PRK11288 6 SFDGIGKTF-PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTA--ALAAGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 529 VVPQDSVLFHN-TIEHNIHYGNL-------SKSHAEVQNAARMADLHDSImswpgQYSTQVGErglkLSGGEKQRVAIAR 600
Cdd:PRK11288 83 IIYQELHLVPEmTVAENLYLGQLphkggivNRRLLNYEAREQLEHLGVDI-----DPDTPLKY----LSIGQRQMVEIAK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45551502 601 AILKNTPILIFDEATSSLdSITEHNILQALTRA--TSGRTSICIAHRLSTVKD-ADEILVLENGR 662
Cdd:PRK11288 154 ALARNARVIAFDEPTSSL-SAREIEQLFRVIRElrAEGRVILYVSHRMEEIFAlCDAITVFKDGR 217
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
451-665 |
7.01e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 61.91 E-value: 7.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIAVV 530
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 531 PQDSVLFHNTIEHnihyGNLSKSHAEVQNAARMADLHDSIMSWPGQYSTqvgergLKLSGGEKQRVAIARAILKNTPILI 610
Cdd:PRK10522 403 FTDFHLFDQLLGP----EGKPANPALVEKWLERLKMAHKLELEDGRISN------LKLSKGQKKRLALLLALAEERDILL 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 45551502 611 FDEATSSLDSI---TEHNILQALTRATsGRTSICIAHRLSTVKDADEILVLENGRVGE 665
Cdd:PRK10522 473 LDEWAADQDPHfrrEFYQVLLPLLQEM-GKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
451-673 |
7.07e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 60.57 E-value: 7.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVS--FEYEPGkpIFR--------DLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDL 520
Cdd:PRK15112 5 LEVRNLSktFRYRTG--WFRrqtveavkPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 521 ESLRKVIAVVPQDSvlfHNTIEHNIHYGNLS----KSHAEVQNAARMADLHDSImswpgqysTQVGERG-------LKLS 589
Cdd:PRK15112 83 SYRSQRIRMIFQDP---STSLNPRQRISQILdfplRLNTDLEPEQREKQIIETL--------RQVGLLPdhasyypHMLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 590 GGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQAL--TRATSGRTSICIAHRLSTVKD-ADEILVLENGRVGER 666
Cdd:PRK15112 152 PGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMleLQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVER 231
|
....*..
gi 45551502 667 GTHSELL 673
Cdd:PRK15112 232 GSTADVL 238
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
503-691 |
7.92e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 59.85 E-value: 7.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 503 PNSGKVLIGGQDISAVDLESLRKVIAVVPQDSVL------FHNTIEHnihygnLSKSHAEVQNAARMADLHDSIMSWPgQ 576
Cdd:COG4138 47 PGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPpfampvFQYLALH------QPAGASSEAVEQLLAQLAEALGLED-K 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 577 YSTQVGerglKLSGGEKQRVAIARAILKNTP-------ILIFDEATSSLDsITEHNILQALTR--ATSGRTSICIAHRLS 647
Cdd:COG4138 120 LSRPLT----QLSGGEWQRVRLAAVLLQVWPtinpegqLLLLDEPMNSLD-VAQQAALDRLLRelCQQGITVVMSSHDLN 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 45551502 648 -TVKDADEILVLENGRVGERGTHSELLRQNGLyARLWETQTQQFD 691
Cdd:COG4138 195 hTLRHADRVWLLKQGKLVASGETAEVMTPENL-SEVFGVKFRRLE 238
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
451-673 |
9.53e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 60.59 E-value: 9.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEPgKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKViAVV 530
Cdd:PRK13537 8 IDFRNVEKRYGD-KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRV-GVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 531 PQdsvlFHN-----TIEHNI----HYGNLSKSHAE--VQNAARMADLHDsimswpgQYSTQVGErglkLSGGEKQRVAIA 599
Cdd:PRK13537 86 PQ----FDNldpdfTVRENLlvfgRYFGLSAAAARalVPPLLEFAKLEN-------KADAKVGE----LSGGMKRRLTLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45551502 600 RAILKNTPILIFDEATSSLDSITEHNILQAL-TRATSGRTSICIAHRLSTVKD-ADEILVLENGRVGERGTHSELL 673
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLrSLLARGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALI 226
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
452-674 |
1.02e-09 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 59.23 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 452 EFRNVSFEYePGKPIFRDLSFTIPAGKNVAIVggsgsgkssMVRLLFRFFEPNSGKVLIGGQDISAVDLESL-RKVIAVV 530
Cdd:COG0410 5 EVENLHAGY-GGIHVLHGVSLEVEEGEIVALLgrngagkttLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 531 PQDSVLFHN-TIEHNIHYG--NLSKSHAEVQNAARMADLHdsimswP--GQYSTQvgeRGLKLSGGEKQRVAIARAILKN 605
Cdd:COG0410 84 PEGRRIFPSlTVEENLLLGayARRDRAEVRADLERVYELF------PrlKERRRQ---RAGTLSGGEQQMLAIGRALMSR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45551502 606 TPILIFDEATSSLD-SITEhNILQALTRATSGRTSICI----AHRLSTVkdADEILVLENGRVGERGTHSELLR 674
Cdd:COG0410 155 PKLLLLDEPSLGLApLIVE-EIFEIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAELLA 225
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
500-678 |
1.04e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 60.02 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 500 FFEPNSGKVLIGGQ--DISAVDLESLRKVIAVVPQD--SVLFHNTIEHNIHYG--NLSKSHAEVqnaARMADlhDSImsw 573
Cdd:PRK13638 50 LLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQDpeQQIFYTDIDSDIAFSlrNLGVPEAEI---TRRVD--EAL--- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 574 pgqysTQVGERGLK------LSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTR-ATSGRTSICIAHRL 646
Cdd:PRK13638 122 -----TLVDAQHFRhqpiqcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDI 196
|
170 180 190
....*....|....*....|....*....|....*....
gi 45551502 647 STVKD-ADEILVLENGRV------GERGTHSELLRQNGL 678
Cdd:PRK13638 197 DLIYEiSDAVYVLRQGQIlthgapGEVFACTEAMEQAGL 235
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
468-658 |
1.05e-09 |
|
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: 59.40 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 468 RDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLrkviaVVPQD-SVLFHNTIEHNIH 546
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNySLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 547 YG------NLSKSHAE--VQNAARMADLHDSIMSWPGQystqvgerglkLSGGEKQRVAIARAILKNTPILIFDEATSSL 618
Cdd:TIGR01184 77 LAvdrvlpDLSKSERRaiVEEHIALVGLTEAADKRPGQ-----------LSGGMKQRVAIARALSIRPKVLLLDEPFGAL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 45551502 619 DSITEHNILQALTRatsgrtsICIAHRLSTV---KDADEILVL 658
Cdd:TIGR01184 146 DALTRGNLQEELMQ-------IWEEHRVTVLmvtHDVDEALLL 181
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
451-662 |
1.14e-09 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 57.07 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEpGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGqdisavdleslRKVIAVV 530
Cdd:cd03221 1 IELENLSKTYG-GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 531 PQdsvlfhntiehnihygnlskshaevqnaarmadlhdsimswpgqystqvgerglkLSGGEKQRVAIARAILKNTPILI 610
Cdd:cd03221 69 EQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 45551502 611 FDEATSSLDSITehniLQALTRA--TSGRTSICIAH-R--LSTVkdADEILVLENGR 662
Cdd:cd03221 94 LDEPTNHLDLES----IEALEEAlkEYPGTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
450-677 |
1.22e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 60.12 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 450 SIEFRNVSFEYEpGKPIFRDLSFTIP------------AGKNVAIvggsgsgkssmvRLLFRFFEPNSGKVLIGGQDISA 517
Cdd:COG4152 1 MLELKGLTKRFG-DKTAVDDVSFTVPkgeifgllgpngAGKTTTI------------RIILGILAPDSGEVLWDGEPLDP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 518 VDleslRKVIAVVPQDSVLFHN-TIEHNIHY-----GnLSKSHAEvQNAARMADLHDsIMSWPGQystQVGErglkLSGG 591
Cdd:COG4152 68 ED----RRRIGYLPEERGLYPKmKVGEQLVYlarlkG-LSKAEAK-RRADEWLERLG-LGDRANK---KVEE----LSKG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 592 EKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALT-RATSGRTSICIAHRLSTVKD-ADEILVLENGRVGERGTH 669
Cdd:COG4152 134 NQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIReLAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSV 213
|
....*...
gi 45551502 670 SELLRQNG 677
Cdd:COG4152 214 DEIRRQFG 221
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
448-673 |
1.34e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 59.12 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 448 NSSIEFRNVSFEYepGK-PIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLES-LRK 525
Cdd:PRK11614 3 KVMLSFDKVSAHY--GKiQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 526 VIAVVPQDSVLFHN-TIEHNIHYGNLSKSHAEVQN-AARMADLhdsimsWPGQYSTQVgERGLKLSGGEKQRVAIARAIL 603
Cdd:PRK11614 81 AVAIVPEGRRVFSRmTVEENLAMGGFFAERDQFQErIKWVYEL------FPRLHERRI-QRAGTMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45551502 604 KNTPILIFDEATSSLDSITEHNILQALTRATSGRTSICIAHRLS--TVKDADEILVLENGRVGERGTHSELL 673
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNAnqALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
454-663 |
1.70e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 58.67 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 454 RNVSFEYEPGK---PIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDI----SAVDLESLRKV 526
Cdd:PRK11629 9 DNLCKRYQEGSvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklsSAAKAELRNQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 527 IAVVPQdsvlFHNTIEHNIHYGNLS-------KSHAEVQNAARmadlhdSIMSWPGqYSTQVGERGLKLSGGEKQRVAIA 599
Cdd:PRK11629 89 LGFIYQ----FHHLLPDFTALENVAmplligkKKPAEINSRAL------EMLAAVG-LEHRANHRPSELSGGERQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45551502 600 RAILKNTPILIFDEATSSLDSITEHNILQALTR--ATSGRTSICIAHRLSTVKDADEILVLENGRV 663
Cdd:PRK11629 158 RALVNNPRLVLADEPTGNLDARNADSIFQLLGElnRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
436-667 |
1.73e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.87 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 436 AANAQPLFvdttnsSIEFRNVSFEYEPG--------KPIFRDLSFTIPAGKNVAIV----GGSGSGKSSMVRLLfrffeP 503
Cdd:PRK15134 269 PEPASPLL------DVEQLQVAFPIRKGilkrtvdhNVVVKNISFTLRPGETLGLVgesgSGKSTTGLALLRLI-----N 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 504 NSGKVLIGGQDISAVD---LESLRKVIAVVPQD---------SVLfhNTIEH--NIHYGNLSKSHAEVQNAARMADL--- 566
Cdd:PRK15134 338 SQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDpnsslnprlNVL--QIIEEglRVHQPTLSAAQREQQVIAVMEEVgld 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 567 HDSIMSWPGQYStqvgerglklsGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALT--RATSGRTSICIAH 644
Cdd:PRK15134 416 PETRHRYPAEFS-----------GGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKslQQKHQLAYLFISH 484
|
250 260
....*....|....*....|....
