|
Name |
Accession |
Description |
Interval |
E-value |
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
12-575 |
0e+00 |
|
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: 715.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 12 QQPLRAFLKQQSKPAAMWLKLSIALGTVNAILMIAGAYLLAQTIHEVMFEGRNLAQVTQYLWPLAGIILLRALFLALSER 91
Cdd:COG4988 1 QKPLDKRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPLSALLPLLGLLLAVLLLRALLAWLRER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 92 LSAFATLKIKSAIRQTLLDKLTQLGPSYIEKNGQGATLNTLHNGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKA 171
Cdd:COG4988 81 AAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 172 GLIFLLTAPLIPFFMILVGHKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATRKELKQIARISDDFRHATLNVLKI 251
Cdd:COG4988 161 GLILLVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKVLRV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 252 AFLSSFALEFLATISVALVAVIIGFRLFFGTLDFATGFVVLLLAPEFYLPLRQLGSHYHARLQGISAAADMLIILNAPLP 331
Cdd:COG4988 241 AFLSSAVLEFFASLSIALVAVYIGFRLLGGSLTLFAALFVLLLAPEFFLPLRDLGSFYHARANGIAAAEKIFALLDAPEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 332 ENDDSHTAnINIDANNTISIHDLNFSYPNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQ 411
Cdd:COG4988 321 AAPAGTAP-LPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 412 PLTTANISQLQQSIAWIPQKPTLFYDTLAANIKLGNPSASHEALEHAAKQAGALEFINELPDGFNTLIGEQGEGLSGGQK 491
Cdd:COG4988 400 DLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 492 QRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIAHRLNTVKNAKQLIVMENGCIVQQGDFKALS 571
Cdd:COG4988 480 QRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELL 559
|
....
gi 1590405536 572 QQSG 575
Cdd:COG4988 560 AKNG 563
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
26-556 |
0e+00 |
|
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: 584.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 26 AAMWLKLSIALGTVNAILMIAGAYLLAQTIHEVMFEGRNLAQVTQYLWPLAGIILLRALFLALSERLSAFATLKIKSAIR 105
Cdd:TIGR02857 1 ARRALALLALLGVLGALLIIAQAWLLARVVDGLISAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 106 QTLLDKLTQLGPSYIEKNGQGATLNTLHNGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFF 185
Cdd:TIGR02857 81 ERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIPIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 186 MILVGHKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATRKELKQIARISDDFRHATLNVLKIAFLSSFALEFLATI 265
Cdd:TIGR02857 161 MILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLELFATL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 266 SVALVAVIIGFRLFFGTLDFATGFVVLLLAPEFYLPLRQLGSHYHARLQGISAAADMLIILNA-PLPENDDshtANINID 344
Cdd:TIGR02857 241 SVALVAVYIGFRLLAGDLDLATGLFVLLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAaPRPLAGK---APVTAA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 345 ANNTISIHDLNFSYPNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQS 424
Cdd:TIGR02857 318 PASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 425 IAWIPQKPTLFYDTLAANIKLGNPSASHEALEHAAKQAGALEFINELPDGFNTLIGEQGEGLSGGQKQRIALARAFLKHA 504
Cdd:TIGR02857 398 IAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDA 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1590405536 505 PILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIAHRLNTVKNAKQLIVM 556
Cdd:TIGR02857 478 PLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
8-586 |
0e+00 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 566.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 8 NRAQQQPLRAFLKQQSKPAAMWLKLSIALGTVNAILMIAGAYLLAQTIHEVMFEGRNLAQVTQYLWPLAGIILLRALFLA 87
Cdd:PRK11174 2 DKSRQKELTRWLKQQSKPAKRWLNLSILLGFLSGLLLIAQAWLLATILQALIIENIPREALLPPFILLILLFVLRALLAW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 88 LSERLSAFATLKIKSAIRQTLLDKLTQLGPSYIEK--NGQGATLntLHNGVEALHDYYAKYLPGVAYSALIPLAILVVIF 165
Cdd:PRK11174 82 LRERVGFKAGQHIRQQIRQQVLDKLQQLGPAWIQGkpAGSWATL--VLEQVEDMHDFYARYLPQMALAVLVPLLILIAVF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 166 PTDYKAGLIFLLTAPLIPFFMILVGHKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATRKELKQIARISDDFRHAT 245
Cdd:PRK11174 160 PINWAAGLILLGTAPLIPLFMALVGMGAADANRRNFLALARLSGHFLDRLRGLETLRLFNRGEAETESIRSASEDFRQRT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 246 LNVLKIAFLSSFALEFLATISVALVAVIIGFRlFFGTLDFA---------TGFVVLLLAPEFYLPLRQLGSHYHARLQGI 316
Cdd:PRK11174 240 MEVLRMAFLSSAVLEFFASISIALVAVYFGFS-YLGELNFGhygtgvtlfAGFFVLILAPEFYQPLRDLGTFYHAKAQAV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 317 SAAADMLIILNAPLPENDDShTANINIDANNTISIHDLNFSYPNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCML 396
Cdd:PRK11174 319 GAAESLVTFLETPLAHPQQG-EKELASNDPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 397 GFHPevIQ-HISIDQQPLTTANISQLQQSIAWIPQKPTLFYDTLAANIKLGNPSASHEALEHAAKQAGALEFINELPDGF 475
Cdd:PRK11174 398 GFLP--YQgSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 476 NTLIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIAHRLNTVKNAKQLIV 555
Cdd:PRK11174 476 DTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWV 555
|
570 580 590
....*....|....*....|....*....|.
gi 1590405536 556 MENGCIVQQGDFKALSQQSGEFAKLLQTAEQ 586
Cdd:PRK11174 556 MQDGQIVQQGDYAELSQAGGLFATLLAHRQE 586
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
15-586 |
8.29e-152 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 448.84 E-value: 8.29e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 15 LRAFLKQQSKPAAMWLKLSIALGTVNAILMIAGAYLLAQTIHEVmFEGRNLAQVTQYLWPLAGIILLRALFLALSERLSA 94
Cdd:COG1132 8 LLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDAL-LAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 95 FATLKIKSAIRQTLLDKLTQLGPSYIEKNGQGATLNTLHNGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLI 174
Cdd:COG1132 87 RLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 175 FLLTAPLIPFFMILVGHKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATRKELKQIARISDDFRHATLNVLKIAFL 254
Cdd:COG1132 167 VLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSAL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 255 SSFALEFLATISVALVAVIIGFRLFFGTLDFATGFVVLLLAPEFYLPLRQLGSHYHARLQGISAAADMLIILNAPlPEND 334
Cdd:COG1132 247 FFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEP-PEIP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 335 DSHTANINIDANNTISIHDLNFSYPNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHpEVIQ-HISIDQQPL 413
Cdd:COG1132 326 DPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFY-DPTSgRILIDGVDI 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 414 TTANISQLQQSIAWIPQKPTLFYDTLAANIKLGNPSASHEALEHAAKQAGALEFINELPDGFNTLIGEQGEGLSGGQKQR 493
Cdd:COG1132 405 RDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQR 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 494 IALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIAHRLNTVKNAKQLIVMENGCIVQQGDFKALSQQ 573
Cdd:COG1132 485 IAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLAR 564
|
570
....*....|....*
gi 1590405536 574 SGEFAKL--LQTAEQ 586
Cdd:COG1132 565 GGLYARLyrLQFGEE 579
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
33-322 |
1.11e-127 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 376.36 E-value: 1.11e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 33 SIALGTVNAILMIAGAYLLAQTIHEVMFEGRNLAQVTQYLWPLAGIILLRALFLALSERLSAFATLKIKSAIRQTLLDKL 112
Cdd:cd18584 1 AVLLGLLAALLIIAQAWLLARIIAGVFLEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 113 TQLGPSYIEKNGQGATLNTLHNGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMILVGHK 192
Cdd:cd18584 81 LALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSALILLVTAPLIPLFMILIGKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 193 AEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATRKELKQIARISDDFRHATLNVLKIAFLSSFALEFLATISVALVAV 272
Cdd:cd18584 161 AQAASRRQWAALSRLSGHFLDRLRGLPTLKLFGRARAQAARIARASEDYRRRTMKVLRVAFLSSAVLEFFATLSIALVAV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1590405536 273 IIGFRLFFGTLDFATGFVVLLLAPEFYLPLRQLGSHYHARLQGISAAADM 322
Cdd:cd18584 241 YIGFRLLGGSLTLFTALFVLLLAPEFYLPLRQLGAAYHARADGLAAAERL 290
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
66-582 |
3.81e-104 |
|
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: 329.87 E-value: 3.81e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 66 AQVTQYLWPLA----GIILLRALFLALSERLSAFATLKIKSAIRQTLLDKLTQLGPSYIEKNGQGATLNTLhNGVEALHD 141
Cdd:COG2274 189 NQDLSTLWVLAigllLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIRE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 142 YYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMILVGHKAEALNQKRWQQLAVLGNYFFDRVQGLTQL 221
Cdd:COG2274 268 FLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETI 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 222 KLFNATRKELKQIARISDDFRHATLNVLKIAFLSSFALEFLATISVALVaVIIGFRLFF------GTLDFATGFVVLLLA 295
Cdd:COG2274 348 KALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVAL-LWLGAYLVIdgqltlGQLIAFNILSGRFLA 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 296 PefylpLRQLGSHYhARLQGISAAADMLI-ILNAPlPENDDSHTANINIDANNTISIHDLNFSYP-NSNEGINNINLTLP 373
Cdd:COG2274 427 P-----VAQLIGLL-QRFQDAKIALERLDdILDLP-PEREEGRSKLSLPRLKGDIELENVSFRYPgDSPPVLDNISLTIK 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 374 STGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAWIPQKPTLFYDTLAANIKLGNPSASHE 453
Cdd:COG2274 500 PGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDE 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 454 ALEHAAKQAGALEFINELPDGFNTLIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAK 533
Cdd:COG2274 580 EIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK 659
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1590405536 534 NHLVITIAHRLNTVKNAKQLIVMENGCIVQQGDFKALSQQSGEFAKLLQ 582
Cdd:COG2274 660 GRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
14-582 |
1.66e-100 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 316.32 E-value: 1.66e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 14 PLRAFLKQqSKPAAMWLKLSIALGTV----NAILMIAGAYLLAQT-IHEVMFEgrnlaqvtqYLWPLAGIillRalFLAL 88
Cdd:COG4987 2 DLLRLLRL-LRPHRGRLLLGVLLGLLtllaGIGLLALSGWLIAAAaLAPPILN---------LFVPIVGV---R--AFAI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 89 S-------ERL-SAFATLKIKSAIRQTLLDKLTQLGPSYIEKNGQGATLNTLHNGVEALHDYYAK-YLPGVAYSALIPLA 159
Cdd:COG4987 67 GrtvfrylERLvSHDATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRvLLPLLVALLVILAA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 160 ILVVIFpTDYKAGLI----FLLTAPLIPFFMILVGHKAEAlnqkRWQQL-AVLGNYFFDRVQGLTQLKLFNATRKELKQI 234
Cdd:COG4987 147 VAFLAF-FSPALALVlalgLLLAGLLLPLLAARLGRRAGR----RLAAArAALRARLTDLLQGAAELAAYGALDRALARL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 235 ARISDDFRHATLNVLKIAFLSSFALEFLATISVALVAVIIGFRLFFGTLDfATGFVVLLLAP----EFYLPLRQLGSHYH 310
Cdd:COG4987 222 DAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALS-GPLLALLVLAAlalfEALAPLPAAAQHLG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 311 arlQGISAAADMLIILNAPLPENDDSHTANIniDANNTISIHDLNFSYPNSNEGI-NNINLTLPSTGLVAIVGASGSGKS 389
Cdd:COG4987 301 ---RVRAAARRLNELLDAPPAVTEPAEPAPA--PGGPSLELEDVSFRYPGAGRPVlDGLSLTLPPGERVAIVGPSGSGKS 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 390 TLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAWIPQKPTLFYDTLAANIKLGNPSASHEALEHAAKQAGALEFIN 469
Cdd:COG4987 376 TLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLA 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 470 ELPDGFNTLIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIAHRLNTVKN 549
Cdd:COG4987 456 ALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLER 535
|
570 580 590
....*....|....*....|....*....|...
gi 1590405536 550 AKQLIVMENGCIVQQGDFKALSQQSGEFAKLLQ 582
Cdd:COG4987 536 MDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
60-580 |
3.11e-80 |
|
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: 263.12 E-value: 3.11e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 60 FEGRNLaqvtQYLW--PLA--GIILLRALFLALSERLSAFATLKIKSAIRQTLLDKLTQLGPSYIEKNGQGATLNTLHNG 135
Cdd:TIGR02203 45 FGGRDR----SVLWwvPLVviGLAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFD 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 136 VEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMILVGHKAEALNQKRWQQLAVLGNYFFDRV 215
Cdd:TIGR02203 121 SEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 216 QGLTQLKLFNATRKELKQIARISDDFRHATLNVLKIAFLSSFALEFLATISVALVAVIIGFRLFFGTL---DFaTGFVVL 292
Cdd:TIGR02203 201 QGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLtagDF-TAFITA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 293 LLApeFYLPLRQLgSHYHARLQ-GISAAADMLIILNAPlPENDDSHTAninID-ANNTISIHDLNFSYP-NSNEGINNIN 369
Cdd:TIGR02203 280 MIA--LIRPLKSL-TNVNAPMQrGLAAAESLFTLLDSP-PEKDTGTRA---IErARGDVEFRNVTFRYPgRDRPALDSIS 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 370 LTLPSTGLVAIVGASGSGKSTLLDCMLGF-HPEVIQhISIDQQPLTTANISQLQQSIAWIPQKPTLFYDTLAANIKLGNP 448
Cdd:TIGR02203 353 LVIEPGETVALVGRSGSGKSTLVNLIPRFyEPDSGQ-ILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRT 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 449 S-ASHEALEHAAKQAGALEFINELPDGFNTLIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNA 527
Cdd:TIGR02203 432 EqADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAA 511
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1590405536 528 IAEYAKNHLVITIAHRLNTVKNAKQLIVMENGCIVQQGDFKALSQQSGEFAKL 580
Cdd:TIGR02203 512 LERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQL 564
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
349-580 |
2.20e-77 |
|
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: 244.83 E-value: 2.20e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSNEGI-NNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAW 427
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVlRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 428 IPQKPTLFYDTLAANIKLGNPSASHEALEHAAKQAGALEFINELPDGFNTLIGEQGEGLSGGQKQRIALARAFLKHAPIL 507
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1590405536 508 VLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIAHRLNTVKNAKQLIVMENGCIVQQGDFKALSQQSGEFAKL 580
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
349-582 |
4.84e-77 |
|
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: 244.06 E-value: 4.84e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAWI 428
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 429 PQKPTLFYDTLAANIKLGNPSASHEALEHAAKQAGALEFINELPDGFNTLIGEQGEGLSGGQKQRIALARAFLKHAPILV 508
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1590405536 509 LDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIAHRLNTVKNAKQLIVMENGCIVQQGDFKALSQQSGEFAKLLQ 582
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWK 234
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
349-584 |
8.62e-77 |
|
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: 243.60 E-value: 8.62e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPN--SNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIA 426
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 427 WIPQKPTLFYDTLAANIKLGNPSASHEALEHAAKQAGALEFINELPDGFNTLIGEQGEGLSGGQKQRIALARAFLKHAPI 506
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1590405536 507 LVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIAHRLNTVKNAKQLIVMENGCIVQQGDFKALSQQSGEFAKLLQTA 584
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
349-575 |
3.56e-73 |
|
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: 233.66 E-value: 3.56e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAWI 428
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 429 PQKPTLFYDTLAANIKLGNPSASHEALEHAAKQAGALEFINELPDGFNTLIGEQGEGLSGGQKQRIALARAFLKHAPILV 508
Cdd:cd03254 83 LQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590405536 509 LDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIAHRLNTVKNAKQLIVMENGCIVQQGDFKALSQQSG 575
Cdd:cd03254 163 LDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
33-319 |
9.41e-73 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 234.87 E-value: 9.41e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 33 SIALGTVNAILMIAGAYLLAQTIhEVMFEGRNLAQVTQYLWPLAGIILLRALFLALSERLSAFATLKIKSAIRQTLLDKL 112
Cdd:cd18561 1 SVLLGLLITALYIAQAWLLARAL-ARIFAGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 113 TQLGPSYIEKNGQGATLNTLHNGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMILVGHK 192
Cdd:cd18561 80 LKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 193 AEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATRKELKQIARISDDFRHATLNVLKIAFLSSFALEFLATISVALVAV 272
Cdd:cd18561 160 AKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALG 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1590405536 273 IIGFRLFFGTLDFATGFVVLLLAPEFYLPLRQLGSHYHARLQGISAA 319
Cdd:cd18561 240 VGALRVLGGQLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQGISAA 286
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
60-580 |
3.64e-72 |
|
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: 241.91 E-value: 3.64e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 60 FEGRNLAQVTQYLWPLAGIILLRALFLALSERLSAFATLKIKSAIRQTLLDKLTQLGPSYIEKNGQGATLNTLHNGVEAL 139
Cdd:TIGR02204 49 FSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 140 HDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMILVGHKAEALNQKRWQQLAVLGNYFFDRVQGLT 219
Cdd:TIGR02204 129 QSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 220 QLKLFNATRKELKQIAR-ISDDFRHATLNVLKIAFLSSFALeFLATISVALVaviigfrLFFGTLDFATG---------F 289
Cdd:TIGR02204 209 TVQAFGHEDAERSRFGGaVEKAYEAARQRIRTRALLTAIVI-VLVFGAIVGV-------LWVGAHDVIAGkmsagtlgqF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 290 VvlLLAPEFYLPLRQLgSHYHARLQGISAAADMLI-ILNAPLPENDDSHTANINIDANNTISIHDLNFSYPNSNE--GIN 366
Cdd:TIGR02204 281 V--FYAVMVAGSIGTL-SEVWGELQRAAGAAERLIeLLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDqpALD 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 367 NINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAWIPQKPTLFYDTLAANIKLG 446
Cdd:TIGR02204 358 GLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYG 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 447 NPSASHEALEHAAKQAGALEFINELPDGFNTLIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQN 526
Cdd:TIGR02204 438 RPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQ 517
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1590405536 527 AIAEYAKNHLVITIAHRLNTVKNAKQLIVMENGCIVQQGDFKALSQQSGEFAKL 580
Cdd:TIGR02204 518 ALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARL 571
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
222-586 |
1.35e-71 |
|
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: 241.26 E-value: 1.35e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 222 KLFNATRKELKQIARISDDFRHATLNVLKIAFLSSFALEFLATISVALVAVIIGFRLFFGTL---DFAtgFVVLLLApEF 298
Cdd:COG5265 232 KYFGNEAREARRYDEALARYERAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMtvgDFV--LVNAYLI-QL 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 299 YLPLRQLGSHYHARLQGISAAADMLIILNAPlPENDDSHTANINIDANNTISIHDLNFSYPNSNEGINNINLTLPSTGLV 378
Cdd:COG5265 309 YIPLNFLGFVYREIRQALADMERMFDLLDQP-PEVADAPDAPPLVVGGGEVRFENVSFGYDPERPILKGVSFEVPAGKTV 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 379 AIVGASGSGKSTLLDCMLGFHpEVIQ-HISIDQQPLTTANISQLQQSIAWIPQKPTLFYDTLAANIKLGNPSASHEALEH 457
Cdd:COG5265 388 AIVGPSGAGKSTLARLLFRFY-DVTSgRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEA 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 458 AAKQAGALEFINELPDGFNTLIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLV 537
Cdd:COG5265 467 AARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTT 546
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1590405536 538 ITIAHRLNTVKNAKQLIVMENGCIVQQGDFKALSQQSGEFAKL--LQTAEQ 586
Cdd:COG5265 547 LVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMwaRQQEEE 597
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
158-580 |
4.82e-67 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 228.36 E-value: 4.82e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 158 LAILVVIFPTDYKAGLIFLLTAPLIPFFMILVGHKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATRKELKQIARI 237
Cdd:PRK11176 154 IGLFIMMFYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKV 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 238 SDDFRHATLNVLKIAFLSSFALEFLATISVALVAVIIGFRLFFGTLDFATGFVVLLLAPEFYLPLRQLgSHYHARLQ-GI 316
Cdd:PRK11176 234 SNRMRQQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSL-TNVNAQFQrGM 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 317 SAAADMLIILNAPLPENDDSHTANiniDANNTISIHDLNFSYPNSNE-GINNINLTLPSTGLVAIVGASGSGKSTLLDCM 395
Cdd:PRK11176 313 AACQTLFAILDLEQEKDEGKRVIE---RAKGDIEFRNVTFTYPGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 396 LGFHpEVIQ-HISIDQQPLTTANISQLQQSIAWIPQKPTLFYDTLAANIKLG-NPSASHEALEHAAKQAGALEFINELPD 473
Cdd:PRK11176 390 TRFY-DIDEgEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYArTEQYSREQIEEAARMAYAMDFINKMDN 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 474 GFNTLIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIAHRLNTVKNAKQL 553
Cdd:PRK11176 469 GLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEI 548
|
410 420
....*....|....*....|....*..