gi 45551502 645 RLSTVKD-ADEILVLENGRVGERG 667
Cdd:PRK15134 485 DLHVVRAlCHQVIVLRQGEVVEQG 508
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
448-644 |
2.14e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 58.70 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 448 NSSIEFRNVSFEYEPGKPIfRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPN-----SGKVLIGGQDISAVDLES 522
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVI-KGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 523 L--RKVIAVVPQDSVLF-HNTIEHNIHYG----NLSKSHAE----VQNAARMADLHDSIMSWPGQYSTQvgerglkLSGG 591
Cdd:PRK14267 81 IevRREVGMVFQYPNPFpHLTIYDNVAIGvklnGLVKSKKElderVEWALKKAALWDEVKDRLNDYPSN-------LSGG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 45551502 592 EKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTRATSGRTSICIAH 644
Cdd:PRK14267 154 QRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
505-675 |
2.21e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 59.86 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 505 SGKVLIGGQDISavDLESLRKVIAVVPQDSVLF-HNTIEHNIHYG----NLSKSHAE--VQNAARMADLHDSIMSWPGQy 577
Cdd:PRK11650 58 SGEIWIGGRVVN--ELEPADRDIAMVFQNYALYpHMSVRENMAYGlkirGMPKAEIEerVAEAARILELEPLLDRKPRE- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 578 stqvgerglkLSGGEKQRVAIARAILKNTPILIFDEATSSLDSI------TEhniLQALTRATsGRTSICIAH-RLSTVK 650
Cdd:PRK11650 135 ----------LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKlrvqmrLE---IQRLHRRL-KTTSLYVTHdQVEAMT 200
|
170 180
....*....|....*....|....*
gi 45551502 651 DADEILVLENGRVGERGTHSELLRQ 675
Cdd:PRK11650 201 LADRVVVMNGGVAEQIGTPVEVYEK 225
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
344-663 |
2.33e-09 |
|
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: 60.58 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 344 AASLKTSSSLALLNFGQNAIFSSALSLIM------VLAAKEIAQGNMTVGdLVMVnaLLFqLSIPL-GFLGSV--YREVR 414
Cdd:COG4615 218 AERYRDLRIRADTIFALANNWGNLLFFALiglilfLLPALGWADPAVLSG-FVLV--LLF-LRGPLsQLVGALptLSRAN 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 415 QALLDMRAMFTLMNVDSSIQTAANAQPLFVDTtnSSIEFRNVSFEY--EPGKPIFR--DLSFTIPAGKNVAIVGGSGSGK 490
Cdd:COG4615 294 VALRKIEELELALAAAEPAAADAAAPPAPADF--QTLELRGVTYRYpgEDGDEGFTlgPIDLTIRRGELVFIVGGNGSGK 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 491 SSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIAVVPQDSVLFhntiEHNIHYGNLsKSHAEVQNAARMADLHD-- 568
Cdd:COG4615 372 STLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF----DRLLGLDGE-ADPARARELLERLELDHkv 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 569 SIMSwpGQYSTqvgergLKLSGGEKQRVAIARAILKNTPILIFDEATSSLDSI------TEhnILQALTRAtsGRTSICI 642
Cdd:COG4615 447 SVED--GRFST------TDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEfrrvfyTE--LLPELKAR--GKTVIAI 514
|
330 340
....*....|....*....|....*..
gi 45551502 643 AHrlstvkD------ADEILVLENGRV 663
Cdd:COG4615 515 SH------DdryfdlADRVLKMDYGKL 535
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
455-666 |
3.22e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 58.17 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 455 NVSFEYePGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLEslRKViaVVPQDS 534
Cdd:PRK11248 6 HLYADY-GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE--RGV--VFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 535 VLFHNTIEHNIHYGnlskshAEVQNAARMADLHDSimswpGQYSTQVGERGL------KLSGGEKQRVAIARAILKNTPI 608
Cdd:PRK11248 81 LLPWRNVQDNVAFG------LQLAGVEKMQRLEIA-----HQMLKKVGLEGAekryiwQLSGGQRQRVGIARALAANPQL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45551502 609 LIFDEATSSLDSITEHNILQALTR--ATSGRTSICIAHRL-STVKDADEILVLE--NGRVGER 666
Cdd:PRK11248 150 LLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITHDIeEAVFMATELVLLSpgPGRVVER 212
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
136-417 |
4.32e-09 |
|
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: 58.23 E-value: 4.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 136 LLTVCVPFLFKGAVDTMTTLNMDTApdavLSAATALMLGYGIARAsaaGFNELRNAVFAKVAHHSIRKIASNVFLHLHNL 215
Cdd:cd18570 16 LLGIAGSFFFQILIDDIIPSGDINL----LNIISIGLILLYLFQS---LLSYIRSYLLLKLSQKLDIRLILGYFKHLLKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 216 DLAFHLNKQTGA-LSKTIDrgSRGINFVLSAMVFNIVPTIFeLALVSSILgvkcgLAF-----AGVSMGCVGIYAAYTLS 289
Cdd:cd18570 89 PLSFFETRKTGEiISRFND--ANKIREAISSTTISLFLDLL-MVIISGII-----LFFynwklFLITLLIIPLYILIILL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 290 VTQW--RTQFRVFMNQAENEAgnKAVDSLINYETVKYFNNEKYeagCYNEVLKKYEAaSLKTSSSLALLNFGQNAIFSSA 367
Cdd:cd18570 161 FNKPfkKKNREVMESNAELNS--YLIESLKGIETIKSLNAEEQ---FLKKIEKKFSK-LLKKSFKLGKLSNLQSSIKGLI 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 45551502 368 LSLIMVLA----AKEIAQGNMTVGDLVMVNALLFQLSIPLGFLGSVYREVRQAL 417
Cdd:cd18570 235 SLIGSLLIlwigSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAK 288
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
127-417 |
4.46e-09 |
|
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: 58.42 E-value: 4.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 127 SLGLLAGSkLLTVCVPFLFKGAVDTMTTLNM---DTAPDAVLSAATALMLGYGIAraSAAGFneLRNAVFAKVAHHSIRK 203
Cdd:cd18780 2 TIALLVSS-GTNLALPYFFGQVIDAVTNHSGsggEEALRALNQAVLILLGVVLIG--SIATF--LRSWLFTLAGERVVAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 204 IASNVFLHLHNLDLAFHLNKQTGALsktIDRGSRGINFVLSAMVFNIvpTIFELALVSSILGVkcGLAFA------GVSM 277
Cdd:cd18780 77 LRKRLFSAIIAQEIAFFDVTRTGEL---LNRLSSDTQVLQNAVTVNL--SMLLRYLVQIIGGL--VFMFTtswkltLVML 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 278 GCVGIYAAYTLSVTQWRTQFRVFMNQAENEAGNKAVDSLINYETVKYFNNEKYEAGCYNEVLKKYEAASLKTSSSLALLN 357
Cdd:cd18780 150 SVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFN 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 358 FGQNAIFSSALSLIMVLAAKEIAQGNMTVGDLVMVNALLFQLSIPLGFLGSVYREVRQAL 417
Cdd:cd18780 230 GFMGAAAQLAIVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAV 289
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
468-674 |
5.11e-09 |
|
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: 57.45 E-value: 5.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 468 RDLSFTIPAGKNVAIVggsgsgkssMVRLLFRFFEPNSGKVLIGGQDISAVDL-ESLRKVIAVVPQDSVLFHN-TIEHNI 545
Cdd:cd03219 17 DDVSFSVRPGEIHGLIgpngagkttLFNLISGFLRPTSGSVLFDGEDITGLPPhEIARLGIGRTFQIPRLFPElTVLENV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 546 ---HYGNLSKSHAEVQNAARMADLHDSIMSW------PGQYSTQVGErglkLSGGEKQRVAIARAILKNTPILIFDEATS 616
Cdd:cd03219 97 mvaAQARTGSGLLLARARREEREARERAEELlervglADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDEPAA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45551502 617 SLdSITEHNILQALTR--ATSGRTSICIAHRLSTVKD-ADEILVLENGRVGERGTHSELLR 674
Cdd:cd03219 173 GL-NPEETEELAELIRelRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
589-662 |
8.34e-09 |
|
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: 56.67 E-value: 8.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 589 SGGEKQRVAIARAILKNTPILIFDEATSSLDsitEHN-------ILQALTRatsGRTSICIAHRLSTVKD-ADEILVLEN 660
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLD---AANravvvelIEEAKAR---GTAIIGIFHDEEVREAvADRVVDVTP 227
|
..
gi 45551502 661 GR 662
Cdd:COG4778 228 FS 229
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
505-630 |
9.09e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 56.71 E-value: 9.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 505 SGKVLIGGQDISA--VDLESLRKVIAVVPQDSVLFHNTIEHNIHYG-------NLSKSHAEVQNAARMADLHDSImswpg 575
Cdd:PRK14239 64 TGSIVYNGHNIYSprTDTVDLRKEIGMVFQQPNPFPMSIYENVVYGlrlkgikDKQVLDEAVEKSLKGASIWDEV----- 138
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 45551502 576 qySTQVGERGLKLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQAL 630
Cdd:PRK14239 139 --KDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETL 191
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
127-417 |
9.27e-09 |
|
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: 57.17 E-value: 9.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 127 SLGLLAGSKLLTVCVPFLFKGAVDTMTTLNMDtapdAVLSAATALMLgygIARASAAGFNELRNAVFAKVAHHSIRKIAS 206
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADGSR----EAFYRAVLLLL---LLSVLSGLFSGLRGGCFSYAGTRLVRRLRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 207 NVFLHLHNLDLAFHLNKQTGALSktidrgSRginfvLSA---MVFNIVPTIFELALVSSILGVkCGLAF--------AGV 275
Cdd:cd18572 74 DLFRSLLRQDIAFFDATKTGELT------SR-----LTSdcqKVSDPLSTNLNVFLRNLVQLV-GGLAFmfslswrlTLL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 276 SMGCVGIYAAYTLSVTQWRTQFRVFMNQAENEAGNKAVDSLINYETVKYFNNEKYEAGCYNEVLKKYEAASLKTSSSLAL 355
Cdd:cd18572 142 AFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAG 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45551502 356 LNFGQNAIFSSALSLIMVLAAKEIAQGNMTVGDLvmVNALLFQLSI--PLGFLGSVYREVRQAL 417
Cdd:cd18572 222 YVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQL--VTFMLYQQQLgeAFQSLGDVFSSLMQAV 283
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
124-417 |
1.03e-08 |
|
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: 57.05 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 124 VGISLGLLAGSKLLTVCVPFLFKGAVDTmttLNMDTAPDAVLSAATALMLGYgIARAsAAGFneLRNAVFAKVAHHSIRK 203
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDD---IFVEKDLEALLLVPLAIIGLF-LLRG-LASY--LQTYLMAYVGQRVVRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 204 IASNVFLHLHNLDLAFHLNKQTGALSktidrgSRGINFV--LSAMVFNIVPTIF-ELALVSSILGV------KcgLAFAG 274
Cdd:cd18552 74 LRNDLFDKLLRLPLSFFDRNSSGDLI------SRITNDVnqVQNALTSALTVLVrDPLTVIGLLGVlfyldwK--LTLIA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 275 VSMGCVGIYAAYTLSvtqwrTQFRVFMNQAENEAGN---KAVDSLINYETVKYFNNEKYEAGCYNEVLKKYEAASLKTSS 351
Cdd:cd18552 146 LVVLPLAALPIRRIG-----KRLRKISRRSQESMGDltsVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIAR 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45551502 352 SLALLNFGQNAIFSSALSLIMVLAAKEIAQGNMTVGDLVMVNALLFQLSIPLGFLGSVYREVRQAL 417
Cdd:cd18552 221 ARALSSPLMELLGAIAIALVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGL 286
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
444-673 |
2.06e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 56.26 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 444 VDTTNSSIEFRNVSFEYePGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEP-----NSGKVLIGGQDI-SA 517
Cdd:PRK14271 15 VDAAAPAMAAVNLTLGF-AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIfNY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 518 VDLESLRKVIAVVPQDSVLFHNTIEHNIHYGnlSKSHAEVQNA-------ARMAD--LHDSImswpgqySTQVGERGLKL 588
Cdd:PRK14271 94 RDVLEFRRRVGMLFQRPNPFPMSIMDNVLAG--VRAHKLVPRKefrgvaqARLTEvgLWDAV-------KDRLSDSPFRL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 589 SGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTRATSGRTSICIAHRLS-TVKDADEILVLENGRVGERG 667
Cdd:PRK14271 165 SGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEG 244
|
....*.
gi 45551502 668 THSELL 673
Cdd:PRK14271 245 PTEQLF 250
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
126-415 |
3.84e-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: 350008 [Multi-domain] Cd Length: 307 Bit Score: 55.60 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 126 ISLGLLAGSKLLTVCVPFLFKGAVD-----------TMTTLNMDTAPDAVLSAATALMLGYGIARASAAGFNelrNAVFA 194
Cdd:cd18564 3 LALLALLLETALRLLEPWPLKVVIDdvlgdkplpglLGLAPLLGPDPLALLLLAAAALVGIALLRGLASYAG---TYLTA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 195 KVAHHSIRKIASNVFLHLHNLDLAFHLNKQTGALSKTIDRGSRGINFVLSAMVFNIVPTIFELALvssILGVKC----GL 270
Cdd:cd18564 80 LVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVG---MLGVMFwldwQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 271 AFAGVSMGCVGIYAAYTLS--VTQWRTQFRvfmnQAENEAGNKAVDSLINYETVKYFNNEKYEAGCYNEVLKKYEAASLK 348
Cdd:cd18564 157 ALIALAVAPLLLLAARRFSrrIKEASREQR----RREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLR 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45551502 349 TSSSLALLNFGQNAIFSSALSLIMVLAAKEIAQGNMTVGDLvmvnaLLFqlsipLGFLGSVYREVRQ 415
Cdd:cd18564 233 AARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDL-----LVF-----LAYLKNLYKPVRD 289
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
463-619 |
3.94e-08 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 54.41 E-value: 3.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 463 GKPIFRDLSFTIPAGKNVAIvggsgsgkssM-------VRLL----------FRFfepnSGKVLIGGQDISAVDLEslRK 525
Cdd:COG4136 13 GRPLLAPLSLTVAPGEILTL----------MgpsgsgkSTLLaaiagtlspaFSA----SGEVLLNGRRLTALPAE--QR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 526 VIAVVPQDSVLF-HNTIEHNIHYG---NLSKS--HAEVQNAARMADLHDSIMSWPGQystqvgerglkLSGGEKQRVAIA 599
Cdd:COG4136 77 RIGILFQDDLLFpHLSVGENLAFAlppTIGRAqrRARVEQALEEAGLAGFADRDPAT-----------LSGGQRARVALL 145
|
170 180
....*....|....*....|
gi 45551502 600 RAILKNTPILIFDEATSSLD 619
Cdd:COG4136 146 RALLAEPRALLLDEPFSKLD 165
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
503-632 |
4.40e-08 |
|
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: 54.47 E-value: 4.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 503 PNSGKVLIGGQDISAVDL-ESLRKVIAVVPQDSVLFHN-TIEHNI----HYGNLSKSHAEVQNAARMADLHdsIMSWPGQ 576
Cdd:cd03218 52 PDSGKILLDGQDITKLPMhKRARLGIGYLPQEASIFRKlTVEENIlavlEIRGLSKKEREEKLEELLEEFH--ITHLRKS 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 45551502 577 ystqvgeRGLKLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNIlQALTR 632
Cdd:cd03218 130 -------KASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDI-QKIIK 177
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
447-674 |
4.42e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 54.71 E-value: 4.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 447 TNSSIEFRNVSFEyePGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPN----SGKVLIGGQDISAVDLES 522
Cdd:PRK10418 1 MPQQIELRNIALQ--AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPVAPCALRG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 523 lrKVIAVVPQDSVLFHNTIeHNIHygnlskSHAEVQNAARMADLHDSIMSwpgQYSTQVG----ERGLKL-----SGGEK 593
Cdd:PRK10418 79 --RKIATIMQNPRSAFNPL-HTMH------THARETCLALGKPADDATLT---AALEAVGlenaARVLKLypfemSGGML 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 594 QRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTR--ATSGRTSICIAHRLSTV-KDADEILVLENGRVGERGTHS 670
Cdd:PRK10418 147 QRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVE 226
|
....
gi 45551502 671 ELLR 674
Cdd:PRK10418 227 TLFN 230
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
505-662 |
4.78e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 56.43 E-value: 4.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 505 SGKVLIGGQDISavdlESLRKVIAVVPQDSVLF-HNTIEHNIHYGNLSKSHAEVQNAARMAdLHDSIMSWPGQY---STQ 580
Cdd:PLN03211 124 TGTILANNRKPT----KQILKRTGFVTQDDILYpHLTVRETLVFCSLLRLPKSLTKQEKIL-VAESVISELGLTkceNTI 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 581 VGERGLK-LSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQAL-TRATSGRTSICIAHRLST--VKDADEIL 656
Cdd:PLN03211 199 IGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLgSLAQKGKTIVTSMHQPSSrvYQMFDSVL 278
|
....*.
gi 45551502 657 VLENGR 662
Cdd:PLN03211 279 VLSEGR 284
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
470-675 |
5.32e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 55.96 E-value: 5.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 470 LSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGK--VLIGGQDISAVDLESL-----RKVIAVVPQDSVLF-HNTI 541
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVDMTKPGPDgrgraKRYIGILHQEYDLYpHRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 542 ehnihYGNLSKSHA-EVQNA-ARMADLHDSIMS-WPGQYSTQVGER-GLKLSGGEKQRVAIARAILKNTPILIFDEATSS 617
Cdd:TIGR03269 383 -----LDNLTEAIGlELPDElARMKAVITLKMVgFDEEKAEEILDKyPDELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45551502 618 LDSITE----HNILQAltRATSGRTSICIAHRLSTVKD-ADEILVLENGRVGERGTHSELLRQ 675
Cdd:TIGR03269 458 MDPITKvdvtHSILKA--REEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
464-673 |
5.65e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 54.61 E-value: 5.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 464 KPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIAVVPQDSVLFHN-TIE 542
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 543 HNIHYGN------LSKSHAEVQNAARMADLHDSIMSWPGQYSTqvgerglKLSGGEKQRVAIARAILKNTPILIFDEATS 616
Cdd:PRK10253 100 ELVARGRyphqplFTRWRKEDEEAVTKAMQATGITHLADQSVD-------TLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 617 SLDSITEHNILQALTR--ATSGRTSICIAHRLS-TVKDADEILVLENGRVGERGTHSELL 673
Cdd:PRK10253 173 WLDISHQIDLLELLSElnREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
453-663 |
6.98e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 53.42 E-value: 6.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 453 FRNVSFEYEPG---KPIFRDLSFTIPAGKnvaivggsgsgkssMVRLLFRffePNSGKvliggqdisavdlESLRKVIAV 529
Cdd:cd03233 6 WRNISFTTGKGrskIPILKDFSGVVKPGE--------------MVLVLGR---PGSGC-------------STLLKALAN 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 530 VPQDSVlfhnTIEHNIHYGNLSKSHAEVQNAARMA-----DLHDSIMSwpgqystqVGE--------------RGLklSG 590
Cdd:cd03233 56 RTEGNV----SVEGDIHYNGIPYKEFAEKYPGEIIyvseeDVHFPTLT--------VREtldfalrckgnefvRGI--SG 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45551502 591 GEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQAL-TRATSGRTSICIAhrLS-----TVKDADEILVLENGRV 663
Cdd:cd03233 122 GERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIrTMADVLKTTTFVS--LYqasdeIYDLFDKVLVLYEGRQ 198
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
453-619 |
7.63e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 55.46 E-value: 7.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 453 FRNVSFEYePGKPIFRDLSFTIPAGKNVAIVggsgsgkssMVRLLFRFFEPNSGKVLIGGqdisavdleslRKVIAVVPQ 532
Cdd:COG0488 1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVgrngagkstLLKILAGELEPDSGEVSIPK-----------GLRIGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 533 DSVLF-HNTIEHNIHYGN------------LSKSHAEV-QNAARMADLHD---------------SIMS----WPGQYST 579
Cdd:COG0488 69 EPPLDdDLTVLDTVLDGDaelraleaeleeLEAKLAEPdEDLERLAELQEefealggweaearaeEILSglgfPEEDLDR 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 45551502 580 QVGErglkLSGGEKQRVAIARAILKNTPILIFDEATSSLD 619
Cdd:COG0488 149 PVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
468-663 |
8.49e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.42 E-value: 8.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 468 RDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQdisAVDLES----LRKVIAVVPQDSVLFHN-TIE 542
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGK---PVRIRSprdaIALGIGMVHQHFMLVPNlTVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 543 HNIHYG---------NLSKSHAEVQNAARmadlhdsimswpgQYstqvgerGLK---------LSGGEKQRVAIARAILK 604
Cdd:COG3845 99 ENIVLGleptkggrlDRKAARARIRELSE-------------RY-------GLDvdpdakvedLSVGEQQRVEILKALYR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45551502 605 NTPILIFDEATSSLdsiTEH------NILQALTRAtsGRTSICIAHRLSTVKD-ADEILVLENGRV 663
Cdd:COG3845 159 GARILILDEPTAVL---TPQeadelfEILRRLAAE--GKSIIFITHKLREVMAiADRVTVLRRGKV 219
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
451-663 |
8.97e-08 |
|
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: 53.49 E-value: 8.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEY-----EPG---------------KPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLI 510
Cdd:cd03267 1 IEVSNLSKSYrvyskEPGligslkslfkrkyreVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 511 GGQDISAVDLESLRKVIAVVPQDSVLFHN-----TIEHNIHYGNLSKSHAEvQNAARMADLHD--SIMSWPGQystqvge 583
Cdd:cd03267 81 AGLVPWKRRKKFLRRIGVVFGQKTQLWWDlpvidSFYLLAAIYDLPPARFK-KRLDELSELLDleELLDTPVR------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 584 rglKLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNI---LQALTRATsGRTSICIAHRLSTV-KDADEILVLE 659
Cdd:cd03267 153 ---QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIrnfLKEYNRER-GTTVLLTSHYMKDIeALARRVLVID 228
|
....
gi 45551502 660 NGRV 663
Cdd:cd03267 229 KGRL 232
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
587-658 |
9.90e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.20 E-value: 9.90e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45551502 587 KLSGGEKQRVAIARAILKNTPILIFDEATSSLDsITEH-NILQALTRATSGRTSICIAHRLsTVKD--ADEILVL 658
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLD-IRQRlNVARLIRELAEGKYVLVVEHDL-AVLDylADNVHIA 284
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
124-417 |
1.03e-07 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 53.98 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 124 VGISLGLLAGskLLTVCVPFLFKGAVDTMTTLNMDTAPDAVLsaaTALMLGYGIARAsaagfneLRNAVFAKVAHHSIRK 203
Cdd:cd18551 3 LALLLSLLGT--AASLAQPLLVKNLIDALSAGGSSGGLLALL---VALFLLQAVLSA-------LSSYLLGRTGERVVLD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 204 IASNVFLHLHNLDLAFHLNKQTGALSktidrgSRGINFvlSAMVFNIVPTIFeLALVSSILGVKCGLAF--------AGV 275
Cdd:cd18551 71 LRRRLWRRLLRLPVSFFDRRRSGDLV------SRVTND--TTLLRELITSGL-PQLVTGVLTVVGAVVLmflldwvlTLV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 276 SMGCVGIYAAYTLSVTQwrtQFRVFMNQAENEAGNKAVD---SLINYETVKYFNNEKYEAGCYNEVLKKYEAASLKTSSS 352
Cdd:cd18551 142 TLAVVPLAFLIILPLGR---RIRKASKRAQDALGELSAAlerALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKI 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45551502 353 LALLNFGQNAIFSSALSLIMVLAAKEIAQGNMTVGDLVMVNALLFQLSIPLGFLGSVYREVRQAL 417
Cdd:cd18551 219 EALIGPLMGLAVQLALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKAL 283
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
463-643 |
1.30e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 52.57 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 463 GKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDIsavDLESLRKVI-------AVVPQDSV 535
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI---DDPDVAEAChylghrnAMKPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 536 L--------FHNTIEHNIHYGnlskshAEVQNAARMADLhdsimswPGQYstqvgerglkLSGGEKQRVAIARAILKNTP 607
Cdd:PRK13539 91 AenlefwaaFLGGEELDIAAA------LEAVGLAPLAHL-------PFGY----------LSAGQKRRVALARLLVSNRP 147
|
170 180 190
....*....|....*....|....*....|....*.