gi 1590405536 554 IVMENGCIVQQGDFKALSQQSGEFAKL 580
Cdd:PRK11176 549 LVVEDGEIVERGTHAELLAQNGVYAQL 575
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
41-590 |
6.92e-67 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 228.31 E-value: 6.92e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 41 AILMIAGAYLLAQTIHE-VMFeGRNLAQVT--QYLWPLAGIILLRALFLALSERLSAFATLKIKSAIRQTLL----DKLT 113
Cdd:PRK13657 22 ILLAVANVLLAAATFAEpILF-GRIIDAISgkGDIFPLLAAWAGFGLFNIIAGVLVARHADRLAHRRRLAVLteyfERII 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 114 QLGPSYIEKNGQGATLNTLHNGVEALH----DYYAKYLpgvaySALIPLAILV-VIFPTDYKAGLIflLTAPLIPFFMI- 187
Cdd:PRK13657 101 QLPLAWHSQRGSGRALHTLLRGTDALFglwlEFMREHL-----ATLVALVVLLpLALFMNWRLSLV--LVVLGIVYTLIt 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 188 -LVGHKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATRKELKQIARISDDFRHATLNVLKIAFLSSFALEFLATIS 266
Cdd:PRK13657 174 tLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNRIEAETQALRDIADNLLAAQMPVLSWWALASVLNRAASTIT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 267 VALVAVI------------------IGF-RLFFGTLDFATGFVVLLLAPEfylplrqlgshyhARLQgisaaaDMLIILN 327
Cdd:PRK13657 254 MLAILVLgaalvqkgqlrvgevvafVGFaTLLIGRLDQVVAFINQVFMAA-------------PKLE------EFFEVED 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 328 APLPENDDSHtaniNIDANN---TISIHDLNFSYPNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQ 404
Cdd:PRK13657 315 AVPDVRDPPG----AIDLGRvkgAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 405 HISIDQQPLTTANISQLQQSIAWIPQKPTLFYDTLAANIKLGNPSASHEALEHAAKQAGALEFINELPDGFNTLIGEQGE 484
Cdd:PRK13657 391 RILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGR 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 485 GLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIAHRLNTVKNAKQLIVMENGCIVQQ 564
Cdd:PRK13657 471 QLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVES 550
|
570 580
....*....|....*....|....*.
gi 1590405536 565 GDFKALSQQSGEFAKLLQTaeQGVTN 590
Cdd:PRK13657 551 GSFDELVARGGRFAALLRA--QGMLQ 574
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
349-559 |
1.67e-63 |
|
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: 206.08 E-value: 1.67e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNS-NEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAW 427
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 428 IPQKPTLFYDTLAANIklgnpsashealehaakqagalefinelpdgfntligeqgegLSGGQKQRIALARAFLKHAPIL 507
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1590405536 508 VLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIAHRLNTVKNAKQLIVMENG 559
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
349-565 |
3.29e-61 |
|
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: 201.95 E-value: 3.29e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSY-PNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAW 427
Cdd:cd03244 3 IEFKNVSLRYrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 428 IPQKPTLFYDTLAANIKLGNpSASHEALEHAAKQAGALEFINELPDGFNTLIGEQGEGLSGGQKQRIALARAFLKHAPIL 507
Cdd:cd03244 83 IPQDPVLFSGTIRSNLDPFG-EYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1590405536 508 VLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIAHRLNTVKNAKQLIVMENGCIVQQG 565
Cdd:cd03244 162 VLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFD 219
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
349-582 |
5.06e-61 |
|
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: 202.33 E-value: 5.06e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSY-PNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAW 427
Cdd:cd03252 1 ITFEHVRFRYkPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 428 IPQKPTLFYDTLAANIKLGNPSASHEALEHAAKQAGALEFINELPDGFNTLIGEQGEGLSGGQKQRIALARAFLKHAPIL 507
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1590405536 508 VLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIAHRLNTVKNAKQLIVMENGCIVQQGDFKALSQQSGEFAKLLQ 582
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQ 235
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
134-582 |
2.46e-59 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 208.03 E-value: 2.46e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 134 NGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMILVGHKAEALNQKRWQQLAVLGNYFFD 213
Cdd:PRK10790 130 NDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 214 RVQGLTQLKLFnatRKELKQIARISDDFRHATLNVLKIAFLSSFALEFLATISVALVavIIGFRLFFGTLDFATGFVVLL 293
Cdd:PRK10790 210 VINGMSVIQQF---RQQARFGERMGEASRSHYMARMQTLRLDGFLLRPLLSLFSALI--LCGLLMLFGFSASGTIEVGVL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 294 LAPEFYL-----PLRQLGSHYHARLQGISAAADMLIILNAPL-PENDDSHTAninidANNTISIHDLNFSYPNSNEGINN 367
Cdd:PRK10790 285 YAFISYLgrlnePLIELTTQQSMLQQAVVAGERVFELMDGPRqQYGNDDRPL-----QSGRIDIDNVSFAYRDDNLVLQN 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 368 INLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAWIPQKPTLFYDTLAANIKLGN 447
Cdd:PRK10790 360 INLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 448 PsASHEALEHAAKQAGALEFINELPDGFNTLIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNA 527
Cdd:PRK10790 440 D-ISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQA 518
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1590405536 528 IAEYAKNHLVITIAHRLNTVKNAKQLIVMENGCIVQQGDFKALSQQSGEFAKLLQ 582
Cdd:PRK10790 519 LAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQ 573
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
30-544 |
3.83e-58 |
|
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: 203.36 E-value: 3.83e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 30 LKLSIALGTVNAI----LMIAGAYLL--AQTIHEVMFEGRNLAQVTqylwpLAGIilLRALFLALsERL-SAFATLKIKS 102
Cdd:TIGR02868 15 LALAVLLGALALGsavaLLGVSAWLIsrAAEMPPVLYLSVAAVAVR-----AFGI--GRAVFRYL-ERLvGHDAALRSLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 103 AIRQTLLDKLTQLGPSYIEKNGQGATLNTLHNGVEALHDYYAK-YLPGVAYSALIPLAILV--VIFPTdykAGLIF---- 175
Cdd:TIGR02868 87 ALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRvIVPAGVALVVGAAAVAAiaVLSVP---AALILaagl 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 176 LLTAPLIPFFMILVGHKAE-ALNQKRWQQLAVLgnyfFDRVQGLTQLKLFNATRKELKQIARISDDFRHATLNVLKIAFL 254
Cdd:TIGR02868 164 LLAGFVAPLVSLRAARAAEqALARLRGELAAQL----TDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 255 SSFALEFLATISVALVAVIIGFRLFFGTLDFATGFVVLLLAPEFYLPLRQLGSHYHARLQGISAAADMLIILNAPLPEND 334
Cdd:TIGR02868 240 GAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAGPVAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 335 -DSHTANINIDANNTISIHDLNFSYPNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPL 413
Cdd:TIGR02868 320 gSAPAAGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 414 TTANISQLQQSIAWIPQKPTLFYDTLAANIKLGNPSASHEALEHAAKQAGALEFINELPDGFNTLIGEQGEGLSGGQKQR 493
Cdd:TIGR02868 400 SSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQR 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1590405536 494 IALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIAHRL 544
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
90-582 |
6.44e-58 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 203.52 E-value: 6.44e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 90 ERL-SAFATLKIKSAIRQTLLDKLTQLGPSYIEKNGQGATLNTLHNGVEALHDYYAKYLPGVAySALipLAILVVIF--- 165
Cdd:PRK11160 80 ERLvSHDATFRVLTHLRVFTFSKLLPLSPAGLARYRQGDLLNRLVADVDTLDHLYLRLISPLV-AAL--VVILVLTIgls 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 166 ----PTDYKAGLIFLLTAPLIPFFMILVGHKA-EALNQKRwqqlAVLGNYFFDRVQGLTQLKLFNATRKELKQIAR---- 236
Cdd:PRK11160 157 ffdlTLALTLGGILLLLLLLLPLLFYRLGKKPgQDLTHLR----AQYRVQLTEWLQGQAELTLFGAEDRYRQQLEQteqq 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 237 -ISDDFRHATLNVLKIAFLSsFALEFLATISVALVAVIIG--------FRLFFgtldFATgfvvlLLAPEFYLPL----R 303
Cdd:PRK11160 233 wLAAQRRQANLTGLSQALMI-LANGLTVVLMLWLAAGGVGgnaqpgalIALFV----FAA-----LAAFEALMPVagafQ 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 304 QLGshyharlQGISAAADML-IILNAPLPENDDSHTANINidaNNTISIHDLNFSYPNSNEG-INNINLTLPSTGLVAIV 381
Cdd:PRK11160 303 HLG-------QVIASARRINeITEQKPEVTFPTTSTAAAD---QVSLTLNNVSFTYPDQPQPvLKGLSLQIKAGEKVALL 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 382 GASGSGKSTLL-------DCMLGfhpeviqHISIDQQPLTTANISQLQQSIAWIPQKPTLFYDTLAANIKLGNPSASHEA 454
Cdd:PRK11160 373 GRTGCGKSTLLqlltrawDPQQG-------EILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEA 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 455 LEHAAKQAGaLEFINELPDGFNTLIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKN 534
Cdd:PRK11160 446 LIEVLQQVG-LEKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQN 524
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1590405536 535 HLVITIAHRLNTVKNAKQLIVMENGCIVQQGDFKALSQQSGEFAKLLQ 582
Cdd:PRK11160 525 KTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQ 572
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
353-565 |
1.98e-57 |
|
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: 192.03 E-value: 1.98e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 353 DLNFSYPNS-NEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAWIPQK 431
Cdd:cd03245 7 NVSFSYPNQeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 432 PTLFYDTLAANIKLGNPSASHEALEHAAKQAGALEFINELPDGFNTLIGEQGEGLSGGQKQRIALARAFLKHAPILVLDE 511
Cdd:cd03245 87 VTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1590405536 512 PTAHLDSQTEQLIQNAIAEYAKNHLVITIAHRLNTVKNAKQLIVMENGCIVQQG 565
Cdd:cd03245 167 PTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
41-584 |
2.97e-57 |
|
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: 202.04 E-value: 2.97e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 41 AILMIAGAYLLAQTIHEVMFEGRNL--------AQVTQYLWPLAGIillralFLALSERLSAFATLKIKSAIRQTLLDK- 111
Cdd:TIGR01192 22 LLIVIANITLAAITIAEPILFGRIIdaissksdVLPTLALWAGFGV------FNTIAYVLVAREADRLAHGRRATLLTEa 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 112 ---LTQLGPSYIEKNGQGATLNTLHNGVEALHDYYAKYL-----PGVAYSALIPLAilvviFPTDYKAGLIFLLTAPLIP 183
Cdd:TIGR01192 96 fgrIISMPLSWHQQRGTSNALHTLLRATETLFGLWLEFMrqhlaTFVALFLLIPTA-----FAMDWRLSIVLMVLGILYI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 184 FFMILVghkaeaLNQKRWQQLAVLGNY------FFDRVQGLTQLKLFNATRKELKQIARISDDFRHATLNVLKIAFLSSF 257
Cdd:TIGR01192 171 LIAKLV------MQRTKNGQAAVEHHYhnvfkhVSDSISNVSVVHSYNRIEAETSALKQFTNNLLSAQYPVLDWWALASG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 258 ALEFLATISVALVAVI------------------IGF-RLFFGTLDFATGFVVLLLAPEfylplrqlgshyhARLQGISA 318
Cdd:TIGR01192 245 LNRMASTISMMCILVIgtvlvikgelsvgeviafIGFaNLLIGRLDQMSGFITQIFEAR-------------AKLEDFFD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 319 AADMLIILNAPlpeNDDSHTANINidanNTISIHDLNFSYPNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGF 398
Cdd:TIGR01192 312 LEDSVFQREEP---ADAPELPNVK----GAVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 399 HPEVIQHISIDQQPLTTANISQLQQSIAWIPQKPTLFYDTLAANIKLGNPSASHEALEHAAKQAGALEFINELPDGFNTL 478
Cdd:TIGR01192 385 YDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTL 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 479 IGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIAHRLNTVKNAKQLIVMEN 558
Cdd:TIGR01192 465 VGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQ 544
|
570 580
....*....|....*....|....*.
gi 1590405536 559 GCIVQQGDFKALSQQSGEFAKLLQTA 584
Cdd:TIGR01192 545 GRLIEKGSFQELIQKDGRFYKLLRRS 570
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
325-582 |
5.62e-57 |
|
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: 203.44 E-value: 5.62e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 325 ILNAPLPENDDSHTANINIDANntISIHDLNFSY-PNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVI 403
Cdd:TIGR01846 434 ILNSPTEPRSAGLAALPELRGA--ITFENIRFRYaPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQH 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 404 QHISIDQQPLTTANISQLQQSIAWIPQKPTLFYDTLAANIKLGNPSASHEALEHAAKQAGALEFINELPDGFNTLIGEQG 483
Cdd:TIGR01846 512 GQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKG 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 484 EGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIAHRLNTVKNAKQLIVMENGCIVQ 563
Cdd:TIGR01846 592 ANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAE 671
|
250
....*....|....*....