gi 45551502 608 ILIFDEATSSLDSITEhNILQALTRATSGRTSICIA 643
Cdd:PRK13539 148 IWILDEPTAALDAAAV-ALFAELIRAHLAQGGIVIA 182
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
451-663 |
1.33e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 54.67 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEpGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKV-IAV 529
Cdd:PRK15439 12 LCARSISKQYS-GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 530 VPQDSVLFHN-TIEHNIHYGnLSKSHAevqNAARMADLHDSIMSwpgQYSTQVGERGLKLSggEKQRVAIARAILKNTPI 608
Cdd:PRK15439 91 VPQEPLLFPNlSVKENILFG-LPKRQA---SMQKMKQLLAALGC---QLDLDSSAGSLEVA--DRQIVEILRGLMRDSRI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 45551502 609 LIFDEATSSLDSITEHNILQALtRA--TSGRTSICIAHRLSTVKD-ADEILVLENGRV 663
Cdd:PRK15439 162 LILDEPTASLTPAETERLFSRI-REllAQGVGIVFISHKLPEIRQlADRISVMRDGTI 218
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
127-417 |
1.42e-07 |
|
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: 53.67 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 127 SLGLLAGSKLLTVCVPFLFKGAVDTMTTLNMDTAPDAV-LSAATALMLGYGIARASAagfNELRNAVFAKVAHHSIRKIA 205
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDVASKESGDIEIFGLsLKTFALALLGVFVVGAAA---NFGRVYLLRIAGERIVARLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 206 SNVFLHLHNLDLAFHLNKQTG---------------ALSKTIDRGSRGINFVL--SAMVFNIVPtifELALVssILGVKC 268
Cdd:cd18573 78 KRLFKSILRQDAAFFDKNKTGelvsrlssdtsvvgkSLTQNLSDGLRSLVSGVggIGMMLYISP---KLTLV--MLLVVP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 269 GLAFAGVsmgcvgIYAAYTLSVTqWRTQfrvfmnQAENEAGNKAVDSLINYETVKYFNNEKYEAGCYNEVLKKyeaaSLK 348
Cdd:cd18573 153 PIAVGAV------FYGRYVRKLS-KQVQ------DALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDE----VFD 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 349 TSSSLALLNfgqnAIFSSA------LSLIMVLAA--KEIAQGNMTVGDL-------VMVNALLFQLSiplgflgSVYREV 413
Cdd:cd18573 216 LAKKEALAS----GLFFGStgfsgnLSLLSVLYYggSLVASGELTVGDLtsflmyaVYVGSSVSGLS-------SFYSEL 284
|
....
gi 45551502 414 RQAL 417
Cdd:cd18573 285 MKGL 288
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
560-662 |
1.48e-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: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 560 AARMADLHDSIMSWPGQYSTQVGE---RGLklSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALtratsg 636
Cdd:TIGR00956 181 AKHIADVYMATYGLSHTRNTKVGNdfvRGV--SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRAL------ 252
|
90 100 110
....*....|....*....|....*....|....*.
gi 45551502 637 RTSICIAHRLSTV------KDA----DEILVLENGR 662
Cdd:TIGR00956 253 KTSANILDTTPLVaiyqcsQDAyelfDKVIVLYEGY 288
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
588-656 |
1.82e-07 |
|
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: 51.55 E-value: 1.82e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45551502 588 LSGGEKQRVAIARAILKNTP--ILIFDEATSSLDSITEHNILQALTR-ATSGRTSICIAHRLSTVKDADEIL 656
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGlIDLGNTVILIEHNLDVLSSADWII 159
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
124-391 |
1.96e-07 |
|
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: 53.16 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 124 VGISLGLLAGSKLLTVCVPFLFKGAVDtmttlNMDTAPDAVLSAATALMLGYGIARASAAGFNELRNAVFAKVAHHSIRK 203
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAID-----DYIVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 204 IASNVFLHLHNLDLAFHLNKQTGALSktidrgSRGINFV--LSAMVFNIVPTIF-ELALVSSILGVkcgLAFAGVSMgcv 280
Cdd:cd18544 76 LRRDLFSHIQRLPLSFFDRTPVGRLV------TRVTNDTeaLNELFTSGLVTLIgDLLLLIGILIA---MFLLNWRL--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 281 giyAAYTLSV-------TQWrtqFRVFMNQAENEAGNKAvdSLIN---------YETVKYFNNEKYEAGCYNEVLKKYEA 344
Cdd:cd18544 144 ---ALISLLVlpllllaTYL---FRKKSRKAYREVREKL--SRLNaflqesisgMSVIQLFNREKREFEEFDEINQEYRK 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 45551502 345 ASLKTSSSLALLNFGQNAIFSSALSLIMVLAAKEIAQGNMTVGDLVM 391
Cdd:cd18544 216 ANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSGAVTLGVLYA 262
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
463-630 |
2.04e-07 |
|
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: 52.11 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 463 GKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIAVVPQDSVLFHNTIE 542
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 543 HNIHYgnlskshaevqnaarMADLHDSIMSWpgQYSTQVGERGLK------LSGGEKQRVAIARAILKNTPILIFDEATS 616
Cdd:cd03231 92 ENLRF---------------WHADHSDEQVE--EALARVGLNGFEdrpvaqLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170
....*....|....
gi 45551502 617 SLDSITEHNILQAL 630
Cdd:cd03231 155 ALDKAGVARFAEAM 168
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
470-688 |
3.10e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 52.24 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 470 LSFTIPAGKNVAIVGGS----GSGKSSMVRLLfrffePNSGKVLIGGQDISAVDLESLRKVIA-VVPQDSVLFhntIEHN 544
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNgagkSTLLARMAGLL-----PGSGSIQFAGQPLEAWSAAELARHRAyLSQQQTPPF---AMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 545 IHYGNLSKsHAEVQNAARMADLHD-----SIMSWPGQYSTQvgerglkLSGGEKQRVAIARAILKNTP-------ILIFD 612
Cdd:PRK03695 87 FQYLTLHQ-PDKTRTEAVASALNEvaealGLDDKLGRSVNQ-------LSGGEWQRVRLAAVVLQVWPdinpagqLLLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45551502 613 EATSSLDsITEHNILQALTR--ATSGRTSICIAHRLS-TVKDADEILVLENGRVGERGTHSELLRQNGLyARLWETQTQ 688
Cdd:PRK03695 159 EPMNSLD-VAQQAALDRLLSelCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPENL-AQVFGVNFR 235
|
|
| ABC_6TM_McjD_like |
cd18556 |
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ... |
199-417 |
5.28e-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: 51.87 E-value: 5.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 199 HSIRKIASNVFLHLHNLDLAFHLNKQTGALSKTIDRGSRGINFVLSAMVFNIVPTIFELALVSSILGVKCGLAFAGVSMg 278
Cdd:cd18556 74 ELIISISSSYFRYLYEQPKTFFVKENSGDITQRLNQASNDLYTLVRNLSTNILPPLLQLIIAIVVILSSGDYFVAALFL- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 279 cvgIYAAYTLSVTQWRTQFRVFMNQAENEAGNKA----VDSLINYETVKYFNNEKYEAGCYNEVLKKYEAAS---LKTSS 351
Cdd:cd18556 153 ---LYAVLFVINNTIFTKKIVSLRNDLMDAGRKSysllTDSVKNIVAAKQNNAFDFLFKRYEATLTNDRNSQkryWKLTF 229
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45551502 352 SLALLNFGQNAIFSSALSLIMVLAAKeiaQGNMTVGDLVMVNALLFQLSIPLGFLGSVYREVRQAL 417
Cdd:cd18556 230 KMLILNSLLNVILFGLSFFYSLYGVV---NGQVSIGHFVLITSYILLLSTPIESLGNMLSELRQSV 292
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
587-619 |
5.65e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.86 E-value: 5.65e-07
10 20 30
....*....|....*....|....*....|...
gi 45551502 587 KLSGGEKQRVAIARAILKNTPILIFDEATSSLD 619
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
469-667 |
6.61e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.55 E-value: 6.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 469 DLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDI---SAVDLESLRKVIAVVPQD---SVLFHNTIE 542
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQDpyaSLDPRQTVG 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 543 HNIH-----YGNLSKSHAevqnAARMADLHDSIMSWPGQYSTQVGErglkLSGGEKQRVAIARAILKNTPILIFDEATSS 617
Cdd:PRK10261 422 DSIMeplrvHGLLPGKAA----AARVAWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEAVSA 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 45551502 618 LD-SITEH--NILQALTRATsGRTSICIAHRLSTVKD-ADEILVLENGRVGERG 667
Cdd:PRK10261 494 LDvSIRGQiiNLLLDLQRDF-GIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
165-421 |
6.80e-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: 51.73 E-value: 6.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 165 LSAATALMLGYGIARASAAGFNELRNAVFAkvahHSIRKI----ASNVFLHLHNLDLAFHLNKQTGalsKTIDRgSRGI- 239
Cdd:cd18588 38 LSTLDVLAIGLLVVALFEAVLSGLRTYLFS----HTTNRIdaelGARLFRHLLRLPLSYFESRQVG---DTVAR-VRELe 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 240 ---NFVLSAMVFNIVPTIFELALVSSILGVKCGLAFagVSMGCVGIYAAYTLSVT---QWRTQfRVFMNQAENEAGNkaV 313
Cdd:cd18588 110 sirQFLTGSALTLVLDLVFSVVFLAVMFYYSPTLTL--IVLASLPLYALLSLLVTpilRRRLE-EKFQRGAENQSFL--V 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 314 DSLINYETVKYFNNEKYEAGCYNEVLKKYEAASLKTSSslaLLNFGQNAIfsSALSLIMVLA-----AKEIAQGNMTVGD 388
Cdd:cd18588 185 ETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTAN---LSNLASQIV--QLIQKLTTLAilwfgAYLVMDGELTIGQ 259
|
250 260 270
....*....|....*....|....*....|...
gi 45551502 389 LVMVNALLFQLSIPLGFLGSVYREVRQALLDMR 421
Cdd:cd18588 260 LIAFNMLAGQVSQPVLRLVQLWQDFQQAKVSVE 292
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
572-671 |
8.31e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 49.88 E-value: 8.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 572 SWPGqYSTQVGERGLKLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTRAT--SGRTSICIAHRLSTV 649
Cdd:cd03222 57 EWDG-ITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSeeGKKTALVVEHDLAVL 135
|
90 100
....*....|....*....|..
gi 45551502 650 KDADEILVLENGRVGERGTHSE 671
Cdd:cd03222 136 DYLSDRIHVFEGEPGVYGIASQ 157
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
124-392 |
9.13e-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: 51.32 E-value: 9.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 124 VGISLGLLAGskLLTVCVPFLFKGAVDTMTTLNM-DTAPDAVLSAAT--ALMLGY-GIARAsAAGFneLRNAVFAKVAHH 199
Cdd:cd18577 3 IGLLAAIAAG--AALPLMTIVFGDLFDAFTDFGSgESSPDEFLDDVNkyALYFVYlGIGSF-VLSY--IQTACWTITGER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 200 SIRKIASNVFLHLHNLDLAFHLNKQTGALSKTIDRGSR----GINFVLSAMVFNIVPTIF----------ELALVSsilg 265
Cdd:cd18577 78 QARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNliqdGIGEKLGLLIQSLSTFIAgfiiafiyswKLTLVL---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 266 vkcgLAFAGVSMGCVGIYAAYTLSVTQWrtqfrvfMNQAENEAGNKAVDSLINYETVKYFNNEKYEAGCYNEVLKKYEAA 345
Cdd:cd18577 154 ----LATLPLIAIVGGIMGKLLSKYTKK-------EQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKA 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 45551502 346 SLKTSSSLALLNFGQNAIFSSALSLIMVLAAKEIAQGNMTVGDLVMV 392
Cdd:cd18577 223 GIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISPGDVLTV 269
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
587-674 |
9.49e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 51.28 E-value: 9.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 587 KLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALT--RATSGRTSICIAHRLSTVKD-ADEILVLENGRV 663
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLelQQKENMALVLITHDLALVAEaAHKIIVMYAGQV 232
|
90
....*....|.
gi 45551502 664 GERGTHSELLR 674
Cdd:PRK11022 233 VETGKAHDIFR 243
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
505-662 |
1.08e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 51.75 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 505 SGKVLIGGQDISAVDL-ESLRKVIAVVPQDSVLFHN-TIEHNIHYGNLSKSHAEVQNAARMADLHDSIMSWPGQYSTQVG 582
Cdd:TIGR02633 57 DGEIYWSGSPLKASNIrDTERAGIVIIHQELTLVPElSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVT 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 583 ERGLKLSGGEKQRVAIARAILKNTPILIFDEATSSLDSiTEHNILQALTRATSGRTSIC--IAHRLSTVKD-ADEILVLE 659
Cdd:TIGR02633 137 RPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTE-KETEILLDIIRDLKAHGVACvyISHKLNEVKAvCDTICVIR 215
|
...
gi 45551502 660 NGR 662
Cdd:TIGR02633 216 DGQ 218
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
463-622 |
1.29e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 50.28 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 463 GKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDL-ESLRKVIAVVPQDSVLFHN-T 540
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRRlS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 541 IEHNIH-----YGNLSKSHAEVQNAARMADLHDSIMSwpgqystqvGERGLKLSGGEKQRVAIARAILKNTPILIFDEAT 615
Cdd:PRK10895 95 VYDNLMavlqiRDDLSAEQREDRANELMEEFHIEHLR---------DSMGQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
....*..