gi 1590405536 564 QGDFKALSQQSGEFAKLLQ 582
Cdd:TIGR01846 672 SGRHEELLALQGLYARLWQ 690
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
153-572 |
3.35e-53 |
|
type I secretion system ATPase, LssB 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. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 192.77 E-value: 3.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 153 SALI--PLAI--LVVIFptdYKAG---LIFLLTAPLIPFFMILVGHKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFN 225
Cdd:TIGR03375 265 TALIdlPFALlfLLVIA---IIGGplvWVPLVAIPLILLPGLLLQRPLSRLAEESMRESAQRNAVLVESLSGLETIKALN 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 226 ATRKELKQ-------IARISDDFRHATlnvlkiAFLSSFALEFLATISVALVAV----IIGFRLFFGTLDFATgfvvlLL 294
Cdd:TIGR03375 342 AEGRFQRRweqtvaaLARSGLKSRFLS------NLATNFAQFIQQLVSVAIVVVgvylISDGELTMGGLIACV-----ML 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 295 APEFYLPLRQLgSHYHARLQGISAAADML-IILNAPLPENDDSHTANInIDANNTISIHDLNFSYPNSN-EGINNINLTL 372
Cdd:TIGR03375 411 SGRALAPLGQL-AGLLTRYQQAKTALQSLdELMQLPVERPEGTRFLHR-PRLQGEIEFRNVSFAYPGQEtPALDNVSLTI 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 373 PSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAWIPQKPTLFYDTLAANIKLGNPSASH 452
Cdd:TIGR03375 489 RPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGYVPQDPRLFYGTLRDNIALGAPYADD 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 453 EALEHAAKQAGALEFINELPDGFNTLIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYA 532
Cdd:TIGR03375 569 EEILRAAELAGVTEFVRRHPDGLDMQIGERGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWL 648
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1590405536 533 KNHLVITIAHRLNTVKNAKQLIVMENGCIVQQGD----FKALSQ 572
Cdd:TIGR03375 649 AGKTLVLVTHRTSLLDLVDRIIVMDNGRIVADGPkdqvLEALRK 692
|
|
| ABC_6TM_AarD_CydDC_like |
cd18781 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine ... |
26-322 |
1.26e-50 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; This subgroup belongs to the ABC_6TM_AarD_CydDC_like subgroup of the ABC_6TM exporter family. The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs). 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: 350054 [Multi-domain] Cd Length: 290 Bit Score: 176.19 E-value: 1.26e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 26 AAMWLKLsIAlgtvNAILMIAGAYLLAQtihevMFEGR-NLAQVTQYLWPLAGIILLRALFLALSERLSAFATLKIKSAI 104
Cdd:cd18781 3 LLQWISL-LA----NIAFVFSIANLLQK-----LLEGKlTTASLLIVLGILAIAIIVRFICTRLASRASYRASADVKKTL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 105 RQTLLDKLTQLGPSYIEKNGQGATLNTLHNGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPF 184
Cdd:cd18781 73 REKIYDKLLRLGPSYQEKVSTAEVVQLSVEGVEQLEIYFGRYLPQFFYSMLAPLTLFVVLAPINWKAALVLLICVPLIPI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 185 FMILVGHKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATRKELKQIARISDDFRHATLNVLKIAFLSSFALEFLAT 264
Cdd:cd18781 153 SIIAVQKIAKKLLSKYWGSYTDLGDSFLENLQGLTTLKIYQADERRHEEMNEEAEDFRKITMKVLTMQLNSITVMDLVAY 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1590405536 265 ISVALVAVIIGFRLFFGTLDFATGFVVLLLAPEFYLPLRQLGSHYHARLQGISAAADM 322
Cdd:cd18781 233 GGAALGIILALLQFANGSISLAGALFIILLSAEFFLPLRLLGSFFHIAMNGMAASDKI 290
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
349-576 |
1.81e-49 |
|
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: 180.33 E-value: 1.81e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSNEGI-NNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAW 427
Cdd:COG4618 331 LSVENLTVVPPGSKRPIlRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 428 IPQKPTLFYDTLAANI-KLGNPSAshEALEHAAKQAGALEFINELPDGFNTLIGEQGEGLSGGQKQRIALARAFLKHAPI 506
Cdd:COG4618 411 LPQDVELFDGTIAENIaRFGDADP--EKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRL 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1590405536 507 LVLDEPTAHLDSQTEQLIQNAIAEyAKNH--LVITIAHRLNTVKNAKQLIVMENGCIVQQGD----FKALSQQSGE 576
Cdd:COG4618 489 VVLDEPNSNLDDEGEAALAAAIRA-LKARgaTVVVITHRPSLLAAVDKLLVLRDGRVQAFGPrdevLARLARPAAA 563
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
282-575 |
4.65e-49 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 179.14 E-value: 4.65e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 282 TLDFATGFVVLL-------LAPEFYLPLRQLGSHYHARLQGISAAADMLIILNAPLPENDDSHTANINidanntisihdl 354
Cdd:PRK10789 252 TLGQLTSFVMYLglmiwpmLALAWMFNIVERGSAAYSRIRAMLAEAPVVKDGSEPVPEGRGELDVNIR------------ 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 355 NFSYP-NSNEGINNINLTLPSTGLVAIVGASGSGKSTLLdCMLGFHPEVIQ-HISIDQQPLTTANISQLQQSIAWIPQKP 432
Cdd:PRK10789 320 QFTYPqTDHPALENVNFTLKPGQMLGICGPTGSGKSTLL-SLIQRHFDVSEgDIRFHDIPLTKLQLDSWRSRLAVVSQTP 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 433 TLFYDTLAANIKLGNPSASHEALEHAAKQAGALEFINELPDGFNTLIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEP 512
Cdd:PRK10789 399 FLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDA 478
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1590405536 513 TAHLDSQTEQLIQNAIAEYAKNHLVITIAHRLNTVKNAKQLIVMENGCIVQQGDFKALSQQSG 575
Cdd:PRK10789 479 LSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSG 541
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
353-561 |
6.29e-49 |
|
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: 169.57 E-value: 6.29e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 353 DLNFSYPNSNEG--INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAWIPQ 430
Cdd:cd03248 16 NVTFAYPTRPDTlvLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 431 KPTLFYDTLAANIKLGNPSASHEALEHAAKQAGALEFINELPDGFNTLIGEQGEGLSGGQKQRIALARAFLKHAPILVLD 510
Cdd:cd03248 96 EPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1590405536 511 EPTAHLDSQTEQLIQNAIAEYAKNHLVITIAHRLNTVKNAKQLIVMENGCI 561
Cdd:cd03248 176 EATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
173-581 |
3.03e-47 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 176.45 E-value: 3.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 173 LIFLLTAPLIPFFMILVGHKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATRKELKQiarisddFRHATLNVLKIA 252
Cdd:TIGR00958 305 MVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASR-------FKEALEETLQLN 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 253 FLSSFA-LEFLATISVALVAVIIGFrLFFGTLDFATGFV-------VLLLAPEFYLPLRQLGSHYHARLQGISAAADMLI 324
Cdd:TIGR00958 378 KRKALAyAGYLWTTSVLGMLIQVLV-LYYGGQLVLTGKVssgnlvsFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 325 ILN-APLPENDDSHTANiniDANNTISIHDLNFSYPN--SNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPE 401
Cdd:TIGR00958 457 YLDrKPNIPLTGTLAPL---NLEGLIEFQDVSFSYPNrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQP 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 402 VIQHISIDQQPLTTANISQLQQSIAWIPQKPTLFYDTLAANIKLGNPSASHEALEHAAKQAGALEFINELPDGFNTLIGE 481
Cdd:TIGR00958 534 TGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGE 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 482 QGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNhlVITIAHRLNTVKNAKQLIVMENGCI 561
Cdd:TIGR00958 614 KGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRT--VLLIAHRLSTVERADQILVLKKGSV 691
|
410 420
....*....|....*....|
gi 1590405536 562 VQQGDFKALSQQSGEFAKLL 581
Cdd:TIGR00958 692 VEMGTHKQLMEDQGCYKHLV 711
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
173-580 |
4.54e-44 |
|
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: 167.22 E-value: 4.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 173 LIFLLTAPLIPFFMILVGHKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATRKELKQIarisdDFRHATLnvLKIA 252
Cdd:TIGR01193 299 LLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKI-----DSEFGDY--LNKS 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 253 FLSSFALEFLATISVALVAVIIGFRLFFGTLDFATGFVVL-------LLAPEFYLPLRQLgSHYHARLQGISAAADMLII 325
Cdd:TIGR01193 372 FKYQKADQGQQAIKAVTKLILNVVILWTGAYLVMRGKLTLgqlitfnALLSYFLTPLENI-INLQPKLQAARVANNRLNE 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 326 LNAPLPENDDSHTANINIDANNTISIHDLNFSYPNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQH 405
Cdd:TIGR01193 451 VYLVDSEFINKKKRTELNNLNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGE 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 406 ISIDQQPLTTANISQLQQSIAWIPQKPTLFYDTLAANIKLGN-PSASHEALEHAAKQAGALEFINELPDGFNTLIGEQGE 484
Cdd:TIGR01193 531 ILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAkENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGS 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 485 GLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAeYAKNHLVITIAHRLNTVKNAKQLIVMENGCIVQQ 564
Cdd:TIGR01193 611 SISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLL-NLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQ 689
|
410
....*....|....*.
gi 1590405536 565 GDFKALSQQSGEFAKL 580
Cdd:TIGR01193 690 GSHDELLDRNGFYASL 705
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
349-561 |
1.61e-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: 150.44 E-value: 1.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSNEGI-NNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAW 427
Cdd:cd03246 1 LEVENVSFRYPGAEPPVlRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 428 IPQKPTLFYDTLAANIklgnpsashealehaakqagalefinelpdgfntligeqgegLSGGQKQRIALARAFLKHAPIL 507
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1590405536 508 VLDEPTAHLDSQTEQLIQNAIAEY-AKNHLVITIAHRLNTVKNAKQLIVMENGCI 561
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
346-561 |
1.39e-41 |
|
type I secretion system ABC transporter, PrtD 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: 200134 [Multi-domain] Cd Length: 544 Bit Score: 157.89 E-value: 1.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 346 NNTISIHDLNFSYPNSNEGI-NNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQS 424
Cdd:TIGR01842 314 EGHLSVENVTIVPPGGKKPTlRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKH 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 425 IAWIPQKPTLFYDTLAANIKLGNPSASHEALEHAAKQAGALEFINELPDGFNTLIGEQGEGLSGGQKQRIALARAFLKHA 504
Cdd:TIGR01842 394 IGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDP 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1590405536 505 PILVLDEPTAHLDSQTEQLIQNAIAEY-AKNHLVITIAHRLNTVKNAKQLIVMENGCI 561
Cdd:TIGR01842 474 KLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
349-559 |
4.16e-40 |
|
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: 144.92 E-value: 4.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSNEGIN----NINLTLPSTGLVAIVGASGSGKSTLLDCMLGfhpEViqhisidqqPLTTANIsQLQQS 424
Cdd:cd03250 1 ISVEDASFTWDSGEQETSftlkDINLEVPKGELVAIVGPVGSGKSSLLSALLG---EL---------EKLSGSV-SVPGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 425 IAWIPQKPTLFYDTLAANIKLGNPsASHEALEHAAKqAGALEF-INELPDGFNTLIGEQGEGLSGGQKQRIALARAFLKH 503
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKP-FDEERYEKVIK-ACALEPdLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1590405536 504 APILVLDEPTAHLDSQTEQ-LIQNAIAEYAKNH-LVITIAHRLNTVKNAKQLIVMENG 559
Cdd:cd03250 146 ADIYLLDDPLSAVDAHVGRhIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
349-565 |
1.62e-37 |
|
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: 137.06 E-value: 1.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSNEGI-NNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANiSQLQQSIAW 427
Cdd:cd03247 1 LSINNVSFSYPEQEQQVlKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 428 IPQKPTLFYDTLAANIklgnpsashealehaakqagalefinelpdgfntligeqGEGLSGGQKQRIALARAFLKHAPIL 507
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1590405536 508 VLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIAHRLNTVKNAKQLIVMENGCIVQQG 565
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
349-561 |
1.97e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 139.07 E-value: 1.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYpNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANisqlqQSIAWI 428
Cdd:COG1121 7 IELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR-----RRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 429 PQK-------PTLFYDTLAANIK-----LGNPSAS-HEALEHAAKQAGALEFINelpdgfnTLIGEqgegLSGGQKQRIA 495
Cdd:COG1121 81 PQRaevdwdfPITVRDVVLMGRYgrrglFRRPSRAdREAVDEALERVGLEDLAD-------RPIGE----LSGGQQQRVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1590405536 496 LARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAK-NHLVITIAHRLNTV-KNAKQLIVMENGCI 561
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRReGKTILVVTHDLGAVrEYFDRVLLLNRGLV 217
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
349-565 |
2.15e-36 |
|
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: 134.85 E-value: 2.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSY-PNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAW 427
Cdd:cd03369 7 IEVENLSVRYaPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 428 IPQKPTLFYDTLAANIKLGNpsashealEHAAKQA-GALEfinelpdgfntlIGEQGEGLSGGQKQRIALARAFLKHAPI 506
Cdd:cd03369 87 IPQDPTLFSGTIRSNLDPFD--------EYSDEEIyGALR------------VSEGGLNLSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1590405536 507 LVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIAHRLNTVKNAKQLIVMENGCIVQQG 565
Cdd:cd03369 147 LVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
365-514 |
4.94e-36 |
|
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: 132.00 E-value: 4.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAWIPQKPTLFYD-TLAANI 443
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1590405536 444 KLGnpsASHEALEHAAKQAGALEFINELPDGF--NTLIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTA 514
Cdd:pfam00005 81 RLG---LLLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
349-561 |
2.90e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 131.86 E-value: 2.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYpNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAWI 428
Cdd:COG4619 1 LELEGLSFRV-GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 429 PQKPTLFYDTLAANI----KLGNPSASHEALEHAAKQAGalefineLPDGF-NTLIGEqgegLSGGQKQRIALARAFLKH 503
Cdd:COG4619 80 PQEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLG-------LPPDIlDKPVER----LSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1590405536 504 APILVLDEPTAHLDSQTEQLIQNAIAEYAKNH--LVITIAH------RLntvknAKQLIVMENGCI 561
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYLAEEgrAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
344-585 |
1.02e-33 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 137.85 E-value: 1.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 344 DANNTISIHDLNFSY---PNSnEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQH--------------- 405
Cdd:PTZ00265 1161 DIKGKIEIMDVNFRYisrPNV-PIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHhivfknehtndmtne 1239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 406 ---------------------------------------ISIDQQPLTTANISQLQQSIAWIPQKPTLFYDTLAANIKLG 446
Cdd:PTZ00265 1240 qdyqgdeeqnvgmknvnefsltkeggsgedstvfknsgkILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFG 1319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 447 NPSASHEALEHAAKQAGALEFINELPDGFNTLIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQN 526
Cdd:PTZ00265 1320 KEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEK 1399
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590405536 527 AIAEYAK--NHLVITIAHRLNTVKNAKQLIVMEN----GCIVQ-QGDFKA-LSQQSGEFAKLLQTAE 585
Cdd:PTZ00265 1400 TIVDIKDkaDKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEElLSVQDGVYKKYVKLAK 1466
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
350-565 |
1.60e-33 |
|
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: 126.01 E-value: 1.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 350 SIHDLNFSYPNsNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAWIP 429
Cdd:cd03214 1 EVENLSVGYGG-RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 430 QkptlfydtlaaniklgnpsashealehAAKQAGALEFINElpdGFNTligeqgegLSGGQKQRIALARAFLKHAPILVL 509
Cdd:cd03214 80 Q---------------------------ALELLGLAHLADR---PFNE--------LSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1590405536 510 DEPTAHLDSQTEQLIQNAIAEYAK--NHLVITIAHRLN-TVKNAKQLIVMENGCIVQQG 565
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARerGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
350-559 |
2.18e-33 |
|
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: 125.05 E-value: 2.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 350 SIHDLNFSYPNsNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAWIP 429
Cdd:cd00267 1 EIENLSFRYGG-RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 430 QkptlfydtlaaniklgnpsashealehaakqagalefinelpdgfntligeqgegLSGGQKQRIALARAFLKHAPILVL 509
Cdd:cd00267 80 Q-------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1590405536 510 DEPTAHLDSQTEQLIQNAIAEYAKNHL-VITIAHRLNTVKNAKQ-LIVMENG 559
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEGRtVIIVTHDPELAELAADrVIVLKDG 156
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
349-566 |
7.36e-33 |
|
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: 125.91 E-value: 7.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAWI 428
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 429 PQKPT--LFYDTLAANIKLG------NPSASHEALEHAAKQAGALEFINELPdgFNtligeqgegLSGGQKQRIALARAF 500
Cdd:COG1122 81 FQNPDdqLFAPTVEEDVAFGpenlglPREEIRERVEEALELVGLEHLADRPP--HE---------LSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1590405536 501 LKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHL-VITIAHRLNTV-KNAKQLIVMENGCIVQQGD 566
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKtVIIVTHDLDLVaELADRVIVLDDGRIVADGT 217
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
215-583 |
2.22e-32 |
|
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: 133.53 E-value: 2.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 215 VQGLTQLKLFNATRKELKQIARIsddfRHATLNVLKI-AFLSSFAL------EFLATISVALVAVIIGFRlffGTLDFAT 287
Cdd:TIGR00957 503 LNGIKVLKLYAWELAFLDKVEGI----RQEELKVLKKsAYLHAVGTftwvctPFLVALITFAVYVTVDEN---NILDAEK 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 288 GFVVLLLAPEFYLPLRQLGSHYHARLQGISAAADMLIILNAPLPENDDSHTANINIDANNTISIHDLNFSYPNSNE-GIN 366
Cdd:TIGR00957 576 AFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPGEGNSITVHNATFTWARDLPpTLN 655
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 367 NINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIdqqplttanisqlQQSIAWIPQKPTLFYDTLAANIKLG 446
Cdd:TIGR00957 656 GITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM-------------KGSVAYVPQQAWIQNDSLRENILFG 722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 447 NPSasHEALEHAAKQAGAL-EFINELPDGFNTLIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQT-EQLI 524
Cdd:TIGR00957 723 KAL--NEKYYQQVLEACALlPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVgKHIF 800
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1590405536 525 QNAIAEYA--KNHLVITIAHRLNTVKNAKQLIVMENGCIVQQGDFKALSQQSGEFAKLLQT 583
Cdd:TIGR00957 801 EHVIGPEGvlKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRT 861
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
365-584 |
3.02e-32 |
|
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: 133.15 E-value: 3.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAWIPQKPTLFYDTLAANIk 444
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL- 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 445 lgNP--SASHEALEHAAKQAGALEFINELPDGFNTLIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQ 522
Cdd:TIGR00957 1381 --DPfsQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDN 1458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1590405536 523 LIQNAIAEYAKNHLVITIAHRLNTVKNAKQLIVMENGCIVQQGDFKALSQQSGEFAKLLQTA 584
Cdd:TIGR00957 1459 LIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSMAKDA 1520
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
349-566 |
3.09e-32 |
|
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: 124.77 E-value: 3.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNsNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAWI 428
Cdd:COG1120 2 LEAENLSVGYGG-RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 429 PQKPTLFYDTLAANI----------KLGNPSAS-HEALEHAAKQAGALEFINELpdgFNTLigeqgeglSGGQKQRIALA 497
Cdd:COG1120 81 PQEPPAPFGLTVRELvalgryphlgLFGRPSAEdREAVEEALERTGLEHLADRP---VDEL--------SGGERQRVLIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1590405536 498 RAFLKHAPILVLDEPTAHLD--SQTE--QLIQNAIAEyaKNHLVITIAHRLNTVKN-AKQLIVMENGCIVQQGD 566
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDlaHQLEvlELLRRLARE--RGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGP 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
350-559 |
1.75e-31 |
|
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: 121.42 E-value: 1.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 350 SIHDLNFSYPNSNE-GINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAWI 428
Cdd:cd03225 1 ELKNLSFSYPDGARpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 429 PQKPT--LFYDTLAANIKLG------NPSASHEALEHAAKQAGALEFINELPdgfntligeqgEGLSGGQKQRIALARAF 500
Cdd:cd03225 81 FQNPDdqFFGPTVEEEVAFGlenlglPEEEIEERVEEALELVGLEGLRDRSP-----------FTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1590405536 501 LKHAPILVLDEPTAHLDSQTEQLIQNAIAEY-AKNHLVITIAHRLNTVKN-AKQLIVMENG 559
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLkAEGKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
350-565 |
4.60e-31 |
|
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: 120.33 E-value: 4.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 350 SIHDLNFSYpNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTtanisQLQQSIAWIP 429
Cdd:cd03235 1 EVEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE-----KERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 430 QK-------PTLFYDTLAANI-----KLGNPSASH-EALEHAAKQAGALEFINELpdgfntlIGEqgegLSGGQKQRIAL 496
Cdd:cd03235 75 QRrsidrdfPISVRDVVLMGLyghkgLFRRLSKADkAKVDEALERVGLSELADRQ-------IGE----LSGGQQQRVLL 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 497 ARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEY-AKNHLVITIAHRLNTVKNAKQLIVMENGCIVQQG 565
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
349-564 |
3.49e-30 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 118.22 E-value: 3.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSNEGI---NNINLTLPSTGLVAIVGASGSGKSTLLDCMLGF-HP---EVIqhisIDQQPLTTANISQL 421
Cdd:COG1136 5 LELRNLTKSYGTGEGEVtalRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLdRPtsgEVL----IDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 422 ----QQSIAWIPQKPTLF-YDTLAANIKL-----GNPSAshEALEHAAKqagALEFINeLPDGFNTLIGEqgegLSGGQK 491
Cdd:COG1136 81 arlrRRHIGFVFQFFNLLpELTALENVALplllaGVSRK--ERRERARE---LLERVG-LGDRLDHRPSQ----LSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590405536 492 QRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNH----LVITiaHRLNTVKNAKQLIVMENGCIVQQ 564
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELgttiVMVT--HDPELAARADRVIRLRDGRIVSD 225
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
241-584 |
7.73e-30 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 125.86 E-value: 7.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 241 FRHATLnvlkiafLSSFALEFLATISVALVAVIIG-FRLFFGTLDFATGFVVLLLAPEFYLPLRQLGSHYHA-------- 311
Cdd:PLN03232 516 FRKAQL-------LSAFNSFILNSIPVVVTLVSFGvFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQvvnanvsl 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 312 -RLQGISAAADMLIILNAPLPENDDShtaninidanntISIHDLNFSYPN--SNEGINNINLTLPSTGLVAIVGASGSGK 388
Cdd:PLN03232 589 qRIEELLLSEERILAQNPPLQPGAPA------------ISIKNGYFSWDSktSKPTLSDINLEIPVGSLVAIVGGTGEGK 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 389 STLLDCMLGFHPeviqhisidqqPLTTANISqLQQSIAWIPQKPTLFYDTLAANIKLGN---PSASHEALEHAAKQAGal 465
Cdd:PLN03232 657 TSLISAMLGELS-----------HAETSSVV-IRGSVAYVPQVSWIFNATVRENILFGSdfeSERYWRAIDVTALQHD-- 722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 466 efINELPDGFNTLIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQ-TEQLIQNAIAEYAKNHLVITIAHRL 544
Cdd:PLN03232 723 --LDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQL 800
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1590405536 545 NTVKNAKQLIVMENGCIVQQGDFKALSQQSGEFAKLLQTA 584
Cdd:PLN03232 801 HFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENA 840
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
32-319 |
9.40e-30 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 118.81 E-value: 9.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 32 LSIALGTVNAILMIAGAYLLAQTIHEVmFEGRNLAQVTQYLWPLAGIILLRALFLALSERLSAFATLKIKSAIRQTLLDK 111
Cdd:cd07346 3 LALLLLLLATALGLALPLLTKLLIDDV-IPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 112 LTQLGPSYIEKNGQGATLNTLHNGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMILVGH 191
Cdd:cd07346 82 LQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 192 KAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATRKELKQIARISDDFRHATLNVLKIAFLSSFALEFLATISVALVA 271
Cdd:cd07346 162 RIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVL 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1590405536 272 VIIGFRLFFGTLDFATGFVVLLLAPEFYLPLRQLGSHYHARLQGISAA 319
Cdd:cd07346 242 LYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASL 289
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
349-565 |
1.85e-29 |
|
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: 115.69 E-value: 1.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYpNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQlqQSIAWI 428
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER--RNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 429 PQKPTLF-YDTLAANI-----KLGNPSASHEALEH-AAKQAGALEFINELPDGfntligeqgegLSGGQKQRIALARAFL 501
Cdd:cd03259 78 FQDYALFpHLTVAENIafglkLRGVPKAEIRARVReLLELVGLEGLLNRYPHE-----------LSGGQQQRVALARALA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1590405536 502 KHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITI--------AHRLntvknAKQLIVMENGCIVQQG 565
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLREELREELKELQRELGITTIyvthdqeeALAL-----ADRIAVMNEGRIVQVG 213
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
349-565 |
4.45e-29 |
|
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: 115.30 E-value: 4.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPN---SNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQ--- 422
Cdd:cd03257 2 LEVKNLSVSFPTgggSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 423 QSIAWIPQKP-----------TLFYDTLAANIKLGNPSASHEALEHAAKQAG-ALEFINELPDGfntligeqgegLSGGQ 490
Cdd:cd03257 82 KEIQMVFQDPmsslnprmtigEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGlPEEVLNRYPHE-----------LSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1590405536 491 KQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNH--LVITIAHRLNTVKN-AKQLIVMENGCIVQQG 565
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
349-566 |
5.81e-29 |
|
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: 114.59 E-value: 5.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYpNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQ-----HISIDQQPLTT--ANISQL 421
Cdd:cd03260 1 IELRDLNVYY-GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGapdegEVLLDGKDIYDldVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 422 QQSIAWIPQKPTLFYDTLAANIKLG-------NPSASHEALEHAAKQAGalefineLPDGFNTLIGeqGEGLSGGQKQRI 494
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKAA-------LWDEVKDRLH--ALGLSGGQQQRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1590405536 495 ALARAfLKHAP-ILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIAHRLNTVKN-AKQLIVMENGCIVQQGD 566
Cdd:cd03260 151 CLARA-LANEPeVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGP 223
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
237-584 |
8.69e-29 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 122.54 E-value: 8.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 237 ISDD----FRHATLnvlkiafLSSFALEFLATISVALVAVIIG-FRLFFGTLDFATGFVVLLLAPEFYLPLRQLGSHYHA 311
Cdd:PLN03130 508 VRDDelswFRKAQL-------LSAFNSFILNSIPVLVTVVSFGvFTLLGGDLTPARAFTSLSLFAVLRFPLFMLPNLITQ 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 312 ---------RLQGISAAADMLIILNAPLPENDDShtaninidanntISIHDLNFSYPNSNE--GINNINLTLPSTGLVAI 380
Cdd:PLN03130 581 avnanvslkRLEELLLAEERVLLPNPPLEPGLPA------------ISIKNGYFSWDSKAErpTLSNINLDVPVGSLVAI 648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 381 VGASGSGKSTLLDCMLGFHPeviqhisidqqPLTTANISqLQQSIAWIPQKPTLFYDTLAANIKLGNPSAShEALEHAAK 460
Cdd:PLN03130 649 VGSTGEGKTSLISAMLGELP-----------PRSDASVV-IRGTVAYVPQVSWIFNATVRDNILFGSPFDP-ERYERAID 715
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 461 QAGALEFINELPDGFNTLIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQT-EQLIQNAIAEYAKNHLVIT 539
Cdd:PLN03130 716 VTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVgRQVFDKCIKDELRGKTRVL 795
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1590405536 540 IAHRLNTVKNAKQLIVMENGCIVQQGDFKALSQQSGEFAKLLQTA 584
Cdd:PLN03130 796 VTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMENA 840
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
349-576 |
1.31e-28 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 114.18 E-value: 1.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYpNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFhpEVIQH--ISIDQQPLTTANIsQLQQSIA 426
Cdd:COG4555 2 IEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGL--LKPDSgsILIDGEDVRKEPR-EARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 427 WIPQKPTLfYDTLAA--NIKL---GNPSASHEALEHAAKQAGALEFINELpdgfNTLIGEqgegLSGGQKQRIALARAFL 501
Cdd:COG4555 78 VLPDERGL-YDRLTVreNIRYfaeLYGLFDEELKKRIEELIELLGLEEFL----DRRVGE----LSTGMKKKVALARALV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590405536 502 KHAPILVLDEPTAHLDSQTEQLIQNAIAEYAK-NHLVITIAHRLNTVKN-AKQLIVMENGCIVQQGDFKALSQQSGE 576
Cdd:COG4555 149 HDPKVLLLDEPTNGLDVMARRLLREILRALKKeGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
349-573 |
1.90e-28 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 113.62 E-value: 1.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYpNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANiSQLQQSIAWI 428
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP-AEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 429 PQKPTLFYD-TLAANIKL-----GNPSAshEALEHAAKqagALEFInELPDGFNTLIGEqgegLSGGQKQRIALARAFLK 502
Cdd:COG1131 79 PQEPALYPDlTVRENLRFfarlyGLPRK--EARERIDE---LLELF-GLTDAADRKVGT----LSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1590405536 503 HAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIA-HRLNTV-KNAKQLIVMENGCIVQQGDFKALSQQ 573
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAeRLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
349-584 |
3.57e-28 |
|
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: 112.97 E-value: 3.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSNEGI---NNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSI 425
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVpvlKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 426 AWIPQKPTLFYD---TLAAniKLGNPSASHEALEHAAKQAGALEFInELPDGFNTLIGEQgegLSGGQKQRIALARAFLK 502
Cdd:COG1124 82 QMVFQDPYASLHprhTVDR--ILAEPLRIHGLPDREERIAELLEQV-GLPPSFLDRYPHQ---LSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 503 HAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNH--LVITIAHRLNTVKN-AKQLIVMENGCIVQQGDFKALSQQ-SGEFA 578
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLAGpKHPYT 235
|
....*.
gi 1590405536 579 KLLQTA 584
Cdd:COG1124 236 RELLAA 241
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
349-583 |
4.23e-28 |
|
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: 113.08 E-value: 4.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSNEGI-NNINLTLPSTGLVAIVGASGSGKSTL-------LDCMLGfhPEVIQHISIDQQPLTTanisq 420
Cdd:cd03288 20 IKIHDLCVRYENNLKPVlKHVKAYIKPGQKVGICGRTGSGKSSLslaffrmVDIFDG--KIVIDGIDISKLPLHT----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 421 LQQSIAWIPQKPTLFYDTLAANIklgNP--SASHEALEHAAKQAGALEFINELPDGFNTLIGEQGEGLSGGQKQRIALAR 498
Cdd:cd03288 93 LRSRLSIILQDPILFSGSIRFNL---DPecKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLAR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 499 AFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIAHRLNTVKNAKQLIVMENGCIVQ-QGDFKALSQQSGEF 577
Cdd:cd03288 170 AFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVEcDTPENLLAQEDGVF 249
|
....*.
gi 1590405536 578 AKLLQT 583
Cdd:cd03288 250 ASLVRT 255
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
349-526 |
4.80e-28 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 113.26 E-value: 4.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSNEG---INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPlttanISQLQQSI 425
Cdd:COG1116 8 LELRGVSKRFPTGGGGvtaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP-----VTGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 426 AWIPQKPTLF-YDTLAANIKLG------NPSASHEALEHAAKQAGALEFINELPDgfntligeQgegLSGGQKQRIALAR 498
Cdd:COG1116 83 GVVFQEPALLpWLTVLDNVALGlelrgvPKAERRERARELLELVGLAGFEDAYPH--------Q---LSGGMRQRVAIAR 151
|
170 180
....*....|....*....|....*...
gi 1590405536 499 AFLKHAPILVLDEPTAHLDSQTEQLIQN 526
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQD 179
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
349-570 |
5.10e-28 |
|
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: 118.08 E-value: 5.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPN-SNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHP---EVIQHISIDQQPLTTANISQLQQS 424
Cdd:COG1123 5 LEVRDLSVRYPGgDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPhggRISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 425 IAWIPQKPT--LFYDTLAANI--KLGNPSASHEALEHAAKQAgaLEFInelpdGFNTLIGEQGEGLSGGQKQRIALARAF 500
Cdd:COG1123 85 IGMVFQDPMtqLNPVTVGDQIaeALENLGLSRAEARARVLEL--LEAV-----GLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1590405536 501 LKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNH--LVITIAHRLNTVKN-AKQLIVMENGCIVQQGDFKAL 570
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
349-561 |
5.47e-28 |
|
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: 110.18 E-value: 5.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNsNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTaNISQLQQSIAWI 428
Cdd:cd03230 1 IEVRNLSKRYGK-KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 429 PQKPTLFYD-TLAANIKLgnpsashealehaakqagalefinelpdgfntligeqgeglSGGQKQRIALARAFLKHAPIL 507
Cdd:cd03230 79 PEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1590405536 508 VLDEPTAHLDSQTEQLIQNAIAEYAK-NHLVITIAHRLNTVKN-AKQLIVMENGCI 561
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKKeGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
378-583 |
5.78e-28 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 120.08 E-value: 5.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 378 VAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAWIPQKPTLFYDTLAANIklgNPSASHE--AL 455
Cdd:PLN03232 1265 VGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI---DPFSEHNdaDL 1341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 456 EHAAKQAGALEFINELPDGFNTLIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNH 535
Cdd:PLN03232 1342 WEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSC 1421
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1590405536 536 LVITIAHRLNTVKNAKQLIVMENGCIVQQGDFKA-LSQQSGEFAKLLQT 583
Cdd:PLN03232 1422 TMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQElLSRDTSAFFRMVHS 1470
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
349-542 |
1.08e-27 |
|
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: 111.02 E-value: 1.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSNEG---INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPlttanISQLQQSI 425
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP-----VTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 426 AWIPQKPTLF-YDTLAANIKLG------NPSASHEALEHAAKQAGALEFINELPDgfntligeQgegLSGGQKQRIALAR 498
Cdd:cd03293 76 GYVFQQDALLpWLTVLDNVALGlelqgvPKAEARERAEELLELVGLSGFENAYPH--------Q---LSGGMRQRVALAR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1590405536 499 AFLKHAPILVLDEPTAHLDSQTEQLIQNAIAE-YAKNHL-VITIAH 542
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDiWRETGKtVLLVTH 190
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
349-581 |
5.11e-27 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 109.46 E-value: 5.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSnegINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIawI 428
Cdd:COG3840 2 LRLDDLTYRYGDF---PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSM--L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 429 PQKPTLF-YDTLAANIKLG-NPS-----ASHEALEHAAKQAGALEFINELPdgfntligeqgEGLSGGQKQRIALARAFL 501
Cdd:COG3840 77 FQENNLFpHLTVAQNIGLGlRPGlkltaEQRAQVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 502 KHAPILVLDEPTAHLD----SQTEQLIQNAIAEYakNHLVITIAHRLNTVKN-AKQLIVMENGCIVQQGDFKALSQQ--S 574
Cdd:COG3840 146 RKRPILLLDEPFSALDpalrQEMLDLVDELCRER--GLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGepP 223
|
....*..
gi 1590405536 575 GEFAKLL 581
Cdd:COG3840 224 PALAAYL 230
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
324-558 |
6.02e-27 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 116.67 E-value: 6.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 324 IILNAPLPENDDSHTANINIdanNTISIHDLNFSYPNSN--EGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPE 401
Cdd:PTZ00265 361 IINRKPLVENNDDGKKLKDI---KKIQFKNVRFHYDTRKdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDP 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 402 VIQHISI-DQQPLTTANISQLQQSIAWIPQKPTLFYDTLAANIKLG----------------NPSASHEALEHA----AK 460
Cdd:PTZ00265 438 TEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyneDGNDSQENKNKRnscrAK 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 461 QAGAL-------------------------------------EFINELPDGFNTLIGEQGEGLSGGQKQRIALARAFLKH 503
Cdd:PTZ00265 518 CAGDLndmsnttdsneliemrknyqtikdsevvdvskkvlihDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRN 597
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1590405536 504 APILVLDEPTAHLDSQTEQLIQNAIAEYA--KNHLVITIAHRLNTVKNAKQLIVMEN 558
Cdd:PTZ00265 598 PKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSN 654
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
349-559 |
1.04e-26 |
|
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: 108.19 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLG----FHPEVIQHISIDQQPLTTANISQLQQS 424
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGemqtLEGKVHWSNKNESEPSFEATRSRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 425 IAWIPQKPTLFYDTLAANIKLGNPSASHEAleHAAKQAGALE-FINELPDGFNTLIGEQGEGLSGGQKQRIALARAFLKH 503
Cdd:cd03290 81 VAYAAQKPWLLNATVEENITFGSPFNKQRY--KAVTDACSLQpDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQN 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1590405536 504 APILVLDEPTAHLDSQ-TEQLIQNAIAEYAKN--HLVITIAHRLNTVKNAKQLIVMENG 559
Cdd:cd03290 159 TNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
32-302 |
2.82e-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: 2.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 32 LSIALGTVNAILMIAGAYLLAQTIhEVMFEGRNLA--QVTQYLWPLAGIILLRALFLALSERLSAFATLKIKSAIRQTLL 109
Cdd:pfam00664 3 LAILLAILSGAISPAFPLVLGRIL-DVLLPDGDPEtqALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 110 DKLTQLGPSYIEKNGQGATLNTLHNGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMILV 189
Cdd:pfam00664 82 KKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 190 GHKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATRKELKQIARISDDFRHATLNVLKIAFLSSFALEFLATISVAL 269
Cdd:pfam00664 162 AKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYAL 241
|
250 260 270
....*....|....*....|....*....|...
gi 1590405536 270 VAVIIGFRLFFGTLDFATGFVVLLLAPEFYLPL 302
Cdd:pfam00664 242 ALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
349-559 |
4.74e-26 |
|
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: 106.03 E-value: 4.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSNEGI---NNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQL---- 421
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqalKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 422 QQSIAWIPQKPTLFyDTLAA--NIKL-----GNPSAS-HEALEHAAKQAGalefineLPDGFNTLIGEqgegLSGGQKQR 493
Cdd:cd03255 81 RRHIGFVFQSFNLL-PDLTAleNVELplllaGVPKKErRERAEELLERVG-------LGDRLNHYPSE----LSGGQQQR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1590405536 494 IALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAK--NHLVITIAHRLNTVKNAKQLIVMENG 559
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
378-583 |
5.92e-26 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 113.68 E-value: 5.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 378 VAIVGASGSGKSTLLDCMLGF-HPEVIQhISIDQQPLTTANISQLQQSIAWIPQKPTLFYDTLAANIklgNPSASH---- 452
Cdd:PLN03130 1268 VGIVGRTGAGKSSMLNALFRIvELERGR-ILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL---DPFNEHndad 1343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 453 --EALEHAAKQagalEFINELPDGFNTLIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAE 530
Cdd:PLN03130 1344 lwESLERAHLK----DVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIRE 1419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1590405536 531 YAKNHLVITIAHRLNTVKNAKQLIVMENGCIVQQGD-FKALSQQSGEFAKLLQT 583
Cdd:PLN03130 1420 EFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTpENLLSNEGSAFSKMVQS 1473
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
367-534 |
6.12e-26 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 105.64 E-value: 6.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 367 NINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTAnISQLQQSIAWIPQKPTLFYD-TLAANI-- 443
Cdd:COG4133 20 GLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDA-REDYRRRLAYLGHADGLKPElTVRENLrf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 444 --KLGNPSASHEALEHAAKQAGalefineLPDGFNTLIGEqgegLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTE 521
Cdd:COG4133 99 waALYGLRADREAIDEALEAVG-------LAGLADLPVRQ----LSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGV 167
|
170
....*....|...