gi 45551502 616 SSLDSIT 622
Cdd:PRK10895 166 AGVDPIS 172
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
141-420 |
1.52e-06 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 50.50 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 141 VPFLFKGAVDTMTTLNMDTAPDAVLSAATALMLGYGIARASAAGFNELRNAVFAKVAHHSIRKIASNVFLHLHNLDLAFH 220
Cdd:cd18554 18 LPLILKYIVDDVIQGSSLTLDEKVYKLFTIIGIMFFIFLILRPPVEYYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 221 LNKQTGAL-SKTIDRGSRGINFVLSAMVfNIVPTIFELALVSSI---LGVKcgLAFAGVSmgcvgIYAAYTLSVTQWRTQ 296
Cdd:cd18554 98 ANNRSGEIiSRVINDVEQTKDFITTGLM-NIWLDMITIIIAICImlvLNPK--LTFVSLV-----IFPFYILAVKYFFGR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 297 FRVF---MNQAENEAGNKAVDSLINYETVKYFNNEKYEAGCYNEVLKKYEAASLKTSSSLALLNFGQNAIFSSALSLIMV 373
Cdd:cd18554 170 LRKLtkeRSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNTITDLAPLLVIG 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 45551502 374 LAAKEIAQGNMTVGDLVMVNALLFQLSIPLGFLGSVYREVRQALLDM 420
Cdd:cd18554 250 FAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASM 296
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
124-416 |
1.96e-06 |
|
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: 50.17 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 124 VGISLGLLAGSKLLTVCVPFLFKGAVDTMTTLNmDTAPdavLSAATALMLGYGIARASAAGfneLRNAVFAKVAH---HS 200
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGPIAHG-DRSA---LWPLVLLLLALGVAEAVLSF---LRRYLAGRLSLgveHD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 201 IRkiaSNVFLHLHNLDLAFHLNKQTGALsktIDRGS---RGINFVLSAMVFNIVPTIfeLALVSSILgvkcgLAFAGVSM 277
Cdd:cd18543 74 LR---TDLFAHLQRLDGAFHDRWQSGQL---LSRATsdlSLVQRFLAFGPFLLGNLL--TLVVGLVV-----MLVLSPPL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 278 GCVGIYAAYTLSVTQWRTQFRVF--MNQAENEAGNKA--VDslinyET------VKYFNNEKYEAGCYNEVLKKYEAASL 347
Cdd:cd18543 141 ALVALASLPPLVLVARRFRRRYFpaSRRAQDQAGDLAtvVE-----ESvtgirvVKAFGRERRELDRFEAAARRLRATRL 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45551502 348 KTSSSLALLNFGQNAIFSSALSLIMVLAAKEIAQGNMTVGDLVMVNALLFQLSIPLGFLGSVYREVRQA 416
Cdd:cd18543 216 RAARLRARFWPLLEALPELGLAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRA 284
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
124-425 |
2.23e-06 |
|
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: 50.17 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 124 VGISLGLLAGSKLLTVCVPFLFKGAVDTmTTLNMDTApdaVLSAATALMLGYGIArasAAGFNELRNAVFAKVAHHSIRK 203
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDD-ALPQGDLG---LLVLLALGMVAVAVA---SALLGVVQTYLSARIGQGVMYD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 204 IASNVFLHLHNLDLAFHLNKQTGALSktidrgSRGINFVLSA--MVFNIVPTIfelalVSSILGVkcglAFAGVSM---- 277
Cdd:cd18550 74 LRVQLYAHLQRMSLAFFTRTRTGEIQ------SRLNNDVGGAqsVVTGTLTSV-----VSNVVTL----VATLVAMlald 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 278 -----GCVGIYAAYTLsVTQW--RTQFRVFMNQAENEAgnkAVDSLINyET--------VKYFNNEKYEAGCYNEVLKky 342
Cdd:cd18550 139 wrlalLSLVLLPLFVL-PTRRvgRRRRKLTREQQEKLA---ELNSIMQ-ETlsvsgallVKLFGREDDEAARFARRSR-- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 343 EAASLKTSSSLA--LLNFGQNAIFSSALSLIMVLAAKEIAQGNMTVGDLVMVNALLFQLSIPLGFLGSVYREVRQALldm 420
Cdd:cd18550 212 ELRDLGVRQALAgrWFFAALGLFTAIGPALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSL--- 288
|
....*
gi 45551502 421 rAMFT 425
Cdd:cd18550 289 -ALFE 292
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
452-665 |
2.35e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 50.79 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 452 EFRNVSfeyepGKPIFRDLSFTIPAGKNVAI----------VggsgsgkssmVRLLFRFFEPNSGKVLIGGQDISAVD-L 520
Cdd:COG1129 258 EVEGLS-----VGGVVRDVSFSVRAGEILGIaglvgagrteL----------ARALFGADPADSGEIRLDGKPVRIRSpR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 521 ESLRKVIAVVPQD----SVLFHNTIEHNIHYGNLSK-------SHAEVQNAA---------RMADLHDSIMSwpgqystq 580
Cdd:COG1129 323 DAIRAGIAYVPEDrkgeGLVLDLSIRENITLASLDRlsrggllDRRRERALAeeyikrlriKTPSPEQPVGN-------- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 581 vgerglkLSGGEKQRVAIARAILKNTPILIFDEATSSLD--SITE-HNILQALTRAtsGRTSICI----------AHRls 647
Cdd:COG1129 395 -------LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDvgAKAEiYRLIRELAAE--GKAVIVIsselpellglSDR-- 463
|
250
....*....|....*....
gi 45551502 648 tvkdadeILVLENGR-VGE 665
Cdd:COG1129 464 -------ILVMREGRiVGE 475
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
445-682 |
3.50e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 50.21 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 445 DTTNSSIEFRNVSfEYEPGKPIFR---DLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPN-SGKVLIGGQDISAVD- 519
Cdd:TIGR02633 252 EIGDVILEARNLT-CWDVINPHRKrvdDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNp 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 520 LESLRKVIAVVPQD----SVLFHNTIEHNIHYGNLSK-SHAEVQNAARMADLHDSIMSwpgQYSTQVGERGL---KLSGG 591
Cdd:TIGR02633 331 AQAIRAGIAMVPEDrkrhGIVPILGVGKNITLSVLKSfCFKMRIDAAAELQIIGSAIQ---RLKVKTASPFLpigRLSGG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 592 EKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTR-ATSGRTSICIAHRLSTVKD-ADEILVLENGRVGERGTH 669
Cdd:TIGR02633 408 NQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKLKGDFVN 487
|
250
....*....|...
gi 45551502 670 SELLRQNGLYARL 682
Cdd:TIGR02633 488 HALTQEQVLAAAL 500
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
567-673 |
3.56e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 49.80 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 567 HDSIM-SWPGQystqvgerglkLSGGEKQRVAIARAiLKNTP-ILIFDEATSSLDSITEHNILQALTR--ATSGRTSICI 642
Cdd:PRK15093 148 HKDAMrSFPYE-----------LTEGECQKVMIAIA-LANQPrLLIADEPTNAMEPTTQAQIFRLLTRlnQNNNTTILLI 215
|
90 100 110
....*....|....*....|....*....|..
gi 45551502 643 AHRLSTV-KDADEILVLENGRVGERGTHSELL 673
Cdd:PRK15093 216 SHDLQMLsQWADKINVLYCGQTVETAPSKELV 247
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
579-659 |
4.00e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 48.90 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 579 TQVGERGL-KLSGGEKQRVAIARAILKNTPILIFDEATSSLDsitehnILQALTRATsgrtsicIAHRLStvKDADEILV 657
Cdd:cd03236 130 RHVLDRNIdQLSGGELQRVAIAAALARDADFYFFDEPSSYLD------IKQRLNAAR-------LIRELA--EDDNYVLV 194
|
..
gi 45551502 658 LE 659
Cdd:cd03236 195 VE 196
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
469-675 |
4.22e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 49.34 E-value: 4.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 469 DLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPN---SGKVLIGGQDISAVDLESLRKV----IAVVPQDSVLFHNT- 540
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKELNKLraeqISMIFQDPMTSLNPy 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 541 -------IEHNIHYGNLSKSHA-----EVQNAARMADLHDSIMSWPGQYstqvgerglklSGGEKQRVAIARAILKNTPI 608
Cdd:PRK09473 114 mrvgeqlMEVLMLHKGMSKAEAfeesvRMLDAVKMPEARKRMKMYPHEF-----------SGGMRQRVMIAMALLCRPKL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 609 LIFDEATSSLDSITEHNILQALTRATS--GRTSICIAHRLSTVKD-ADEILVLENGRVGERGTHSELLRQ 675
Cdd:PRK09473 183 LIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGNARDVFYQ 252
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
576-663 |
6.29e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 48.47 E-value: 6.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 576 QYSTQVG------ERGLKLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQAL--TRATSGRTSICIAHRLS 647
Cdd:PRK09984 135 QALTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLrdINQNDGITVVVTLHQVD 214
|
90
....*....|....*..
gi 45551502 648 -TVKDADEILVLENGRV 663
Cdd:PRK09984 215 yALRYCERIVALRQGHV 231
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
126-417 |
7.17e-06 |
|
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: 48.55 E-value: 7.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 126 ISLGLLAGSKLLTVCVPFLFKGAVDTMTTLNMDTAP---DAVLSAATALMLGYGIArasaAGFNELRNAVFAKVAHHSIR 202
Cdd:cd18547 3 LVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGvdfSGLLRILLLLLGLYLLS----ALFSYLQNRLMARVSQRTVY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 203 KIASNVFLHLHNLDLAFHLNKQTGA-LSKT---IDRGSRGINFVLSAM---VFNIVPTIFELALVSSILGVkCGLAFAGV 275
Cdd:cd18547 79 DLRKDLFEKLQRLPLSYFDTHSHGDiMSRVtndVDNISQALSQSLTQLissILTIVGTLIMMLYISPLLTL-IVLVTVPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 276 SMGCVGIYAAytlsvtqwRTQfRVFMNQAENEAgnkAVDSLI-----NYETVKYFNNEKYEAGCYNEVLKKYEAASLK-- 348
Cdd:cd18547 158 SLLVTKFIAK--------RSQ-KYFRKQQKALG---ELNGYIeemisGQKVVKAFNREEEAIEEFDEINEELYKASFKaq 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45551502 349 -TSSSLA-LLNFGQNAIFssalSLIMVLAAKEIAQGNMTVGDLVMVNALLFQLSIPLGFLGSVYREVRQAL 417
Cdd:cd18547 226 fYSGLLMpIMNFINNLGY----VLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSAL 292
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
505-665 |
7.72e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 47.85 E-value: 7.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 505 SGKVLIGGQDISAVDLE---SLR-KVIAVVPQDSVLFH--NTIEhNIHYGNLSKSHAEVQNAARMADLHDSImswpgqys 578
Cdd:PRK10584 64 SGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQSFMLIPtlNALE-NVELPALLRGESSRQSRNGAKALLEQL-------- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 579 tQVGER----GLKLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNI---LQALTRaTSGRTSICIAHRLSTVKD 651
Cdd:PRK10584 135 -GLGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIadlLFSLNR-EHGTTLILVTHDLQLAAR 212
|
170
....*....|....