gi 1590405536 522 QLIQNAIAEYAKN 534
Cdd:COG4133 168 ALLAELIAAHLAR 180
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
349-566 |
9.54e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 107.00 E-value: 9.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNS-NEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAW 427
Cdd:PRK13632 8 IKVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 428 IPQKPtlfyD------TLAANIKLG------NPSASHEALEHAAKQAGALEFINELPdgfntligeqgEGLSGGQKQRIA 495
Cdd:PRK13632 88 IFQNP----DnqfigaTVEDDIAFGlenkkvPPKKMKDIIDDLAKKVGMEDYLDKEP-----------QNLSGGQKQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1590405536 496 LARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAK--NHLVITIAHRLNTVKNAKQLIVMENGCIVQQGD 566
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrKKTLISITHDMDEAILADKVIVFSEGKLIAQGK 225
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
349-565 |
9.83e-26 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 104.97 E-value: 9.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSnEGINNINLTLPsTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPlTTANISQLQQSIAWI 428
Cdd:cd03264 1 LQLENLTKRYGKK-RALDGVSLTLG-PGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQD-VLKQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 429 PQKPTL--------FYDTLAAnIKLGNPSASHEALEHAakqagaLEFINeLPDGFNTLIGeqgeGLSGGQKQRIALARAF 500
Cdd:cd03264 78 PQEFGVypnftvreFLDYIAW-LKGIPSKEVKARVDEV------LELVN-LGDRAKKKIG----SLSGGMRRRVGIAQAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1590405536 501 LKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIAHRLNTVKN-AKQLIVMENGCIVQQG 565
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
349-566 |
3.48e-25 |
|
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: 109.22 E-value: 3.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSNEG----INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTT---ANISQL 421
Cdd:COG1123 261 LEVRNLSKRYPVRGKGgvraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlsrRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 422 QQSIAWIPQKPT--LF-----YDTLA---ANIKLGNPSASHEALEHAAKQAG-ALEFINELPdgfntligeqGEgLSGGQ 490
Cdd:COG1123 341 RRRVQMVFQDPYssLNprmtvGDIIAeplRLHGLLSRAERRERVAELLERVGlPPDLADRYP----------HE-LSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 491 KQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNH----LVITiaHRLNTVKN-AKQLIVMENGCIVQQG 565
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELgltyLFIS--HDLAVVRYiADRVAVMYDGRIVEDG 487
|
.
gi 1590405536 566 D 566
Cdd:COG1123 488 P 488
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
349-565 |
1.33e-24 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 101.80 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSNEginNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQlqQSIAWI 428
Cdd:cd03298 1 VRLDKIRFSYGEQPM---HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 429 PQKPTLF-YDTLAANIKLG-NPS-----ASHEALEHAAKQAGALEFINELPDGfntligeqgegLSGGQKQRIALARAFL 501
Cdd:cd03298 76 FQENNLFaHLTVEQNVGLGlSPGlkltaEDRQAIEVALARVGLAGLEKRLPGE-----------LSGGERQRVALARVLV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1590405536 502 KHAPILVLDEPTAHLD----SQTEQLIQNAIAEyAKNHLVITIAHRLNTVKNAKQLIVMENGCIVQQG 565
Cdd:cd03298 145 RDKPVLLLDEPFAALDpalrAEMLDLVLDLHAE-TKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
349-565 |
2.55e-24 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 102.91 E-value: 2.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSY----PNSNEGINNINLTLPSTGLVAIVGASGSGKSTLldcmlgfhpevIQH-----------ISIDQQPL 413
Cdd:TIGR04521 1 IKLKNVSYIYqpgtPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTL-----------IQHlngllkptsgtVTIDGRDI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 414 TT---ANISQLQQSIAWIPQKP--TLFYDTLAANIKLG--NPSASHEALEHAAKQAgaLEFINeLPDG------FNtlig 480
Cdd:TIGR04521 70 TAkkkKKLKDLRKKVGLVFQFPehQLFEETVYKDIAFGpkNLGLSEEEAEERVKEA--LELVG-LDEEylerspFE---- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 481 eqgegLSGGQKQRIALArAFLKHAP-ILVLDEPTAHLDSQTEQLIQNAIAEYAK--NHLVITIAHRLNTV-KNAKQLIVM 556
Cdd:TIGR04521 143 -----LSGGQMRRVAIA-GVLAMEPeVLILDEPTAGLDPKGRKEILDLFKRLHKekGLTVILVTHSMEDVaEYADRVIVM 216
|
....*....
gi 1590405536 557 ENGCIVQQG 565
Cdd:TIGR04521 217 HKGKIVLDG 225
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
349-561 |
3.77e-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: 100.68 E-value: 3.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYpNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFhpEVIQ--HISIDQQPLT--TANISQLQQS 424
Cdd:cd03262 1 IEIKNLHKSF-GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLL--EEPDsgTIIIDGLKLTddKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 425 IAWIPQKPTLF-YDTLAANIKLGnP-----SASHEALEHAA---KQAGALEFINELPDGfntligeqgegLSGGQKQRIA 495
Cdd:cd03262 78 VGMVFQQFNLFpHLTVLENITLA-PikvkgMSKAEAEERALellEKVGLADKADAYPAQ-----------LSGGQQQRVA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1590405536 496 LARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHL-VITIAHRLNTVKN-AKQLIVMENGCI 561
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMtMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
32-323 |
9.65e-24 |
|
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: 101.73 E-value: 9.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 32 LSIALGTVNAILMIAGAYLLAQTIHEVmFEGRNLAQVTQYLWPLAGIILLRALFLALSERLSAFATLKIKSAIRQTLLDK 111
Cdd:cd18552 3 LAILGMILVAATTAALAWLLKPLLDDI-FVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 112 LTQLGPSYIEKNGQGATLNTLHNGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMILVGH 191
Cdd:cd18552 82 LLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 192 KAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATRKELKQIARISDDFRHATLNVLKIAFLSSFALEFLATISVALVA 271
Cdd:cd18552 162 RLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALVL 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1590405536 272 VIIGFRLFFGTLDFAT--GFVVLLLApeFYLPLRQLGShYHARLQGISAAADML 323
Cdd:cd18552 242 WYGGYQVISGELTPGEfiSFITALLL--LYQPIKRLSN-VNANLQRGLAAAERI 292
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
349-586 |
1.47e-23 |
|
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: 100.70 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNS-NEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFhPEVIQHISIDQQPLTTANISQLQQSIAW 427
Cdd:cd03289 3 MTVKDLTAKYTEGgNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 428 IPQKPTLFYDTLAANIklgNPSASH--EALEHAAKQAGALEFINELPDGFNTLIGEQGEGLSGGQKQRIALARAFLKHAP 505
Cdd:cd03289 82 IPQKVFIFSGTFRKNL---DPYGKWsdEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 506 ILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIAHRLNTVKNAKQLIVMENGCIVQQGDFKALSQQSGEFAKLLQTAE 585
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAISPSD 238
|
.
gi 1590405536 586 Q 586
Cdd:cd03289 239 R 239
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
349-559 |
2.06e-23 |
|
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: 97.26 E-value: 2.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYpNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTT--ANISQLQQSIA 426
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDleDELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 427 WIPQKPTLFydtlaaniklgnpsaSH-EALEHAAkqagalefinelpdgfntligeqgEGLSGGQKQRIALARAFLKHAP 505
Cdd:cd03229 80 MVFQDFALF---------------PHlTVLENIA------------------------LGLSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1590405536 506 ILVLDEPTAHLDSQTEQLIQNAIAEYAKNH--LVITIAHRLNTVKN-AKQLIVMENG 559
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQLgiTVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
378-581 |
2.21e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 98.89 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 378 VAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAWipQKPTLF-YDTLAANIKLG-NP-----SA 450
Cdd:PRK10771 28 VAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLF--QENNLFsHLTVAQNIGLGlNPglklnAA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 451 SHEALEHAAKQAGALEFINELPdgfntligeqGEgLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQ----LIQN 526
Cdd:PRK10771 106 QREKLHAIARQMGIEDLLARLP----------GQ-LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQemltLVSQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1590405536 527 AIAEyaKNHLVITIAHRL-NTVKNAKQLIVMENGCIVQQGDFKALSQQSGEFAKLL 581
Cdd:PRK10771 175 VCQE--RQLTLLMVSHSLeDAARIAPRSLVVADGRIAWDGPTDELLSGKASASALL 228
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
350-562 |
2.84e-23 |
|
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: 97.71 E-value: 2.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 350 SIHDLNFSYPNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPlttANISQLQQSIAWIP 429
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP---IKAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 430 QKPT--LFYDTLAANIKLGNP--SASHEALEHAAKQAGALEFINELPdgfntligeqgEGLSGGQKQRIALARAFLKHAP 505
Cdd:cd03226 78 QDVDyqLFTDSVREELLLGLKelDAGNEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1590405536 506 ILVLDEPTAHLDSQTEQLIQNAIAEYAK-NHLVITIAHRLNTVKN-AKQLIVMENGCIV 562
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELAAqGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
348-562 |
3.09e-23 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 98.17 E-value: 3.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 348 TISIHDLNFSYPNSN---EGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQ- 423
Cdd:TIGR02982 1 VISIRNLNHYYGHGSlrkQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 424 --SIAWIPQKPTLFyDTLAA--NIKLG---NPSASHEALEHAAKQ----AGALEFINELPDGfntligeqgegLSGGQKQ 492
Cdd:TIGR02982 81 rrRIGYIFQAHNLL-GFLTArqNVQMAlelQPNLSYQEARERARAmleaVGLGDHLNYYPHN-----------LSGGQKQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1590405536 493 RIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNH----LVITIAHRLNTVknAKQLIVMENGCIV 562
Cdd:TIGR02982 149 RVAIARALVHHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQgctiLMVTHDNRILDV--ADRILQMEDGKLL 220
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
349-562 |
4.70e-23 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 98.59 E-value: 4.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQ---SI 425
Cdd:COG3638 3 LELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRlrrRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 426 AWIPQKPTLFYD-TLAANI---KLGNPS---------------ASHEALE------HAAKQAGALefinelpdgfntlig 480
Cdd:COG3638 83 GMIFQQFNLVPRlSVLTNVlagRLGRTStwrsllglfppedreRALEALErvgladKAYQRADQL--------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 481 eqgeglSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNH---LVITIaHRLNTVKN-AKQLIVM 556
Cdd:COG3638 148 ------SGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDgitVVVNL-HQVDLARRyADRIIGL 220
|
....*.
gi 1590405536 557 ENGCIV 562
Cdd:COG3638 221 RDGRVV 226
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
32-319 |
5.31e-23 |
|
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: 99.38 E-value: 5.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 32 LSIALGTVNAILMIAGAYLLAQTI-HEVMFEGRNLAQVTQYLWPLAGIILLRALFLALSERLSAFATLKIKSAIRQTLLD 110
Cdd:cd18544 3 LALLLLLLATALELLGPLLIKRAIdDYIVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 111 KLTQLGPSYIEKNGQGATLNTLHNGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMILVG 190
Cdd:cd18544 83 HIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 191 HKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATRKELKQIARISDDFRHATLNVLKIAFLSSFALEFLATISVALV 270
Cdd:cd18544 163 KKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALV 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1590405536 271 AVIIGFRLFFGTLDFATGFVVLLLAPEFYLPLRQLGSHYHARLQGISAA 319
Cdd:cd18544 243 LWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASA 291
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
369-566 |
5.55e-23 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 97.24 E-value: 5.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 369 NLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAWipQKPTLF-YDTLAANIKLG- 446
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLF--QENNLFaHLTVRQNIGLGl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 447 NPS-----ASHEALEHAAKQAGALEFINELPdgfntligeqgEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTE 521
Cdd:TIGR01277 96 HPGlklnaEQQEKVVDAAQQVGIADYLDRLP-----------EQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1590405536 522 QLIQNAIAEYA--KNHLVITIAHRL-NTVKNAKQLIVMENGCIVQQGD 566
Cdd:TIGR01277 165 EEMLALVKQLCseRQRTLLMVTHHLsDARAIASQIAVVSQGKIKVVSD 212
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
349-570 |
8.58e-23 |
|
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: 97.19 E-value: 8.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYpNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQS---I 425
Cdd:cd03261 1 IELRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrrrM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 426 AWIPQKPTLFYD-TLAANIKLgnPSASHEALEHAAKQAGALEFINE--LPDGFNTLIGEqgegLSGGQKQRIALARAFLK 502
Cdd:cd03261 80 GMLFQSGALFDSlTVFENVAF--PLREHTRLSEEEIREIVLEKLEAvgLRGAEDLYPAE----LSGGMKKRVALARALAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1590405536 503 HAPILVLDEPTAHLDSQTEQLIQNAIAEY--AKNHLVITIAHRLNTV-KNAKQLIVMENGCIVQQGDFKAL 570
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
349-566 |
1.11e-22 |
|
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: 103.45 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSNEGI-NNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFhPEVIQHISIDQQPLTTANISQLQQSIAW 427
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAVlQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 428 IPQKPTLFYDTLAANIklgNPSA--SHEALEHAAKQAGALEFINELPDGFNTLIGEQGEGLSGGQKQRIALARAFLKHAP 505
Cdd:TIGR01271 1297 IPQKVFIFSGTFRKNL---DPYEqwSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAK 1373
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1590405536 506 ILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIAHRLNTVKNAKQLIVMEnGCIVQQGD 566
Cdd:TIGR01271 1374 ILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIE-GSSVKQYD 1433
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
378-574 |
1.23e-22 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 103.32 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 378 VAIVGASGSGKSTLLdcmLGFHP--EVIQ-HISIDQQPLTTANISQLQQSIAWIPQKPTLFYDTLAANIklgNP--SASH 452
Cdd:PTZ00243 1339 VGIVGRTGSGKSTLL---LTFMRmvEVCGgEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV---DPflEASS 1412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 453 EALEHAAKQAGALEFINELPDGFNTLIGEQGEGLSGGQKQRIALARAFLKHAPILVL-DEPTAHLDSQTEQLIQNAIAEY 531
Cdd:PTZ00243 1413 AEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMSA 1492
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1590405536 532 AKNHLVITIAHRLNTVKNAKQLIVMENGCIVQQGDFK--ALSQQS 574
Cdd:PTZ00243 1493 FSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRelVMNRQS 1537
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
348-565 |
2.98e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 96.38 E-value: 2.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 348 TISIHDLNFSYpNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAW 427
Cdd:PRK13548 2 MLEARNLSVRL-GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 428 IPQKPTL-FYDTLAANIKLG------NPSASHEALEHAAKQAGALEFINELpdgFNTligeqgegLSGGQKQRIALARAF 500
Cdd:PRK13548 81 LPQHSSLsFPFTVEEVVAMGraphglSRAEDDALVAAALAQVDLAHLAGRD---YPQ--------LSGGEQQRVQLARVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1590405536 501 --LKHA----PILVLDEPTAHLDSQTEQLIQNAIAEYAKNH--LVITIAHRLN-TVKNAKQLIVMENGCIVQQG 565
Cdd:PRK13548 150 aqLWEPdgppRWLLLDEPTSALDLAHQHHVLRLARQLAHERglAVIVVLHDLNlAARYADRIVLLHQGRLVADG 223
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
349-565 |
5.45e-22 |
|
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: 95.96 E-value: 5.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSNE-GINNINLTLPSTGLVAIVGASGSGKSTL---LDCML----GfhpeviqHISID-QQPLTTANIS 419
Cdd:TIGR04520 1 IEVENVSFSYPESEKpALKNVSLSIEKGEFVAIIGHNGSGKSTLaklLNGLLlptsG-------KVTVDgLDTLDEENLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 420 QLQQSIAWIPQKP------TLFYDTLA---ANIKLgNPSASHEALEHAAKQAGALEFINELPdgfntligeqgEGLSGGQ 490
Cdd:TIGR04520 74 EIRKKVGMVFQNPdnqfvgATVEDDVAfglENLGV-PREEMRKRVDEALKLVGMEDFRDREP-----------HLLSGGQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590405536 491 KQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAE-YAKNHL-VITIAHRLNTVKNAKQLIVMENGCIVQQG 565
Cdd:TIGR04520 142 KQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKlNKEEGItVISITHDMEEAVLADRVIVMNKGKIVAEG 218
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
344-565 |
5.60e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 95.97 E-value: 5.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 344 DANNTISIHDLNFSYpNSNEG--INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQL 421
Cdd:PRK13648 3 DKNSIIVFKNVSFQY-QSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 422 QQSIAWIPQKP-------TLFYDTLaanIKLGNPSASHEALEHAAKQA----GALEFINELPdgfntligeqgEGLSGGQ 490
Cdd:PRK13648 82 RKHIGIVFQNPdnqfvgsIVKYDVA---FGLENHAVPYDEMHRRVSEAlkqvDMLERADYEP-----------NALSGGQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590405536 491 KQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLV--ITIAHRLNTVKNAKQLIVMENGCIVQQG 565
Cdd:PRK13648 148 KQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNItiISITHDLSEAMEADHVIVMNKGTVYKEG 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
349-566 |
8.00e-22 |
|
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: 94.57 E-value: 8.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSNEGI---NNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQL---Q 422
Cdd:cd03258 2 IELKNVSKVFGDTGGKVtalKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 423 QSIAWIPQKPTLFYD-TLAANIKLgnpsasheALEHA-AKQAGALEFINELPDgfntLIGEQGEG------LSGGQKQRI 494
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVAL--------PLEIAgVPKAEIEERVLELLE----LVGLEDKAdaypaqLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1590405536 495 ALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNhLVIT---IAHRLNTVKN-AKQLIVMENGCIVQQGD 566
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETTQSILALLRDINRE-LGLTivlITHEMEVVKRiCDRVAVMEKGEVVEEGT 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
344-544 |
8.75e-22 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 95.10 E-value: 8.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 344 DANNTISIHDLNFSYpNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDC---MLGFHPEV-IQ-HISIDQQPL--TTA 416
Cdd:COG1117 7 TLEPKIEVRNLNVYY-GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrMNDLIPGArVEgEILLDGEDIydPDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 417 NISQLQQSIAWIPQKPTLF----YDTLAANIKLG---NPSASHEALEHAAKQAgALefINELPDGFNtligEQGEGLSGG 489
Cdd:COG1117 86 DVVELRRRVGMVFQKPNPFpksiYDNVAYGLRLHgikSKSELDEIVEESLRKA-AL--WDEVKDRLK----KSALGLSGG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1590405536 490 QKQRIALARAfLKHAP-ILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIAHRL 544
Cdd:COG1117 159 QQQRLCIARA-LAVEPeVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNM 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
349-562 |
2.28e-21 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 92.81 E-value: 2.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLG-FHPEVIQhISIDQQPLTT---ANISQLQQS 424
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGeERPTSGQ-VLVNGQDLSRlkrREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 425 IAWIPQKPTLFYD-TLAANIKLG------NPSASHEALEHAAKQAGALEFINELPDgfntligEqgegLSGGQKQRIALA 497
Cdd:COG2884 81 IGVVFQDFRLLPDrTVYENVALPlrvtgkSRKEIRRRVREVLDLVGLSDKAKALPH-------E----LSGGEQQRVAIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590405536 498 RAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIA-HRLNTVKNA-KQLIVMENGCIV 562
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMpKRVLELEDGRLV 216
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
344-565 |
3.86e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 93.54 E-value: 3.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 344 DANNTISIHDLNFSYPNSNE-GINNINLTLPSTGLVAIVGASGSGKSTLLDCMLG-FHPEViQHISIDQQPLTTANISQL 421
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAATyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGlLLPEA-GTITVGGMVLSEETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 422 QQSIAWIPQKP------TLFYDTLAanIKLGNPSASH----EALEHAAKQAGALEFINELPdgfntligeqgEGLSGGQK 491
Cdd:PRK13635 80 RRQVGMVFQNPdnqfvgATVQDDVA--FGLENIGVPReemvERVDQALRQVGMEDFLNREP-----------HRLSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1590405536 492 QRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEY--AKNHLVITIAHRLNTVKNAKQLIVMENGCIVQQG 565
Cdd:PRK13635 147 QRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLkeQKGITVLSITHDLDEAAQADRVIVMNKGEILEEG 222
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
18-511 |
4.12e-21 |
|
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: 97.18 E-value: 4.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 18 FLKQQSKPaamWLKLSIALGTVNAIlmiAGAYLLAqTIHEVMFEGRNLAqvTQYLWPLAGIILLRALFLALSERLSAFAT 97
Cdd:COG4615 6 LLLRESRW---LLLLALLLGLLSGL---ANAGLIA-LINQALNATGAAL--ARLLLLFAGLLVLLLLSRLASQLLLTRLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 98 LKIKSAIRQTLLDKLTQLGPSYIEKNGQGATLNTLHNGVEALHDYyAKYLPGVAYSALIPLAILVVIFptdYKAGLIFLL 177
Cdd:COG4615 77 QHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQA-FVRLPELLQSVALVLGCLAYLA---WLSPPLFLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 178 TAPLIpFFMILVGHKAEALNQKRWQQLAVLGNYFFDRVQGLTQ----LKLFNATRKEL--KQIARISDDFRHATLNVLKI 251
Cdd:COG4615 153 TLVLL-GLGVAGYRLLVRRARRHLRRAREAEDRLFKHFRALLEgfkeLKLNRRRRRAFfdEDLQPTAERYRDLRIRADTI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 252 aFLSSFAleFLATISVALVAVIIGFRLFFGTLDFA--TGFVVLLLapefYL--PLRQLGSHYHARLQGiSAAADMLIILN 327
Cdd:COG4615 232 -FALANN--WGNLLFFALIGLILFLLPALGWADPAvlSGFVLVLL----FLrgPLSQLVGALPTLSRA-NVALRKIEELE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 328 APLPENDDSHTANINIDAN---NTISIHDLNFSYPNSNEG----INNINLTLPSTGLVAIVGASGSGKSTLLDCMLG-FH 399
Cdd:COG4615 304 LALAAAEPAAADAAAPPAPadfQTLELRGVTYRYPGEDGDegftLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGlYR 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 400 PEViQHISIDQQPLTTANISQLQQSIAWIPQKPTLFYDTLAANIKLGNPSASH--EALEHAAKqagaLEFINelpDGFNT 477
Cdd:COG4615 384 PES-GEILLDGQPVTADNREAYRQLFSAVFSDFHLFDRLLGLDGEADPARAREllERLELDHK----VSVED---GRFST 455
|
490 500 510
....*....|....*....|....*....|....
gi 1590405536 478 LigeqgeGLSGGQKQRIALARAFLKHAPILVLDE 511
Cdd:COG4615 456 T------DLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
349-570 |
5.96e-21 |
|
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: 91.96 E-value: 5.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYpNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQ------ 422
Cdd:COG1127 6 IEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrrri 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 423 ----QSIAwipqkptLFYD-TLAANIKLG---NPSASHEALEHAAKQagALEFINeLPDGFNTLIGEqgegLSGGQKQRI 494
Cdd:COG1127 85 gmlfQGGA-------LFDSlTVFENVAFPlreHTDLSEAEIRELVLE--KLELVG-LPGAADKMPSE----LSGGMRKRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1590405536 495 ALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEY-AKNHL-VITIAHRLNTVKN-AKQLIVMENGCIVQQGDFKAL 570
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLDPITSAVIDELIRELrDELGLtSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEEL 229
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
367-581 |
6.78e-21 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 92.01 E-value: 6.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 367 NINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTtaNISQLQQSIAWIPQKPTLF-----YDTLAA 441
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISYVPQNYALFphmtvYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 442 NIK--LGNPSASHEALEHAAKQAGALEFINELPdgfntligeqgEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQ 519
Cdd:cd03299 95 GLKkrKVDKKEIERKVLEIAEMLGIDHLLNRKP-----------ETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1590405536 520 TEQLIQNAIAEYAKNH--LVITIAHRLNTVKN-AKQLIVMENGCIVQQGD----FKalSQQSGEFAKLL 581
Cdd:cd03299 164 TKEKLREELKKIRKEFgvTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKpeevFK--KPKNEFVAEFL 230
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
349-565 |
9.93e-21 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 91.59 E-value: 9.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTAN---ISQLQQSI 425
Cdd:TIGR02315 2 LEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRgkkLRKLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 426 AWIPQKPTLFYD-TLAANIKLGNpSASHEALE------HAAKQAGALEFINELpdGFNTLIGEQGEGLSGGQKQRIALAR 498
Cdd:TIGR02315 82 GMIFQHYNLIERlTVLENVLHGR-LGYKPTWRsllgrfSEEDKERALSALERV--GLADKAYQRADQLSGGQQQRVAIAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 499 AFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIA--HRLNTVKN-AKQLIVMENGCIVQQG 565
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIInlHQVDLAKKyADRIVGLKAGEIVFDG 228
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
365-565 |
1.44e-20 |
|
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: 90.79 E-value: 1.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLD---CMLGFHPEVIQHISIDQQPLttaNISQLQQSIAWIPQK----PTL-FY 436
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDaisGRVEGGGTTSGQILFNGQPR---KPDQFQKCVAYVRQDdillPGLtVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 437 DTL--AANIKLGNPSAShealehaaKQAGALEFINELPDGFNTLIGEQG-EGLSGGQKQRIALARAFLKHAPILVLDEPT 513
Cdd:cd03234 100 ETLtyTAILRLPRKSSD--------AIRKKRVEDVLLRDLALTRIGGNLvKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1590405536 514 AHLDSQTEQLIQNAIAEYAK-NHLVITIAH--RLNTVKNAKQLIVMENGCIVQQG 565
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARrNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
348-565 |
2.80e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 91.26 E-value: 2.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 348 TISIHDLNFSY----PNSNEGINNINLTLPSTGLVAIVGASGSGKSTLldcmlgfhpevIQH-----------ISIDQQP 412
Cdd:PRK13637 2 SIKIENLTHIYmegtPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTL-----------IQHlngllkptsgkIIIDGVD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 413 LT--TANISQLQQSIAWIPQKP--TLFYDTLAANIKLG--NPSASHEALEHAAKQAgalefINELPDGFNTLIGEQGEGL 486
Cdd:PRK13637 71 ITdkKVKLSDIRKKVGLVFQYPeyQLFEETIEKDIAFGpiNLGLSEEEIENRVKRA-----MNIVGLDYEDYKDKSPFEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 487 SGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAK--NHLVITIAHRLNTV-KNAKQLIVMENGCIVQ 563
Cdd:PRK13637 146 SGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVaKLADRIIVMNKGKCEL 225
|
..
gi 1590405536 564 QG 565
Cdd:PRK13637 226 QG 227
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
349-573 |
2.98e-20 |
|
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: 90.32 E-value: 2.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQS---I 425
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrqI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 426 AWIPQKPTLFYD-TLAANI---KLGNPSA--SHEALEHAAKQAGALEFINE--LPDGFNTLIGEqgegLSGGQKQRIALA 497
Cdd:cd03256 81 GMIFQQFNLIERlSVLENVlsgRLGRRSTwrSLFGLFPKEEKQRALAALERvgLLDKAYQRADQ----LSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1590405536 498 RAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIA--HRLNTVK-NAKQLIVMENGCIVQQGDFKALSQQ 573
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVslHQVDLAReYADRIVGLKDGRIVFDGPPAELTDE 235
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
349-565 |
4.09e-20 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 90.17 E-value: 4.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYpNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAWI 428
Cdd:COG4559 2 LEAENLSVRL-GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 429 PQKPTL-FYDTLAANIKLG------NPSASHEALEHAAKQAGALEFINELpdgFNTLigeqgeglSGGQKQRIALARAF- 500
Cdd:COG4559 81 PQHSSLaFPFTVEEVVALGraphgsSAAQDRQIVREALALVGLAHLAGRS---YQTL--------SGGEQQRVQLARVLa 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1590405536 501 -LKHAP-----ILVLDEPTAHLDSQTEQLIQNAIAEYAKNHL-VITIAHRLN-TVKNAKQLIVMENGCIVQQG 565
Cdd:COG4559 150 qLWEPVdggprWLFLDEPTSALDLAHQHAVLRLARQLARRGGgVVAVLHDLNlAAQYADRILLLHQGRLVAQG 222
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
349-566 |
4.58e-20 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 89.67 E-value: 4.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYpNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFhpEVIQ--HISIDQQPLT--TANISQLQQS 424
Cdd:COG1126 2 IEIENLHKSF-GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLL--EEPDsgTITVDGEDLTdsKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 425 IAWIPQKPTLFYD-TLAANIKLGnPSASH-----EALEHAAK---QAGALEFINELPDgfntligeQgegLSGGQKQRIA 495
Cdd:COG1126 79 VGMVFQQFNLFPHlTVLENVTLA-PIKVKkmskaEAEERAMElleRVGLADKADAYPA--------Q---LSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 496 LARAfLKHAP-ILVLDEPTAHLDSQTEQLIQNAIAEYAKNH---LVIT--------IAHRlntvknakqLIVMENGCIVQ 563
Cdd:COG1126 147 IARA-LAMEPkVMLFDEPTSALDPELVGEVLDVMRDLAKEGmtmVVVThemgfareVADR---------VVFMDGGRIVE 216
|
...
gi 1590405536 564 QGD 566
Cdd:COG1126 217 EGP 219
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
348-565 |
5.40e-20 |
|
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: 87.99 E-value: 5.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 348 TISIHDLNFSYPNSNEG-----INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEViqHIS----IDQQPLTtanI 418
Cdd:cd03213 3 TLSFRNLTVTVKSSPSKsgkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGL--GVSgevlINGRPLD---K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 419 SQLQQSIAWIPQKpTLFYDTLAAniklgnpsasHEALEHAAKQagalefinelpdgfntligeqgEGLSGGQKQRIALAR 498
Cdd:cd03213 78 RSFRKIIGYVPQD-DILHPTLTV----------RETLMFAAKL----------------------RGLSGGERKRVSIAL 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 499 AFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAK-NHLVITIAHRLNT--VKNAKQLIVMENGCIVQQG 565
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADtGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
349-565 |
5.50e-20 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 89.28 E-value: 5.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDcMLGfhpEVIQH----ISIDQQPLTTANISQLQQS 424
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMK-MIN---RLIEPtsgeIFIDGEDIREQDPVELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 425 IAWIPQKPTLF-YDTLAANIKLgNPSASHEALEHAAKQAGALEFINELPDGfnTLIGEQGEGLSGGQKQRIALARAFLKH 503
Cdd:cd03295 77 IGYVIQQIGLFpHMTVEENIAL-VPKLLKWPKEKIRERADELLALVGLDPA--EFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1590405536 504 APILVLDEPTAHLDSQTEQLIQNAIAEYAK--NHLVITIAHRLN-TVKNAKQLIVMENGCIVQQG 565
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVG 218
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
348-565 |
7.98e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 89.30 E-value: 7.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 348 TISIHDLNFSYPNSNEgINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAW 427
Cdd:PRK11231 2 TLRTENLTVGYGTKRI-LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 428 IPQKPTLFYD-TLAANIKLG-NPSASH-----EALEHAAKQAGALEFINELPDgfntligEQGEGLSGGQKQRIALARAF 500
Cdd:PRK11231 81 LPQHHLTPEGiTVRELVAYGrSPWLSLwgrlsAEDNARVNQAMEQTRINHLAD-------RRLTDLSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 501 LKHAPILVLDEPTAHLD--SQTE--QLIQNAIAEyakNHLVITIAHRLNTV-KNAKQLIVMENGCIVQQG 565
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDinHQVElmRLMRELNTQ---GKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQG 220
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
346-581 |
8.49e-20 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 89.92 E-value: 8.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 346 NNTISIHDLNFSYPN----SNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLG-FHPE--VIQHisidqqpltTANI 418
Cdd:cd03291 30 DRKHSSDDNNLFFSNlclvGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGeLEPSegKIKH---------SGRI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 419 SQLQQsIAWIpqkptlFYDTLAANIKLGnpsASHEALEH-AAKQAGALEF-INELPDGFNTLIGEQGEGLSGGQKQRIAL 496
Cdd:cd03291 101 SFSSQ-FSWI------MPGTIKENIIFG---VSYDEYRYkSVVKACQLEEdITKFPEKDNTVLGEGGITLSGGQRARISL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 497 ARAFLKHAPILVLDEPTAHLDSQTE-QLIQNAIAEYAKNHLVITIAHRLNTVKNAKQLIVMENGCIVQQGDFKALSQQSG 575
Cdd:cd03291 171 ARAVYKDADLYLLDSPFGYLDVFTEkEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRP 250
|
....*.
gi 1590405536 576 EFAKLL 581
Cdd:cd03291 251 DFSSKL 256
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
367-565 |
9.14e-20 |
|
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: 88.12 E-value: 9.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 367 NINLTLPsTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTA----NISQLQQSIAWIPQKPTLF-YDTLAA 441
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSrkkiNLPPQQRKIGLVFQQYALFpHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 442 NIKLGNPSAShealehaakQAGALEFINELPDGFN--TLIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQ 519
Cdd:cd03297 95 NLAFGLKRKR---------NREDRISVDELLDLLGldHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1590405536 520 TEQLIQNAIAEYAK--NHLVITIAHRLNTV-KNAKQLIVMENGCIVQQG 565
Cdd:cd03297 166 LRLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
35-319 |
9.84e-20 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 89.90 E-value: 9.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 35 ALGTVNAILMIAGAYLLAQT-----IHEVMFEGRNLAQVTQYLWPLAGIILLRALFLALSERLSAFATLKIKSAIRQTLL 109
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWlirelVDLVTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 110 DKLTQLGPSYIEKNGQGATLNTLHNGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMILV 189
Cdd:cd18778 81 DKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 190 GHKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATRKELKQIARISDDFRHATLNVLKIAFLSSFALEFLATISVAL 269
Cdd:cd18778 161 SKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1590405536 270 VaVIIGFRLFF-GTLDFATGFVVLLLAPEFYLPLRQLGSHYHARLQGISAA 319
Cdd:cd18778 241 V-LGFGGRLVLaGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGA 290
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
349-566 |
1.03e-19 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 90.52 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSNEGI---NNINLTLPSTGLVAIVGASGSGKSTLLDC--ML-----GfhpeviqHISIDQQPLTTANI 418
Cdd:COG1135 2 IELENLSKTFPTKGGPVtalDDVSLTIEKGEIFGIIGYSGAGKSTLIRCinLLerptsG-------SVLVDGVDLTALSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 419 SQLQ---QSIAWIPQKPTLFYD-TLAANIKLgnpsasheALEHA----AKQAgalEFINELPDgfntLIGEQGEG----- 485
Cdd:COG1135 75 RELRaarRKIGMIFQHFNLLSSrTVAENVAL--------PLEIAgvpkAEIR---KRVAELLE----LVGLSDKAdayps 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 486 -LSGGQKQRIALARAfLKHAP-ILVLDEPTAHLDSQTEQ----LIQNAIAEYAKNHLVITiaHRLNTVKN-AKQLIVMEN 558
Cdd:COG1135 140 qLSGGQKQRVGIARA-LANNPkVLLCDEATSALDPETTRsildLLKDINRELGLTIVLIT--HEMDVVRRiCDRVAVLEN 216
|
....*...
gi 1590405536 559 GCIVQQGD 566
Cdd:COG1135 217 GRIVEQGP 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
348-525 |
1.21e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 88.77 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 348 TISIHDLNFSYPNSNEG---INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQlqqs 424
Cdd:COG4525 3 MLTVRHVSVRYPGGGQPqpaLQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 425 iAWIPQKPTLF-----YDTLAANIKLgnpsashEALEHAAKQAGALEFInelpdgfnTLIGEQGEG------LSGGQKQR 493
Cdd:COG4525 79 -GVVFQKDALLpwlnvLDNVAFGLRL-------RGVPKAERRARAEELL--------ALVGLADFArrriwqLSGGMRQR 142
|
170 180 190
....*....|....*....|....*....|..