gi 45551502 652 ADEILVLENGRVGE 665
Cdd:PRK10584 213 CDRRLRLVNGQLQE 226
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
464-679 |
8.25e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.96 E-value: 8.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 464 KPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVD-LESLRKVIAVVPQD---SVLFHN 539
Cdd:PRK10982 261 QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaNEAINHGFALVTEErrsTGIYAY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 540 -TIEHNIHYGNLS--KSHAEVQNAARM-ADLH---DSIMSWPGQYSTQVGErglkLSGGEKQRVAIARAILKNTPILIFD 612
Cdd:PRK10982 341 lDIGFNSLISNIRnyKNKVGLLDNSRMkSDTQwviDSMRVKTPGHRTQIGS----LSGGNQQKVIIGRWLLTQPEILMLD 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45551502 613 EATSSLDSITEHNILQALTR-ATSGRTSICIAHRLSTVKD-ADEILVLENGRVG-----ERGTHSELLRQNGLY 679
Cdd:PRK10982 417 EPTRGIDVGAKFEIYQLIAElAKKDKGIIIISSEMPELLGiTDRILVMSNGLVAgivdtKTTTQNEILRLASLH 490
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
163-409 |
9.02e-06 |
|
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: 48.16 E-value: 9.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 163 AVLSAATALMLGYGIARASAAGFNELRNAVFAKVAHHSirkiasnvflhLHNLDlAFhlnkQTGALsktIDRGSRGINFV 242
Cdd:cd18548 49 ALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFS-----------FAEID-KF----GTSSL---ITRLTNDVTQV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 243 LSA--MVFNIV---PTIFELALV-SSILGVKCGLAFAgVSMGCVGIYAAYTLSVTqwrtqFRVFMN-QAENEAGNKAV-D 314
Cdd:cd18548 110 QNFvmMLLRMLvraPIMLIGAIImAFRINPKLALILL-VAIPILALVVFLIMKKA-----IPLFKKvQKKLDRLNRVVrE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 315 SLINYETVKYFNNEKYEAGCYNEVLKKYEAASLKTSSSLALLNFGQNAIFSSALSLIMVLAAKEIAQGNMTVGDLVMVNA 394
Cdd:cd18548 184 NLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLVAFIN 263
|
250
....*....|....*
gi 45551502 395 LLFQLSIPLGFLGSV 409
Cdd:cd18548 264 YLMQILMSLMMLSMV 278
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
581-662 |
9.56e-06 |
|
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: 46.21 E-value: 9.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 581 VGERGLKLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQAL-------TRATSGRTSICIAHRLSTVKDA- 652
Cdd:smart00382 54 VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllllLKSEKNLTVILTTNDEKDLGPAl 133
|
90
....*....|....*
gi 45551502 653 -----DEILVLENGR 662
Cdd:smart00382 134 lrrrfDRRIVLLLIL 148
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
433-619 |
9.85e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.79 E-value: 9.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 433 IQTAANAQplfVDTTNSS----IEFRNVSFEYePGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKV 508
Cdd:PRK11147 301 VMGTAKMQ---VEEASRSgkivFEMENVNYQI-DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 509 LIG--------GQDISAVDLEslrkviavvpqdsvlfhNTIEHNIHYGnlsKSHAEVQNAAR--MADLHDSIMSwPGQYS 578
Cdd:PRK11147 377 HCGtklevayfDQHRAELDPE-----------------KTVMDNLAEG---KQEVMVNGRPRhvLGYLQDFLFH-PKRAM 435
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 45551502 579 TQVGerglKLSGGEKQRVAIARAILKNTPILIFDEATSSLD 619
Cdd:PRK11147 436 TPVK----ALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
579-662 |
1.02e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.63 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 579 TQVGERGLklsgGEKQRVAIARAILKNTPILIFDEATSSL-DSITEH--NILQALtRAtSGRTSICIAHRLSTV-KDADE 654
Cdd:NF040905 135 TLVTDIGV----GKQQLVEIAKALSKDVKLLILDEPTAALnEEDSAAllDLLLEL-KA-QGITSIIISHKLNEIrRVADS 208
|
....*...
gi 45551502 655 ILVLENGR 662
Cdd:NF040905 209 ITVLRDGR 216
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
454-667 |
1.34e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 47.23 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 454 RNVSFEYEPGKPiFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDL----ESLRKVIA- 528
Cdd:PRK11701 10 RGLTKLYGPRKG-CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLyalsEAERRRLLr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 529 ----VV---PQDSVLFHNTIEHNI----------HYGNLSKSHA----EVQ-NAARMADLhdsimswPGQYstqvgergl 586
Cdd:PRK11701 89 tewgFVhqhPRDGLRMQVSAGGNIgerlmavgarHYGDIRATAGdwleRVEiDAARIDDL-------PTTF--------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 587 klSGGEKQRVAIARAiLKNTPILIF-DEATSSLDSITEHNILQALTRATS--GRTSICIAHRLSTVKD-ADEILVLENGR 662
Cdd:PRK11701 153 --SGGMQQRLQIARN-LVTHPRLVFmDEPTGGLDVSVQARLLDLLRGLVRelGLAVVIVTHDLAVARLlAHRLLVMKQGR 229
|
....*
gi 45551502 663 VGERG 667
Cdd:PRK11701 230 VVESG 234
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
123-390 |
1.47e-05 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 47.46 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 123 RVGISLGLLAGSKLLTVCVPFLFKGAVDTmTTLNMDTapdAVLSAATALMLGYGIArasAAGFNELRNAVFAKVAHHSIR 202
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLIKIAIDE-YIPNGDL---SGLLIIALLFLALNLV---NWVASRLRIYLMAKVGQRILY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 203 KIASNVFLHLHNLDLAFHLNKQTGalsKTIdrgSRGINFV------LSAMVFNIVPTIFELALVSSI---LGVKCGL-AF 272
Cdd:cd18545 74 DLRQDLFSHLQKLSFSFFDSRPVG---KIL---SRVINDVnslsdlLSNGLINLIPDLLTLVGIVIImfsLNVRLALvTL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 273 AGVSMGCVGIYAaytlsvtqWRTQFR-VFMNQ-----------AENEAGNKavdslinyeTVKYFNNEKYEAGCYNEVLK 340
Cdd:cd18545 148 AVLPLLVLVVFL--------LRRRARkAWQRVrkkisnlnaylHESISGIR---------VIQSFAREDENEEIFDELNR 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 45551502 341 KYEAASLKTSSSLALLNFGQNAIFSSALSLIMVLAAKEIAQGNMTVGDLV 390
Cdd:cd18545 211 ENRKANMRAVRLNALFWPLVELISALGTALVYWYGGKLVLGGAITVGVLV 260
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
451-675 |
2.93e-05 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 45.60 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEpGKPIFRDLSFTIPAGKNVAIvggsgsgkssmvrllfrfFEPN-SGKvliggqdisavdlESLRKVIAV 529
Cdd:cd03217 1 LEIKDLHVSVG-GKEILKGVNLTIKKGEVHAL------------------MGPNgSGK-------------STLAKTIMG 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 530 VPQDSVlfhntIEHNIHYGNLSKSHAEVQNAARMADLhdsiMSWpgQYSTQVgeRGLKL-----------SGGEKQRVAI 598
Cdd:cd03217 49 HPKYEV-----TEGEILFKGEDITDLPPEERARLGIF----LAF--QYPPEI--PGVKNadflryvnegfSGGEKKRNEI 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 599 ARAILKNTPILIFDEATSSLDSITEHNILQALTR-ATSGRTSICIAH--RLSTVKDADEILVLENGRVGERGThSELLRQ 675
Cdd:cd03217 116 LQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD-KELALE 194
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
466-674 |
4.15e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 45.97 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 466 IFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFF----EPN----SGKVLIGGQDISAVDLESLRKVIAVVPQDSV-L 536
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggAPRgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQpA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 537 FHNTIEHNIHYGNLSKSHAEVQNAARMADLHDSIMSWPGQySTQVGERGLKLSGGEKQRVAIARAILKNTP--------- 607
Cdd:PRK13547 96 FAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGA-TALVGRDVTTLSGGELARVQFARVLAQLWPphdaaqppr 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 608 ILIFDEATSSLDSITEHNILQALTRATS--GRTSICIAHRLS-TVKDADEILVLENGRVGERGTHSELLR 674
Cdd:PRK13547 175 YLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNlAARHADRIAMLADGAIVAHGAPADVLT 244
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
580-658 |
4.34e-05 |
|
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: 45.68 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 580 QVGERGLKLSGGEKQRVAIARAILKNTP---ILIFDEATSSLDSITEHNILQALTRATS-GRTSICIAHRLSTVKDADEI 655
Cdd:cd03271 162 KLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNLDVIKCADWI 241
|
...
gi 45551502 656 LVL 658
Cdd:cd03271 242 IDL 244
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
507-620 |
5.00e-05 |
|
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: 45.48 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 507 KVLIGGQDISAVDLESLRKVIAVVPQD-SVLFHNTIEHNIH-----YGNLSKSHAEVQNAARMADLHDSimswpgqystQ 580
Cdd:cd03237 43 KMLAGVLKPDEGDIEIELDTVSYKPQYiKADYEGTVRDLLSsitkdFYTHPYFKTEIAKPLQIEQILDR----------E 112
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 45551502 581 VGErglkLSGGEKQRVAIARAILKNTPILIFDEATSSLDS 620
Cdd:cd03237 113 VPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
580-658 |
9.56e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.77 E-value: 9.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 580 QVGERGLKLSGGEKQRVAIARAILKNT---PILIFDEATSSL---DSITEHNILQALTRAtsGRTSICIAHRLSTVKDAD 653
Cdd:TIGR00630 822 RLGQPATTLSGGEAQRIKLAKELSKRStgrTLYILDEPTTGLhfdDIKKLLEVLQRLVDK--GNTVVVIEHNLDVIKTAD 899
|
....*
gi 45551502 654 EILVL 658
Cdd:TIGR00630 900 YIIDL 904
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
451-661 |
1.22e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.16 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSfEYEPGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKV-IAV 529
Cdd:PRK09700 6 ISMAGIG-KSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 530 VPQD-SVLFHNTIEHNIHYGNLSK---------SHAEVQNAARM----ADLHDSImswpgqySTQVGErglkLSGGEKQR 595
Cdd:PRK09700 85 IYQElSVIDELTVLENLYIGRHLTkkvcgvniiDWREMRVRAAMmllrVGLKVDL-------DEKVAN----LSISHKQM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45551502 596 VAIARAILKNTPILIFDEATSSLDSiTEHNILQALTRA--TSGRTSICIAHRLSTVKD-ADEILVLENG 661
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSLTN-KEVDYLFLIMNQlrKEGTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
136-416 |
1.50e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 44.42 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 136 LLTVCVPFLFKGAVDTMTTLNMDTAPDAVLSAATALMLGYGIarasaagFNELRNAVFAKVAHHSIRKIASNVFLHLHNL 215
Cdd:cd18555 16 LLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGL-------FSFLRGYIIIKLQTKLDKSLMSDFFEHLLKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 216 DLAFHLNKQTGAL-----SKTIDRG---SRGINFVLSAMVfniVPTIFELALVSSILgvkcglaFAGVSMGCVGIYAAYT 287
Cdd:cd18555 89 PYSFFENRSSGDLlfranSNVYIRQilsNQVISLIIDLLL---LVIYLIYMLYYSPL-------LTLIVLLLGLLIVLLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 288 LsVTQWRTQFrvfMNQAENEAGNKA----VDSLINYETVKYFNNEKYeagCYNEVLKKYE---AASLKTSSSLALLNFGQ 360
Cdd:cd18555 159 L-LTRKKIKK---LNQEEIVAQTKVqsylTETLYGIETIKSLGSEKN---IYKKWENLFKkqlKAFKKKERLSNILNSIS 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 45551502 361 NAIFSSALSLIMVLAAKEIAQGNMTVGDLVMVNALLFQLSIPLGFLGSVYREVRQA 416
Cdd:cd18555 232 SSIQFIAPLLILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILL 287
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
467-664 |
1.52e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 45.04 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 467 FRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVD-LESLRKVIAVVPQD---SVLFHNT-I 541
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStAQRLARGLVYLPEDrqsSGLYLDApL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 542 EHNI---HYGNLSKSHAEVQNAARMADLHDSImswpGQYSTQVGERGLKLSGGEKQRVAIARAILKNTPILIFDEATSSL 618
Cdd:PRK15439 359 AWNVcalTHNRRGFWIKPARENAVLERYRRAL----NIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 45551502 619 DSITEHNILQALTR-ATSGRTSICIAHRLSTV-KDADEILVLENGRVG 664
Cdd:PRK15439 435 DVSARNDIYQLIRSiAAQNVAVLFISSDLEEIeQMADRVLVMHQGEIS 482
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
455-637 |
1.59e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 43.40 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 455 NVSFEYEpGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAvDLESLRKVIAVVPQDS 534
Cdd:PRK13540 6 ELDFDYH-DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHRS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 535 VLFHN-TIEHNIHYG-NLSKSHAEVQNAARMADLhDSIMSWPGqystqvgerGLkLSGGEKQRVAIARAILKNTPILIFD 612
Cdd:PRK13540 84 GINPYlTLRENCLYDiHFSPGAVGITELCRLFSL-EHLIDYPC---------GL-LSSGQKRQVALLRLWMSKAKLWLLD 152
|
170 180
....*....|....*....|....*
gi 45551502 613 EATSSLDsitEHNILQALTRATSGR 637
Cdd:PRK13540 153 EPLVALD---ELSLLTIITKIQEHR 174
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
588-668 |
1.62e-04 |
|
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: 44.78 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 588 LSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTRAT--SGRTSICIAHRLSTVkD--ADEILVLEnGRV 663
Cdd:COG1245 456 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAenRGKTAMVVDHDIYLI-DyiSDRLMVFE-GEP 533
|
....*
gi 45551502 664 GERGT 668
Cdd:COG1245 534 GVHGH 538
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
562-656 |
1.66e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 42.73 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 562 RMADLHDSIMSWPGQYSTQV-----GERgLKLSGGEKQRVAIARAI----LKNTPILIFDEATSSLDSITEHNILQALTR 632
Cdd:cd03227 48 AQSATRRRSGVKAGCIVAAVsaeliFTR-LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILE 126
|
90 100
....*....|....*....|....*
gi 45551502 633 -ATSGRTSICIAHRLSTVKDADEIL 656
Cdd:cd03227 127 hLVKGAQVIVITHLPELAELADKLI 151
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
451-663 |
1.85e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYePGKPI-FRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVL--------------IGGQDI 515
Cdd:PLN03073 509 ISFSDASFGY-PGGPLlFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFrsakvrmavfsqhhVDGLDL 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 516 SAVDLESLRKVIAVVPQDSVlfhntiehNIHYGNLSKShaevQNAARMAdlhdsimswpgQYStqvgerglkLSGGEKQR 595
Cdd:PLN03073 588 SSNPLLYMMRCFPGVPEQKL--------RAHLGSFGVT----GNLALQP-----------MYT---------LSGGQKSR 635
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45551502 596 VAIARAILKNTPILIFDEATSSLDSITEHNILQALTRATSGrtsICIA----HRLStvKDADEILVLENGRV 663
Cdd:PLN03073 636 VAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGG---VLMVshdeHLIS--GSVDELWVVSEGKV 702
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
587-619 |
2.10e-04 |
|
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: 44.54 E-value: 2.10e-04
10 20 30
....*....|....*....|....*....|...
gi 45551502 587 KLSGGEKQRVAIARAILKNTPILIFDEATSSLD 619
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
395-650 |
2.19e-04 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 44.74 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 395 LLFQLSIPLGFLGSVYREVRQaLLDMRA-MFTLMNV----------------DSSIQTAANAQPLF-----VDTTNSSIE 452
Cdd:TIGR00954 375 LLLKAADALGRLMLAGRDMTR-LAGFTArVDTLLQVlddvksgnfkrprveeIESGREGGRNSNLVpgrgiVEYQDNGIK 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 453 FRNVSFEYEPGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLF--------RFFEPNSGKVLIGGQDiSAVDLESLR 524
Cdd:TIGR00954 454 FENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKLFYVPQR-PYMTLGTLR 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 525 kviavvpqDSVLFHNTIEHNIHYGnlsKSHAEVQNAARMADLHDsIMSWPGQYSTqVGERGLKLSGGEKQRVAIARAILK 604
Cdd:TIGR00954 533 --------DQIIYPDSSEDMKRRG---LSDKDLEQILDNVQLTH-ILEREGGWSA-VQDWMDVLSGGEKQRIAMARLFYH 599
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 45551502 605 NTPILIFDEATSSLDSITEHNILQALTRAtsGRTSICIAHRLSTVK 650
Cdd:TIGR00954 600 KPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKSLWK 643
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
451-663 |
2.82e-04 |
|
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: 42.90 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYE---------------------PGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVL 509
Cdd:cd03220 1 IELENVSKSYPtykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 510 IGGQDISAVDLeslrkviavvpqdSVLFHN--TIEHNIHYGNLSKSHAEVQNAARMADLHDsiMSWPGQY-STQVGErgl 586
Cdd:cd03220 81 VRGRVSSLLGL-------------GGGFNPelTGRENIYLNGRLLGLSRKEIDEKIDEIIE--FSELGDFiDLPVKT--- 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45551502 587 kLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALT-RATSGRTSICIAHRLSTVKD-ADEILVLENGRV 663
Cdd:cd03220 143 -YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLReLLKQGKTVILVSHDPSSIKRlCDRALVLEKGKI 220
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
126-406 |
3.01e-04 |
|
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and similar proteins; This group includes the 6-TMD of an uncharacterized peptidase-containing ABC transporter of T1SS (type 1 secretion systems), similar to heterocyst differentiation protein HetC. HetC 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: 350015 [Multi-domain] Cd Length: 294 Bit Score: 43.20 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 126 ISLGLLAGSkLLTVCVPFLFKGAVDT---MTTLNMDTApdaVLSAATALMLGYgiaraSAAGFneLRNAVFAKVahhSIR 202
Cdd:cd18571 7 LLLGLLLGS-LLQLIFPFLTQSIVDKginNKDLNFIYL---ILIAQLVLFLGS-----TSIEF--IRSWILLHI---SSR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 203 ---KIASNVFLHLHNLDLAFHLNKQTGALSKTIDRGSR--------GINFVLSAM---VFNIV-----PTIFELALVSSI 263
Cdd:cd18571 73 iniSIISDFLIKLMRLPISFFDTKMTGDILQRINDHSRiesfltssSLSILFSLLnliVFSIVlayynLTIFLIFLIGSV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 264 LgvkcglafagvsmgcvgiYAAYTLSVTQWRTQ--FRVFMNQAENEagNKAVDSLINYETVKYFNNEKYEAGCYnevlKK 341
Cdd:cd18571 153 L------------------YILWILLFLKKRKKldYKRFDLSSENQ--SKLIELINGMQEIKLNNSERQKRWEW----ER 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45551502 342 YEAASLKTSSSLALLN----FGQNAIFSSALSLIMVLAAKEIAQGNMTVGDLVMVNALLFQLSIPLGFL 406
Cdd:cd18571 209 IQAKLFKINIKSLKLDqyqqIGALFINQLKNILITFLAAKLVIDGEITLGMMLAIQYIIGQLNSPIEQL 277
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
126-409 |
3.35e-04 |
|
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: 43.17 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 126 ISLGLLAGSKLLTVCVPFLFKGAVDTMTTLNMDTAPDAVLSAAT-ALMLGYGIAR---------ASAAGFNELRNAVFAk 195
Cdd:cd18541 3 LGILFLILVDLLQLLIPRIIGRAIDALTAGTLTASQLLRYALLIlLLALLIGIFRflwrylifgASRRIEYDLRNDLFA- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 196 vahhsirkiasnvflHLHNLDLAFHLNKQTGALSktidrgSRGIN------FVLSAMVFNIVPTIF-------------- 255
Cdd:cd18541 82 ---------------HLLTLSPSFYQKNRTGDLM------ARATNdlnavrMALGPGILYLVDALFlgvlvlvmmftisp 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 256 ELALVSSILgvkcgLAFAGVSMGCVG--IYAAYTLSvtqwRTQFRVFMNQA-ENEAGNKavdslinyeTVKYFNNEKYEA 332
Cdd:cd18541 141 KLTLIALLP-----LPLLALLVYRLGkkIHKRFRKV----QEAFSDLSDRVqESFSGIR---------VIKAFVQEEAEI 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 333 GCYNEVLKKYEAASLKtsssLALLN--FGQNAIFSSALSLIMVLA--AKEIAQGNMTVGDLVMVNALLFQLSIPLGFLGS 408
Cdd:cd18541 203 ERFDKLNEEYVEKNLR----LARVDalFFPLIGLLIGLSFLIVLWygGRLVIRGTITLGDLVAFNSYLGMLIWPMMALGW 278
|
.
gi 45551502 409 V 409
Cdd:cd18541 279 V 279
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
427-665 |
3.68e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 43.62 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 427 MNVDSSIQTAANAQPLFVDTTNSSI--EFRNVSfEYEPGKpiFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPN 504
Cdd:PRK09700 240 LMVGRELQNRFNAMKENVSNLAHETvfEVRNVT-SRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 505 SGKVLIGGQDIS-AVDLESLRKVIAVVPQ---DSVLFHN-TIEHNIHYGN------------LSKSHAEVQNAARMADLH 567
Cdd:PRK09700 317 GGEIRLNGKDISpRSPLDAVKKGMAYITEsrrDNGFFPNfSIAQNMAISRslkdggykgamgLFHEVDEQRTAENQRELL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 568 DSIMSWPGQYSTQvgerglkLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTR-ATSGRTSICIAHRL 646
Cdd:PRK09700 397 ALKCHSVNQNITE-------LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSEL 469
|
250 260
....*....|....*....|
gi 45551502 647 STVKDA-DEILVLENGRVGE 665
Cdd:PRK09700 470 PEIITVcDRIAVFCEGRLTQ 489
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
556-661 |
3.69e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.07 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 556 EVQNAARMADLHDSIMSWPGQYStqvgerglkLSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALtRAT- 634
Cdd:PLN03140 997 EVMELVELDNLKDAIVGLPGVTG---------LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTV-RNTv 1066
|
90 100 110
....*....|....*....|....*....|
gi 45551502 635 -SGRTSICIAHRLS--TVKDADEILVLENG 661
Cdd:PLN03140 1067 dTGRTVVCTIHQPSidIFEAFDELLLMKRG 1096
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
170-397 |
4.20e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 43.21 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 170 ALM-LGYGIArASAAGFneLRNAVFAKVAHHSIRKIASNVFLHLHNLDLAFHLNKQ--TGALSKTIDRGSRGINFVLSAM 246
Cdd:cd18578 55 ALMfLVLAIV-AGIAYF--LQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDDPEnsTGALTSRLSTDASDVRGLVGDR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 247 VFNIVPTIFELAL---VSSILGVK---CGLAFAGVSMGCVGIYAAYTlsvtqwrTQFRVFMNQAENEAGNKAVDSLINYE 320
Cdd:cd18578 132 LGLILQAIVTLVAgliIAFVYGWKlalVGLATVPLLLLAGYLRMRLL-------SGFEEKNKKAYEESSKIASEAVSNIR 204
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45551502 321 TVKYFNNEKYEAGCYNEVLKKYEAASLKTSSSLALLNFGQNAIFSSALSLIMVLAAKEIAQGNMTVGDLVMV-NALLF 397
Cdd:cd18578 205 TVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVfMALIF 282
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
588-664 |
4.41e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 588 LSGGEKQRVAIARAIL---KNTPILIFDEATSSLDSITEHNILQALTRAT-SGRTSICIAHRLSTVKDADEILVL--ENG 661
Cdd:PRK00635 810 LSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLQSLThQGHTVVIIEHNMHVVKVADYVLELgpEGG 889
|
...
gi 45551502 662 RVG 664
Cdd:PRK00635 890 NLG 892
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
451-633 |
5.32e-04 |
|
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: 43.39 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEpGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGgqdiSAVDLeslrkviAVV 530
Cdd:TIGR03719 323 IEAENLTKAFG-DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG----ETVKL-------AYV 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 531 PQ--DSVLFHNTIEHNIHYGNlskSHAEVQNAARMADLHDSIMSWPGQYSTQ-VGErglkLSGGEKQRVAIARAILKNTP 607
Cdd:TIGR03719 391 DQsrDALDPNKTVWEEISGGL---DIIKLGKREIPSRAYVGRFNFKGSDQQKkVGQ----LSGGERNRVHLAKTLKSGGN 463
|
170 180
....*....|....*....|....*.
gi 45551502 608 ILIFDEATSSLDSITehniLQALTRA 633
Cdd:TIGR03719 464 VLLLDEPTNDLDVET----LRALEEA 485
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
587-619 |
6.30e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.80 E-value: 6.30e-04
10 20 30
....*....|....*....|....*....|...
gi 45551502 587 KLSGGEKQRVAIARAILKNTPILIFDEATSSLD 619
Cdd:PRK11819 163 KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
587-619 |
6.85e-04 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 42.02 E-value: 6.85e-04
10 20 30
....*....|....*....|....*....|...