gi 1590405536 494 IALARAFLKHAPILVLDEPTAHLDSQTEQLIQ 525
Cdd:COG4525 143 VGIARALAADPRFLLMDEPFGALDALTREQMQ 174
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
346-565 |
1.32e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 89.09 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 346 NNTISIHDLNFSYPNSNEGI-NNINLTLPSTGLVAIVGASGSGKST---LLDCMLGFHPEVIQHISIDQQPLTTANISQL 421
Cdd:PRK13640 3 DNIVEFKHVSFTYPDSKKPAlNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 422 QQSIAWIPQKP--TLFYDTLAANIKLG--NPSASHEAL----EHAAKQAGALEFINELPdgfntligeqgEGLSGGQKQR 493
Cdd:PRK13640 83 REKVGIVFQNPdnQFVGATVGDDVAFGleNRAVPRPEMikivRDVLADVGMLDYIDSEP-----------ANLSGGQKQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1590405536 494 IALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAK--NHLVITIAHRLNTVKNAKQLIVMENGCIVQQG 565
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQG 225
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
346-568 |
1.43e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 89.14 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 346 NNTISIHDLNFSYPNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPL--TTANISQLQQ 423
Cdd:PRK13636 3 DYILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 424 SIAWIPQKP-------TLFYDTLAANIKLGNPSAS-HEALEHAAKQAGalefINELPDgfntligEQGEGLSGGQKQRIA 495
Cdd:PRK13636 83 SVGMVFQDPdnqlfsaSVYQDVSFGAVNLKLPEDEvRKRVDNALKRTG----IEHLKD-------KPTHCLSFGQKKRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1590405536 496 LARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKN-HLVITIA-HRLNTVK-NAKQLIVMENGCIVQQGDFK 568
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIAtHDIDIVPlYCDNVFVMKEGRVILQGNPK 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
348-565 |
1.51e-19 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 90.21 E-value: 1.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 348 TISIHDLNFSYPNSNeGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGF-HPEViQHISIDQQPLTTaNISQLQQSIA 426
Cdd:COG1118 2 SIEVRNISKRFGSFT-LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLeTPDS-GRIVLNGRDLFT-NLPPRERRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 427 WIPQKPTLF-YDTLAANIKLG----NPSAshealehAAKQAGALEFINelpdgfntLIGEQGEG------LSGGQKQRIA 495
Cdd:COG1118 79 FVFQHYALFpHMTVAENIAFGlrvrPPSK-------AEIRARVEELLE--------LVQLEGLAdrypsqLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 496 LARAFLKHAPILVLDEPTAHLDSQT----EQLIQNAIAEYakNHLVITIAH------RLntvknAKQLIVMENGCIVQQG 565
Cdd:COG1118 144 LARALAVEPEVLLLDEPFGALDAKVrkelRRWLRRLHDEL--GGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVG 216
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
365-548 |
1.73e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 91.91 E-value: 1.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPeviqH------ISIDQQPLTTANISQLQQS-IAWIPQKPTLFYD 437
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYP----HgtyegeIIFEGEELQASNIRDTERAgIAIIHQELALVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 438 -TLAANIKLGNPSASHEALEHAAKQAGALEFINELPDGFN--TLIGEqgegLSGGQKQRIALARAFLKHAPILVLDEPTA 514
Cdd:PRK13549 97 lSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINpaTPVGN----LGLGQQQLVEIAKALNKQARLLILDEPTA 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 1590405536 515 HL-DSQTEQLIqnAIAEYAKNHLV--ITIAHRLNTVK 548
Cdd:PRK13549 173 SLtESETAVLL--DIIRDLKAHGIacIYISHKLNEVK 207
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
345-565 |
1.84e-19 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 88.79 E-value: 1.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 345 ANNTISIHDLNFSYPNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTAnisqLQQS 424
Cdd:PRK15056 3 QQAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA----LQKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 425 -IAWIPQK-------PTLFYDTLAANIK-----LGNPSA-SHEALEHAAKQAGALEFINELpdgfntlIGEqgegLSGGQ 490
Cdd:PRK15056 79 lVAYVPQSeevdwsfPVLVEDVVMMGRYghmgwLRRAKKrDRQIVTAALARVDMVEFRHRQ-------IGE----LSGGQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1590405536 491 KQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEY---AKNHLVITiaHRLNTVKNAKQLIVMENGCIVQQG 565
Cdd:PRK15056 148 KKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELrdeGKTMLVST--HNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
348-565 |
2.13e-19 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 89.75 E-value: 2.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 348 TISIHDLNFSYpNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFhpEVIQH--ISIDQQPLTTA-----NISQ 420
Cdd:COG3839 3 SLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGL--EDPTSgeILIGGRDVTDLppkdrNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 421 LQQSIAWIPQKptlfydTLAANI----KLGNPSAS--HEALEHAAKQAGALEFINELPDGfntligeqgegLSGGQKQRI 494
Cdd:COG3839 80 VFQSYALYPHM------TVYENIafplKLRKVPKAeiDRRVREAAELLGLEDLLDRKPKQ-----------LSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 495 ALARAFLKHAPILVLDEPTAHLDSqteQLIQNAIAEYAKNH------LVI---------TIAHRlntvknakqLIVMENG 559
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLDA---KLRVEMRAEIKRLHrrlgttTIYvthdqveamTLADR---------IAVMNDG 210
|
....*.
gi 1590405536 560 CIVQQG 565
Cdd:COG3839 211 RIQQVG 216
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
367-574 |
2.33e-19 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 92.92 E-value: 2.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 367 NINLTLPSTGLVAIVGASGSGKSTLLDCMLG-FHpevIQHISIdqqplttanisQLQQSIAWIPQKPTLFYDTLAANIKL 445
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSqFE---ISEGRV-----------WAERSIAYVPQQAWIMNATVRGNILF 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 446 GNPsashealEHAAKQAGA-----LEF-INELPDGFNTLIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQ 519
Cdd:PTZ00243 744 FDE-------EDAARLADAvrvsqLEAdLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 520 T-----EQLIQNAIAeyAKNHLVITiaHRLNTVKNAKQLIVMENGCIVQQGDFKALSQQS 574
Cdd:PTZ00243 817 VgervvEECFLGALA--GKTRVLAT--HQVHVVPRADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
349-559 |
2.91e-19 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 86.69 E-value: 2.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQP---LTTANISQLQQSI 425
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 426 AWIPQKPTLFYD-TLAANIKLGNPSASHEALEHAAKQAGALEFInelpdGFNTLIGEQGEGLSGGQKQRIALARAFLKHA 504
Cdd:cd03292 81 GVVFQDFRLLPDrNVYENVAFALEVTGVPPREIRKRVPAALELV-----GLSHKHRALPAELSGGEQQRVAIARAIVNSP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1590405536 505 PILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIA-HRLNTVKN-AKQLIVMENG 559
Cdd:cd03292 156 TILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVAtHAKELVDTtRHRVIALERG 212
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
349-565 |
4.85e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.55 E-value: 4.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAWI 428
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 429 PQKP--TLFYDTLAANIKLG--NPSASHEALEHAAKQAGALEFINELPDgfntligEQGEGLSGGQKQRIALARAFLKHA 504
Cdd:PRK13652 84 FQNPddQIFSPTVEQDIAFGpiNLGLDEETVAHRVSSALHMLGLEELRD-------RVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1590405536 505 PILVLDEPTAHLDSQTEQLIQNAIAEYAKNH--LVITIAHRLNTVKN-AKQLIVMENGCIVQQG 565
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETYgmTVIFSTHQLDLVPEmADYIYVMDKGRIVAYG 220
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
348-581 |
4.98e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 86.61 E-value: 4.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 348 TISIHDLNFSYpNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDC--MLgfhpEVIQ----HISIDQ----QPLTTAN 417
Cdd:PRK11124 2 SIQLNGINCFY-GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVlnLL----EMPRsgtlNIAGNHfdfsKTPSDKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 418 ISQLQQSIAWIPQK----P--TLFYDTLAANIK---LGNPSASHEALEHAAKqagaLEfINELPDGFNTligeqgeGLSG 488
Cdd:PRK11124 77 IRELRRNVGMVFQQynlwPhlTVQQNLIEAPCRvlgLSKDQALARAEKLLER----LR-LKPYADRFPL-------HLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 489 GQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLV-ITIAHRLNTV-KNAKQLIVMENGCIVQQGD 566
Cdd:PRK11124 145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITqVIVTHEVEVArKTASRVVYMENGHIVEQGD 224
|
250
....*....|....*.
gi 1590405536 567 FKALSQ-QSGEFAKLL 581
Cdd:PRK11124 225 ASCFTQpQTEAFKNYL 240
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
347-542 |
5.14e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 86.89 E-value: 5.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 347 NTISIHDLNFSYPNSnEGINNINLTLPSTGLVAIVGASGSGKSTLL---DCMLGFHPE--VIQHISIDQQPLTTANISQL 421
Cdd:PRK14247 2 NKIEIRDLKVSFGQV-EVLDGVNLEIPDNTITALMGPSGSGKSTLLrvfNRLIELYPEarVSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 422 Q---QSIAWIPQK-PTL-FYDTLAANIKLGNPSASHEALEHAAKQA-GALEFINELPDGFNTLIGEqgegLSGGQKQRIA 495
Cdd:PRK14247 81 RrrvQMVFQIPNPiPNLsIFENVALGLKLNRLVKSKKELQERVRWAlEKAQLWDEVKDRLDAPAGK----LSGGQQQRLC 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1590405536 496 LARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIAH 542
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTH 203
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
331-543 |
6.36e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 90.25 E-value: 6.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 331 PENDDSHTANINIDANNTISIHDLNFSYPNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQ 410
Cdd:COG4178 345 ADALPEAASRIETSEDGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPA 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 411 QplttanisqlqQSIAWIPQKPTLFYDTLAANIKLGNP--SASHEALEHAAKQAGaLEfinELPDGFNTligEQ--GEGL 486
Cdd:COG4178 425 G-----------ARVLFLPQRPYLPLGTLREALLYPATaeAFSDAELREALEAVG-LG---HLAERLDE---EAdwDQVL 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1590405536 487 SGGQKQRIALARAFLkHAP-ILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIAHR 543
Cdd:COG4178 487 SLGEQQRLAFARLLL-HKPdWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
349-566 |
1.03e-18 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 87.85 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYpNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFhpEVIQ--HISIDQQPLTT--ANisqlQQS 424
Cdd:COG3842 6 LELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGF--ETPDsgRILLDGRDVTGlpPE----KRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 425 IAWIPQKPTLF-YDTLAANI-----KLGNPSAshealEHAAKQAGALEFINeLpDGF-NTLIGEqgegLSGGQKQRIALA 497
Cdd:COG3842 79 VGMVFQDYALFpHLTVAENVafglrMRGVPKA-----EIRARVAELLELVG-L-EGLaDRYPHQ----LSGGQQQRVALA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 498 RAFLKHAPILVLDEPTAHLDSQT-EQLiQNAIAEYAKNH----LVIT--------IAHRlntvknakqLIVMENGCIVQQ 564
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALDAKLrEEM-REELRRLQRELgitfIYVThdqeealaLADR---------IAVMNDGRIEQV 217
|
..
gi 1590405536 565 GD 566
Cdd:COG3842 218 GT 219
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
360-570 |
1.14e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 85.96 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 360 NSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCM-LGFHPEV----IQHISID-------QQPLttanISQLQQSIAW 427
Cdd:PRK11264 14 HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInLLEQPEAgtirVGDITIDtarslsqQKGL----IRQLRQHVGF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 428 IPQKPTLF-YDTLAANIKLGNPSASHEALEHAAKQAGALEfinelpdgfnTLIGEQGEG------LSGGQKQRIALARAF 500
Cdd:PRK11264 90 VFQNFNLFpHRTVLENIIEGPVIVKGEPKEEATARARELL----------AKVGLAGKEtsyprrLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1590405536 501 LKHAPILVLDEPTAHLDSQTEQLIQNAIAEYA--KNHLVItIAHRLNTVKN-AKQLIVMENGCIVQQGDFKAL 570
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAqeKRTMVI-VTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
32-321 |
1.22e-18 |
|
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: 86.69 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 32 LSIALGTVNAILMIAGAYLLAQTI-----HEVMFEGRNLAQVTQYLWPLAGIILLRALFLALSERLSAFATLKIKSAIRQ 106
Cdd:cd18547 3 LVIILAIISTLLSVLGPYLLGKAIdliieGLGGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 107 TLLDKLTQLGPSYIEKNGQGATLNTLHNGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFM 186
Cdd:cd18547 83 DLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 187 ILVGHKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATRKELKQIARISDDFRHATlnvLKIAFLSSF---ALEFLA 263
Cdd:cd18547 163 KFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKAS---FKAQFYSGLlmpIMNFIN 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1590405536 264 TISVALVAVIIGFRLFFGTLDFATGFVVLLLAPEFYLPLRQLGSHYhARLQGISAAAD 321
Cdd:cd18547 240 NLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQI-NSLQSALAGAE 296
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
348-580 |
1.51e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 86.37 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 348 TISIHDLNFSY----PNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTAN----IS 419
Cdd:PRK13646 2 TIRFDNVSYTYqkgtPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 420 QLQQSIAWIPQKP--TLFYDTLAANIKLGnPSASHEALEHAakQAGALEFINELpdGFNTLIGEQGE-GLSGGQKQRIAL 496
Cdd:PRK13646 82 PVRKRIGMVFQFPesQLFEDTVEREIIFG-PKNFKMNLDEV--KNYAHRLLMDL--GFSRDVMSQSPfQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 497 ARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYA--KNHLVITIAHRLNTV-KNAKQLIVMENGCIVQQGDFKALSQQ 573
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKD 236
|
....*..
gi 1590405536 574 SGEFAKL 580
Cdd:PRK13646 237 KKKLADW 243
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
349-565 |
1.86e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 85.84 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSY----PNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLdcmlgfhpeviQH-----------ISIDQQPL 413
Cdd:PRK13634 3 ITFQKVEHRYqyktPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLL-----------QHlngllqptsgtVTIGERVI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 414 TTA----NISQLQQSIAWIPQKP--TLFYDTLAANIKLG--NPSASHEALEHAAKQAGALEFINElpdgfnTLIGEQGEG 485
Cdd:PRK13634 72 TAGkknkKLKPLRKKVGIVFQFPehQLFEETVEKDICFGpmNFGVSEEDAKQKAREMIELVGLPE------ELLARSPFE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 486 LSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEY--AKNHLVITIAHRLNTVKN-AKQLIVMENGCIV 562
Cdd:PRK13634 146 LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAARyADQIVVMHKGTVF 225
|
...
gi 1590405536 563 QQG 565
Cdd:PRK13634 226 LQG 228
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
365-581 |
2.57e-18 |
|
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: 89.58 E-value: 2.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLG-FHPE--VIQHisidqqplttanisqlQQSIAWIPQKPTLFYDTLAA 441
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGeLEPSegKIKH----------------SGRISFSPQTSWIMPGTIKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 442 NIKLGnpsASHEALEHAA--KQAGALEFINELPDGFNTLIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQ 519
Cdd:TIGR01271 506 NIIFG---LSYDEYRYTSviKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1590405536 520 TEQLI-QNAIAEYAKNHLVITIAHRLNTVKNAKQLIVMENGCIVQQGDFKALSQQSGEFAKLL 581
Cdd:TIGR01271 583 TEKEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLL 645
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
348-581 |
2.92e-18 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 84.29 E-value: 2.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 348 TISIHDLNFSYpNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCM-LGFHPEVIQ-HISIDQ----QPLTTANISQL 421
Cdd:COG4161 2 SIQLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLnLLETPDSGQlNIAGHQfdfsQKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 422 QQSIAWIPQK----P--TLFYDTLAANIKLGNPSAShEALEHAAKQAGALEfINELPDGFNTLigeqgegLSGGQKQRIA 495
Cdd:COG4161 81 RQKVGMVFQQynlwPhlTVMENLIEAPCKVLGLSKE-QAREKAMKLLARLR-LTDKADRFPLH-------LSGGQQQRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 496 LARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLV-ITIAHRLNTV-KNAKQLIVMENGCIVQQGDFKALSQ- 572
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITqVIVTHEVEFArKVASQVVYMEKGRIIEQGDASHFTQp 231
|
....*....
gi 1590405536 573 QSGEFAKLL 581
Cdd:COG4161 232 QTEAFAHYL 240
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
366-573 |
3.44e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 87.77 E-value: 3.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 366 NNINLTLPStGLV-AIVGASGSGKSTLLDCMLGFHP----EviqhISIDQQPLTTANISQ-LQQSIAWIPQKPTLFYD-T 438
Cdd:COG1129 21 DGVSLELRP-GEVhALLGENGAGKSTLMKILSGVYQpdsgE----ILLDGEPVRFRSPRDaQAAGIAIIHQELNLVPNlS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 439 LAANIKLGNPSASHEALEHAAKQAGALEFINELpdGFN----TLIGEqgegLSGGQKQRIALARAFLKHAPILVLDEPTA 514
Cdd:COG1129 96 VAENIFLGREPRRGGLIDWRAMRRRARELLARL--GLDidpdTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1590405536 515 HL-DSQTEQLIqNAIAEY-AKNHLVITIAHRLNTVKN-AKQLIVMENGCIVQQGDFKALSQQ 573
Cdd:COG1129 170 SLtEREVERLF-RIIRRLkAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAELTED 230
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
359-566 |
5.29e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 85.29 E-value: 5.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 359 PNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGF----------------HPEVIQHISIDQQPLTTANISQLQ 422
Cdd:PRK13631 36 ENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLikskygtiqvgdiyigDKKNNHELITNPYSKKIKNFKELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 423 QSIAWIPQKP--TLFYDTLAANIKLGnPSASHEALEHAAKQAGalEFINELPDGFNTLigEQGE-GLSGGQKQRIALARA 499
Cdd:PRK13631 116 RRVSMVFQFPeyQLFKDTIEKDIMFG-PVALGVKKSEAKKLAK--FYLNKMGLDDSYL--ERSPfGLSGGQKRRVAIAGI 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1590405536 500 FLKHAPILVLDEPTAHLDSQTEQLIQNAIAEY-AKNHLVITIAHRL-NTVKNAKQLIVMENGCIVQQGD 566
Cdd:PRK13631 191 LAIQPEILIFDEPTAGLDPKGEHEMMQLILDAkANNKTVFVITHTMeHVLEVADEVIVMDKGKILKTGT 259
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
349-565 |
5.54e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 84.36 E-value: 5.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQ--QSIA 426
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEvrKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 427 WIPQKP--TLFYDTLAANIKLG--NPSASHEALEHAAKQA----GALEFINELPdgfntligeqgEGLSGGQKQRIALAR 498
Cdd:PRK13639 82 IVFQNPddQLFAPTVEEDVAFGplNLGLSKEEVEKRVKEAlkavGMEGFENKPP-----------HHLSGGQKKRVAIAG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1590405536 499 AFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIA-HRLNTV-KNAKQLIVMENGCIVQQG 565
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEG 219
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
349-544 |
6.57e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 83.67 E-value: 6.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYpNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDC---MLGFHPEVIQHISIDQQ------PLTtaNIS 419
Cdd:PRK14239 6 LQVSDLSVYY-NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSinrMNDLNPEVTITGSIVYNghniysPRT--DTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 420 QLQQSIAWIPQKPTLFYDTLAANIKLG-------NPSASHEALEHAAKQAGALefiNELPDGFNtligEQGEGLSGGQKQ 492
Cdd:PRK14239 83 DLRKEIGMVFQQPNPFPMSIYENVVYGlrlkgikDKQVLDEAVEKSLKGASIW---DEVKDRLH----DSALGLSGGQQQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1590405536 493 RIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIAHRL 544
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
367-588 |
7.50e-18 |
|
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: 85.15 E-value: 7.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 367 NINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPL--TTANISQL--QQSIAWIPQKPTLF--YdTLA 440
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdSARGIFLPphRRRIGYVFQEARLFphL-SVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 441 ANIKLGnpsasheaLEHAAKQAGALEF---INELpdGFNTLIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLD 517
Cdd:COG4148 96 GNLLYG--------RKRAPRAERRISFdevVELL--GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 518 SQT--------EQLIQN----------AIAEYAknhlvitiahRLntvknAKQLIVMENGCIVQQGDFKALSQQSgEFAK 579
Cdd:COG4148 166 LARkaeilpylERLRDEldipilyvshSLDEVA----------RL-----ADHVVLLEQGRVVASGPLAEVLSRP-DLLP 229
|
....*....