gi 45551502 587 KLSGGEKQRVAIARAILKNTPILIFDEATSSLD 619
Cdd:PRK09544 120 KLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
581-661 |
8.08e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.79 E-value: 8.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 581 VGERGLKLSGGEKQRVAIARAILKNTPILIF-DEATSSLDSITEHNILQALTR-ATSGRTSICIAHRLSTV--KDADEIL 656
Cdd:TIGR00956 895 VGVPGEGLNVEQRKRLTIGVELVAKPKLLLFlDEPTSGLDSQTAWSICKLMRKlADHGQAILCTIHQPSAIlfEEFDRLL 974
|
....*
gi 45551502 657 VLENG 661
Cdd:TIGR00956 975 LLQKG 979
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
588-665 |
1.33e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.91 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 588 LSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTR-ATSGRTSICIAHRLSTVKD-ADEILVLENGRV-G 664
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQfKAEGLSIILVSSEMPEVLGmSDRILVMHEGRIsG 475
|
.
gi 45551502 665 E 665
Cdd:PRK10762 476 E 476
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
588-619 |
1.66e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 41.72 E-value: 1.66e-03
10 20 30
....*....|....*....|....*....|..
gi 45551502 588 LSGGEKQRVAIARAILKNTPILIFDEATSSLD 619
Cdd:PRK13409 454 LSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
588-653 |
1.71e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.54 E-value: 1.71e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45551502 588 LSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQAL-TRATSGRTSI------------CIAHRLSTVKDAD 653
Cdd:PRK10938 402 LSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVdVLISEGETQLlfvshhaedapaCITHRLEFVPDGD 480
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
164-416 |
1.73e-03 |
|
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: 40.93 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 164 VLSAATALMLGYGIARASAAGFNE-----LRNAVFA--------------------KVAHHSIRKIASNVFLHLHNLDLA 218
Cdd:cd18575 6 LIAAAATLALGQGLRLLIDQGFAAgntalLNRAFLLllavalvlalasalrfylvsWLGERVVADLRKAVFAHLLRLSPS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 219 FHLNKQTG-ALSK-TIDrgsrginfvlSAMVFNIVPTIFELALVSSILGVKcGLAF--------AGVSMGCV-------G 281
Cdd:cd18575 86 FFETTRTGeVLSRlTTD----------TTLIQTVVGSSLSIALRNLLLLIG-GLVMlfitspklTLLVLLVIplvvlpiI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 282 IYAAY--TLSVtqwRTQFRVfmnqaeNEAGNKAVDSLINYETVKYFNNEKYEAGCYNEVLKKYEAASLKTSSSLALLNFG 359
Cdd:cd18575 155 LFGRRvrRLSR---ASQDRL------ADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTAL 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 45551502 360 QNAIFSSALSLIMVLAAKEIAQGNMTVGDLV--MVNALLFQLSipLGFLGSVYREVRQA 416
Cdd:cd18575 226 VIFLVFGAIVFVLWLGAHDVLAGRMSAGELSqfVFYAVLAAGS--VGALSEVWGDLQRA 282
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
462-676 |
2.69e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 41.07 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 462 PGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFE-PNSGKVLIGGQDISAVD-LESLRKVIAVVPQD------ 533
Cdd:PRK13549 273 PHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNpQQAIAQGIAMVPEDrkrdgi 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 534 -SVLfhnTIEHNIHYGNLSK--SHAEVQNAARMADLHDSIMSWPGQYST---QVGerglKLSGGEKQRVAIARAILKNTP 607
Cdd:PRK13549 353 vPVM---GVGKNITLAALDRftGGSRIDDAAELKTILESIQRLKVKTASpelAIA----RLSGGNQQKAVLAKCLLLNPK 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45551502 608 ILIFDEATSSLDSITEHNILQALTR-ATSGRTSICIAHRLSTVKD-ADEILVLENGRVgeRGthsELLRQN 676
Cdd:PRK13549 426 ILILDEPTRGIDVGAKYEIYKLINQlVQQGVAIIVISSELPEVLGlSDRVLVMHEGKL--KG---DLINHN 491
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
270-420 |
2.75e-03 |
|
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: 40.24 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 270 LAFAGVSMGCVGIYAAYTLSVTQW--RTQFRVFmnQAENEAGNKAVDSLINYETVKYFNNEkyeagcyNEVLKKYEA--- 344
Cdd:cd18568 141 LQLTLIVLAFIPLYVLLTLLSSPKlkRNSREIF--QANAEQQSFLVEALTGIATIKALAAE-------RPIRWRWENkfa 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 345 ----ASLKTSSSLALLNFGQNAIFSSALSLIMVLAAKEIAQGNMTVGDLVMVNALLFQLSIPLGFLGSVYREVRQALLDM 420
Cdd:cd18568 212 kalnTRFRGQKLSIVLQLISSLINHLGTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISV 291
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
576-682 |
2.92e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.77 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 576 QYSTQVG-----ERGLK-LSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNILQALTR-ATSGRTSICIAHRLST 648
Cdd:PRK10938 118 QLAQQFGitallDRRFKyLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASlHQSGITLVLVLNRFDE 197
|
90 100 110
....*....|....*....|....*....|....*
gi 45551502 649 VKD-ADEILVLENGRVGERGTHSELLRQnGLYARL 682
Cdd:PRK10938 198 IPDfVQFAGVLADCTLAETGEREEILQQ-ALVAQL 231
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
588-656 |
4.27e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.13 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 588 LSGGEKQ------RVAIARAILKNTPILIFDEATSSLDsitEHNILQALTRATSGRTS------ICIAHRLSTVKDADEI 655
Cdd:cd03240 116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLD---EENIEESLAEIIEERKSqknfqlIVITHDEELVDAADHI 192
|
.
gi 45551502 656 L 656
Cdd:cd03240 193 Y 193
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
505-619 |
5.29e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.77 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 505 SGKVLIGGQ--DISAVDlESLRKVIAVVPQDS-----VLfHNTIEHNIHYGNLSK--------SHAEVQNAARM-ADLHd 568
Cdd:NF040905 316 SGTVFKDGKevDVSTVS-DAIDAGLAYVTEDRkgyglNL-IDDIKRNITLANLGKvsrrgvidENEEIKVAEEYrKKMN- 392
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 45551502 569 sIMSwPGqystqVGERGLKLSGGEKQRVAIARAILKNTPILIFDEATSSLD 619
Cdd:NF040905 393 -IKT-PS-----VFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
579-666 |
5.81e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 39.99 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 579 TQVGErglkLSGGEKQRVAIARAILKNTPILIFDEATSSL-DSITEH--NILQALtRAtSGRTSICIAHRLSTVKD-ADE 654
Cdd:PRK10762 137 KLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESlfRVIREL-KS-QGRGIVYISHRLKEIFEiCDD 210
|
90
....*....|...
gi 45551502 655 ILVLENGR-VGER 666
Cdd:PRK10762 211 VTVFRDGQfIAER 223
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
465-619 |
6.28e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 38.68 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 465 PIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVIAVVP---QDSvlfhNTI 541
Cdd:PRK13543 25 PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPglkADL----STL 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45551502 542 EhNIHYGN-LSKSHAEvqnaaRMADLHDSIMSWPGQYSTQVGErglkLSGGEKQRVAIARAILKNTPILIFDEATSSLD 619
Cdd:PRK13543 101 E-NLHFLCgLHGRRAK-----QMPGSALAIVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
463-619 |
6.71e-03 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 38.63 E-value: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 463 GKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKVI------AVvpqDSVL 536
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLylghqpGI---KTEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 537 fhnTIEHNIHYgnlskshaevqnAARMADLHDSIMSWpgQYSTQVGERGLK------LSGGEKQRVAIARAILKNTPILI 610
Cdd:PRK13538 90 ---TALENLRF------------YQRLHGPGDDEALW--EALAQVGLAGFEdvpvrqLSAGQQRRVALARLWLTRAPLWI 152
|
....*....
gi 45551502 611 FDEATSSLD 619
Cdd:PRK13538 153 LDEPFTAID 161
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
451-678 |
7.11e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.49 E-value: 7.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 451 IEFRNVSFEYEpGKPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSGKVLIggqdisavdleSLRKVIAVV 530
Cdd:PRK15064 320 LEVENLTKGFD-NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW-----------SENANIGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 531 PQDSVlfhntiehnihygnlskshAEVQNaarmaDLhdSIMSWPGQYsTQVGE-----RGL----------------KLS 589
Cdd:PRK15064 388 AQDHA-------------------YDFEN-----DL--TLFDWMSQW-RQEGDdeqavRGTlgrllfsqddikksvkVLS 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 590 GGEKQRVAIARAILKNTPILIFDEATSSLD--SITEHNIlqALTRATSgrTSICIAHRLSTVKD-ADEIL-VLENGRVGE 665
Cdd:PRK15064 441 GGEKGRMLFGKLMMQKPNVLVMDEPTNHMDmeSIESLNM--ALEKYEG--TLIFVSHDREFVSSlATRIIeITPDGVVDF 516
|
250
....*....|...
gi 45551502 666 RGTHSELLRQNGL 678
Cdd:PRK15064 517 SGTYEEYLRSQGI 529
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
452-666 |
8.96e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 39.24 E-value: 8.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 452 EFRNVSFEYEPGKPIFRDLSFTIPAGKNVAIVggsgsgkssMVRLLFRFFEPNSGKVLIGGQDISAVDLESLRKV-IAVV 530
Cdd:COG3845 259 EVENLSVRDDRGVPALKDVSLEVRAGEILGIAgvagngqseLAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 531 PQD-----SVLfHNTIEHNI---HYGNLSKSHAEVQNAARMADLHDSIMSwpgQYSTQVGERGLK---LSGGEKQRVAIA 599
Cdd:COG3845 339 PEDrlgrgLVP-DMSVAENLilgRYRRPPFSRGGFLDRKAIRAFAEELIE---EFDVRTPGPDTParsLSGGNQQKVILA 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45551502 600 RAILKNTPILIFDEATSSLD--SITE-HNILQALTRAtsGRTSICIahrlSTVKD-----ADEILVLENGR-VGER 666
Cdd:COG3845 415 RELSRDPKLLIAAQPTRGLDvgAIEFiHQRLLELRDA--GAAVLLI----SEDLDeilalSDRIAVMYEGRiVGEV 484
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
579-673 |
9.00e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 39.44 E-value: 9.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 579 TQVGERGLK-LSGGEKQRVAIARAILKNTPILIFDEATSSLDSITEHNI---LQALTRATSGRTSICIAHRLSTVKDA-D 653
Cdd:PLN03140 327 TIVGDEMIRgISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIvkcLQQIVHLTEATVLMSLLQPAPETFDLfD 406
|
90 100
....*....|....*....|
gi 45551502 654 EILVLENGRVGERGTHSELL 673
Cdd:PLN03140 407 DIILLSEGQIVYQGPRDHIL 426
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
589-668 |
9.40e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 38.47 E-value: 9.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 589 SGGEKQRVAIARAILKNTPILIFDEATSSLD-----SITEH-NILqaltrATSGRTSICIAH--RLSTVKDADEILVLEN 660
Cdd:CHL00131 153 SGGEKKRNEILQMALLDSELAILDETDSGLDidalkIIAEGiNKL-----MTSENSIILITHyqRLLDYIKPDYVHVMQN 227
|
....*...
gi 45551502 661 GRVGERGT 668
Cdd:CHL00131 228 GKIIKTGD 235
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
448-668 |
9.81e-03 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 38.52 E-value: 9.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 448 NSSIEFRNVSFEYEPG---------------------KPIFRDLSFTIPAGKNVAIVGGSGSGKSSMVRLLFRFFEPNSG 506
Cdd:COG1134 2 SSMIEVENVSKSYRLYhepsrslkelllrrrrtrreeFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 507 KVLIGGQdISAvdleslrkVIAVvpqdSVLFHN--TIEHNIHYG----NLSKshAEVQnaARM------ADLHDSIMSwP 574
Cdd:COG1134 82 RVEVNGR-VSA--------LLEL----GAGFHPelTGRENIYLNgrllGLSR--KEID--EKFdeivefAELGDFIDQ-P 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551502 575 -GQYSTqvgerglklsgGEKQRVAIARAILKNTPILIFDEATS---------SLDSITEhnilqaltRATSGRTSICIAH 644
Cdd:COG1134 144 vKTYSS-----------GMRARLAFAVATAVDPDILLVDEVLAvgdaafqkkCLARIRE--------LRESGRTVIFVSH 204
|
250 260
....*....|....*....|....*
gi 45551502 645 RLSTVKD-ADEILVLENGRVGERGT 668
Cdd:COG1134 205 SMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| |