gi 1590405536 580 LLQTAEQGV 588
Cdd:COG4148 230 LAGGEEAGS 238
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
349-559 |
8.78e-18 |
|
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: 80.19 E-value: 8.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNsNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQqpltTANISQLQQsiawi 428
Cdd:cd03221 1 IELENLSKTYGG-KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS----TVKIGYFEQ----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 429 pqkptlfydtlaaniklgnpsashealehaakqagalefinelpdgfntligeqgegLSGGQKQRIALARAFLKHAPILV 508
Cdd:cd03221 71 ---------------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1590405536 509 LDEPTAHLDSQTEQLIQNAIAEYakNHLVITIAH-R--LNTVknAKQLIVMENG 559
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEY--PGTVILVSHdRyfLDQV--ATKIIELEDG 143
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
349-566 |
9.04e-18 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 83.35 E-value: 9.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPN--------SNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQ 420
Cdd:COG4167 5 LEVRNLSKTFKYrtglfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 421 LQQSIAWIPQKPTlfyDTLAANIKLG-------------NPSASHEALEHAAKQAGALefinelPDGFNTLIGEqgegLS 487
Cdd:COG4167 85 RCKHIRMIFQDPN---TSLNPRLNIGqileeplrlntdlTAEEREERIFATLRLVGLL------PEHANFYPHM----LS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 488 GGQKQRIALARAFLKHAPILVLDEPTAHLD-SQTEQLIqNAIAEYAKNHLV--ITIAHRLNTVKN-AKQLIVMENGCIVQ 563
Cdd:COG4167 152 SGQKQRVALARALILQPKIIIADEALAALDmSVRSQII-NLMLELQEKLGIsyIYVSQHLGIVKHiSDKVLVMHQGEVVE 230
|
...
gi 1590405536 564 QGD 566
Cdd:COG4167 231 YGK 233
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
343-573 |
1.10e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 83.90 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 343 IDANNTISIHDLNFSY----PNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFH-PEVIQHISIDQQ-PLTTA 416
Cdd:PRK13645 1 FDFSKDIILDNVSYTYakktPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIiSETGQTIVGDYAiPANLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 417 NISQ---LQQSIAWIPQKP--TLFYDTLAANIKLGnPSASHEALEHAAKQAGALEFINELPDGFntlIGEQGEGLSGGQK 491
Cdd:PRK13645 81 KIKEvkrLRKEIGLVFQFPeyQLFQETIEKDIAFG-PVNLGENKQEAYKKVPELLKLVQLPEDY---VKRSPFELSGGQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 492 QRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNH--LVITIAHRLNTV-KNAKQLIVMENGCIVQQGD-F 567
Cdd:PRK13645 157 RRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYkkRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSpF 236
|
....*.
gi 1590405536 568 KALSQQ 573
Cdd:PRK13645 237 EIFSNQ 242
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
364-530 |
2.66e-17 |
|
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: 81.33 E-value: 2.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 364 GINNINLTLPSTGLVAIVGASGSGKSTLLDCMLG-FHPE----VIQHIS--IDqqpLTTANISQL----QQSIAW----- 427
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnYLPDsgsiLVRHDGgwVD---LAQASPREIlalrRRTIGYvsqfl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 428 --IPQKPTLfyDTLA-ANIKLGNPSAshEALEHAAKqagALEFINeLPdgfntligeqgEGL--------SGGQKQRIAL 496
Cdd:COG4778 103 rvIPRVSAL--DVVAePLLERGVDRE--EARARARE---LLARLN-LP-----------ERLwdlppatfSGGEQQRVNI 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 1590405536 497 ARAFLKHAPILVLDEPTAHLDSQTEQ----LIQNAIAE 530
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDAANRAvvveLIEEAKAR 201
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
335-567 |
2.92e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.12 E-value: 2.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 335 DSHTANINIDA-----NNTISIHDLNFSYPNsNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGfhpeviqhisiD 409
Cdd:COG0488 297 RDKTVEIRFPPperlgKKVLELEGLSKSYGD-KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAG-----------E 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 410 QQPL-------TTANI---SQLQQSIAwiPQKptlfydTLAANIKLGNPSASHEaleHAAKQAGALEFInelPDGFNTLI 479
Cdd:COG0488 365 LEPDsgtvklgETVKIgyfDQHQEELD--PDK------TVLDELRDGAPGGTEQ---EVRGYLGRFLFS---GDDAFKPV 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 480 GEqgegLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNhlVITIAH-R--LNTVknAKQLIVM 556
Cdd:COG0488 431 GV----LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGT--VLLVSHdRyfLDRV--ATRILEF 502
|
250
....*....|..
gi 1590405536 557 ENGCIVQ-QGDF 567
Cdd:COG0488 503 EDGGVREyPGGY 514
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
346-565 |
3.23e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 82.06 E-value: 3.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 346 NNTISIHDLNFSYPNSNE--GINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQ 423
Cdd:PRK13642 2 NKILEVENLVFKYEKESDvnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 424 SIAWIPQKP--TLFYDTLAANIKLGNPSASHEALEHAAKQAGALEFINELpdGFNTligEQGEGLSGGQKQRIALARAFL 501
Cdd:PRK13642 82 KIGMVFQNPdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNML--DFKT---REPARLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1590405536 502 KHAPILVLDEPTAHLDSQTEQLIQNAIAEYA-KNHL-VITIAHRLNTVKNAKQLIVMENGCIVQQG 565
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIHEIKeKYQLtVLSITHDLDEAASSDRILVMKAGEIIKEA 222
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
365-558 |
3.59e-17 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 80.60 E-value: 3.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQ---HISIDQQPLTTANISQLQqsIAWIPQKPTLF-YDTLA 440
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSasgEVLLNGRRLTALPAEQRR--IGILFQDDLLFpHLSVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 441 ANIKLGNPSASHEALEHAAKQAgALEFINeLPDGFNTLIGEqgegLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQT 520
Cdd:COG4136 95 ENLAFALPPTIGRAQRRARVEQ-ALEEAG-LAGFADRDPAT----LSGGQRARVALLRALLAEPRALLLDEPFSKLDAAL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1590405536 521 ---------EQLIQNAIAeyaknhlVITIAHRLNTVKNAKQLIVMEN 558
Cdd:COG4136 169 raqfrefvfEQIRQRGIP-------ALLVTHDEEDAPAAGRVLDLGN 208
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
365-556 |
4.39e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 80.53 E-value: 4.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAWIPQKPTLFYDTLAANIK 444
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDNLI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 445 LgnP-SASHEALEHAAKQAGALEFinELPDgfnTLIGEQGEGLSGGQKQRIALARAfLKHAP-ILVLDEPTAHLDSQTEQ 522
Cdd:PRK10247 103 F--PwQIRNQQPDPAIFLDDLERF--ALPD---TILTKNIAELSGGEKQRISLIRN-LQFMPkVLLLDEITSALDESNKH 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 1590405536 523 LIQNAIAEYAKNH--LVITIAHRLNTVKNAKQLIVM 556
Cdd:PRK10247 175 NVNEIIHRYVREQniAVLWVTHDKDEINHADKVITL 210
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
368-590 |
4.48e-17 |
|
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: 82.85 E-value: 4.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 368 INLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTAN----ISQLQQSIAWIPQKPTLF-YDTLAAN 442
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRkgifLPPEKRRIGYVFQEARLFpHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 443 IKLGNPSASHEalEHAAKQAGALEFInelpdGFNTLIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQ 522
Cdd:TIGR02142 96 LRYGMKRARPS--ERRISFERVIELL-----GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1590405536 523 LI----QNAIAEYakNHLVITIAHRLNTVKN-AKQLIVMENGCIVQQGDFKALsQQSGEFAkLLQTAEQGVTN 590
Cdd:TIGR02142 169 EIlpylERLHAEF--GIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEV-WASPDLP-WLAREDQGSLI 237
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
348-565 |
5.04e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 83.35 E-value: 5.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 348 TISIHDLNFSYpNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAW 427
Cdd:PRK09536 3 MIDVSDLSVEF-GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 428 IPQKPTLFYD-TLAANIKLG-NP---------SASHEALEHAAKQAGALEFINELPDGfntligeqgegLSGGQKQRIAL 496
Cdd:PRK09536 82 VPQDTSLSFEfDVRQVVEMGrTPhrsrfdtwtETDRAAVERAMERTGVAQFADRPVTS-----------LSGGERQRVLL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1590405536 497 ARAFLKHAPILVLDEPTAHLD----SQTEQLIQNaIAEYAKNhlVITIAHRLN-TVKNAKQLIVMENGCIVQQG 565
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLDinhqVRTLELVRR-LVDDGKT--AVAAIHDLDlAARYCDELVLLADGRVRAAG 221
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
361-561 |
5.48e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 80.88 E-value: 5.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 361 SNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTA--NISQLQQSIAWIPQKPTLfyDT 438
Cdd:PRK11247 24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAreDTRLMFQDARLLPWKKVI--DN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 439 LAANIKLGNPSASHEALEhaakQAGALEFINELPdgfntligeqgEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDS 518
Cdd:PRK11247 102 VGLGLKGQWRDAALQALA----AVGLADRANEWP-----------AALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1590405536 519 QT----EQLIQNAIAEYAKNHLVITiaHRLN-TVKNAKQLIVMENGCI 561
Cdd:PRK11247 167 LTriemQDLIESLWQQHGFTVLLVT--HDVSeAVAMADRVLLIEEGKI 212
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
346-565 |
5.94e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 81.29 E-value: 5.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 346 NNTISIHDLNFSYPNSNEG-----INNINLTLPSTGLVAIVGASGSGKSTLLDCMLG-FHPEVIQHISIDQQPLTTANIS 419
Cdd:PRK13633 2 NEMIKCKNVSYKYESNEESteklaLDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNAlLIPSEGKVYVDGLDTSDEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 420 QLQQSIAWIPQKPTlfyDTLAANI----------KLG-NPSASHEALEHAAKQAGALEFINELPdgfntligeqgEGLSG 488
Cdd:PRK13633 82 DIRNKAGMVFQNPD---NQIVATIveedvafgpeNLGiPPEEIRERVDESLKKVGMYEYRRHAP-----------HLLSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1590405536 489 GQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNH--LVITIAHRLNTVKNAKQLIVMENGCIVQQG 565
Cdd:PRK13633 148 GQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEG 226
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
349-562 |
7.33e-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: 78.24 E-value: 7.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNsNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQ-LQQSIAW 427
Cdd:cd03216 1 LELRGITKRFGG-VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 428 IPQkptlfydtlaaniklgnpsashealehaakqagalefinelpdgfntligeqgegLSGGQKQRIALARAFLKHAPIL 507
Cdd:cd03216 80 VYQ-------------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1590405536 508 VLDEPTAHL-DSQTEQLIqNAIAEYAKNHL-VITIAHRLNTVKN-AKQLIVMENGCIV 562
Cdd:cd03216 105 ILDEPTAALtPAEVERLF-KVIRRLRAQGVaVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
365-584 |
7.45e-17 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 80.62 E-value: 7.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQ---LQQSIAWIPQK-PTLFYDTLA 440
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrraFRRDVQLVFQDsPSAVNPRMT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 441 ANIKLGNPSASHEALEHAAKQAGALEFIN--ELPDGFNTLIGEQgegLSGGQKQRIALARAFLKHAPILVLDEPTAHLD- 517
Cdd:TIGR02769 107 VRQIIGEPLRHLTSLDESEQKARIAELLDmvGLRSEDADKLPRQ---LSGGQLQRINIARALAVKPKLIVLDEAVSNLDm 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1590405536 518 ---SQTEQLIQNAIAEYAKNHLVITiaHRLNTVKN-AKQLIVMENGCIVQQGDFKALSQQSGEFAKLLQTA 584
Cdd:TIGR02769 184 vlqAVILELLRKLQQAFGTAYLFIT--HDLRLVQSfCQRVAVMDKGQIVEECDVAQLLSFKHPAGRNLQSA 252
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
346-542 |
8.42e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 80.27 E-value: 8.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 346 NNTISIHDLNFSYpNSNEGINNINLTLPSTGLVAIVGASGSGKSTLL---DCMLGFHPE--VIQHISIDQQPLTTANIS- 419
Cdd:PRK14267 2 KFAIETVNLRVYY-GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLrtfNRLLELNEEarVEGEVRLFGRNIYSPDVDp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 420 -QLQQSIAWIPQKPTLF-----YDTLAANIKLGNPSASHEAL----EHAAKQAGALEfinELPDGFNTLIGEqgegLSGG 489
Cdd:PRK14267 81 iEVRREVGMVFQYPNPFphltiYDNVAIGVKLNGLVKSKKELdervEWALKKAALWD---EVKDRLNDYPSN----LSGG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1590405536 490 QKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIAH 542
Cdd:PRK14267 154 QRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
364-565 |
8.54e-17 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 80.77 E-value: 8.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 364 GINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQ-----------QSIAWIPQKp 432
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRelrrkkismvfQSFALLPHR- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 433 tlfydTLAANIKLG------NPSASHEALEHAAKQAGALEFINELPDGfntligeqgegLSGGQKQRIALARAFLKHAPI 506
Cdd:cd03294 118 -----TVLENVAFGlevqgvPRAEREERAAEALELVGLEGWEHKYPDE-----------LSGGMQQRVGLARALAVDPDI 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1590405536 507 LVLDEPTAHLDSQTEQLIQNAIAEYAKNH--LVITIAHRLN-TVKNAKQLIVMENGCIVQQG 565
Cdd:cd03294 182 LLMDEAFSALDPLIRREMQDELLRLQAELqkTIVFITHDLDeALRLGDRIAIMKDGRLVQVG 243
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
347-559 |
1.11e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 80.55 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 347 NTISIHDLNFSYPNSNEG--INNINLTLPSTGLVAIVGASGSGKST---LLDCMLgfHPEVIQhISIDQQPLTTANISQL 421
Cdd:PRK13650 3 NIIEVKNLTFKYKEDQEKytLNDVSFHVKQGEWLSIIGHNGSGKSTtvrLIDGLL--EAESGQ-IIIDGDLLTEENVWDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 422 QQSIAWIPQKP--TLFYDTLAANIKLG--NPSASHEALEHAAKQA----GALEFINELPdgfntligeqgEGLSGGQKQR 493
Cdd:PRK13650 80 RHKIGMVFQNPdnQFVGATVEDDVAFGleNKGIPHEEMKERVNEAlelvGMQDFKEREP-----------ARLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 494 IALARAFLKHAPILVLDEPTAHLDSQTE----QLIQNAIAEYakNHLVITIAHRLNTVKNAKQLIVMENG 559
Cdd:PRK13650 149 VAIAGAVAMRPKIIILDEATSMLDPEGRleliKTIKGIRDDY--QMTVISITHDLDEVALSDRVLVMKNG 216
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
367-550 |
1.18e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 78.43 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 367 NINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPE---------------VIQHISIDQQ-PLTTANISQLQqsiAWIPQ 430
Cdd:NF040873 10 GVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPtsgtvrraggarvayVPQRSEVPDSlPLTVRDLVAMG---RWARR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 431 KPtlfydtlaanikLGNPSAS-HEALEHAAKQAGALEfinelpdgfntLIGEQGEGLSGGQKQRIALARAFLKHAPILVL 509
Cdd:NF040873 87 GL------------WRRLTRDdRAAVDDALERVGLAD-----------LAGRQLGELSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1590405536 510 DEPTAHLDSQTEQLIQNAIAEY-AKNHLVITIAHRLNTVKNA 550
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEEhARGATVVVVTHDLELVRRA 185
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
349-570 |
1.51e-16 |
|
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: 79.02 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSnEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQ-LQQSIAW 427
Cdd:cd03224 1 LEVENLNAGYGKS-QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 428 IPQKPTLFYD-TLAANIKLGnpsashEALEHAAKQAGALEFINELpdgFNTL---IGEQGEGLSGGQKQRIALARAFLKH 503
Cdd:cd03224 80 VPEGRRIFPElTVEENLLLG------AYARRRAKRKARLERVYEL---FPRLkerRKQLAGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1590405536 504 APILVLDEPTAHLDSQTEQLIQNAIAEYAK----------N-HLVITIAHRlntvknakqLIVMENGCIVQQGDFKAL 570
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIRELRDegvtillveqNaRFALEIADR---------AYVLERGRVVLEGTAAEL 219
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
361-573 |
1.84e-16 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 80.92 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 361 SNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQlqQSIAWIPQKPTLF----- 435
Cdd:PRK11432 18 SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--RDICMVFQSYALFphmsl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 436 YDTLAANIK-LGNPSAshealEHAAKQAGALEFINElpDGFNTLIGEQgegLSGGQKQRIALARAFLKHAPILVLDEPTA 514
Cdd:PRK11432 96 GENVGYGLKmLGVPKE-----ERKQRVKEALELVDL--AGFEDRYVDQ---ISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1590405536 515 HLDSQTEQLIQNAIAEYAKnHLVIT---IAH-RLNTVKNAKQLIVMENGCIVQQGDFKALSQQ 573
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQ-QFNITslyVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
348-559 |
1.92e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 79.87 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 348 TISIHDLNFSY----PNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLT----TANIS 419
Cdd:PRK13641 2 SIKFENVDYIYspgtPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 420 QLQQSIAWIPQKP--TLFYDTLAANIKLG--NPSAShealEHAAKQAgALEFINE--LPDgfnTLIGEQGEGLSGGQKQR 493
Cdd:PRK13641 82 KLRKKVSLVFQFPeaQLFENTVLKDVEFGpkNFGFS----EDEAKEK-ALKWLKKvgLSE---DLISKSPFELSGGQMRR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1590405536 494 IALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAK-NHLVITIAHRLNTV-KNAKQLIVMENG 559
Cdd:PRK13641 154 VAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaGHTVILVTHNMDDVaEYADDVLVLEHG 221
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
349-573 |
1.97e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 79.79 E-value: 1.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSY----PNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTA----NISQ 420
Cdd:PRK13649 3 INLQNVSYTYqagtPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 421 LQQSIAWIPQKP--TLFYDTLAANIKLG--NPSASHEALEHAAKQAGALEFINElpdgfnTLIGEQGEGLSGGQKQRIAL 496
Cdd:PRK13649 83 IRKKVGLVFQFPesQLFEETVLKDVAFGpqNFGVSQEEAEALAREKLALVGISE------SLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1590405536 497 ARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVIT-IAHRLNTVKN-AKQLIVMENGCIVQQGDFKALSQQ 573
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
349-538 |
2.14e-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: 78.32 E-value: 2.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPN-SNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTaNISQLQQSIAW 427
Cdd:cd03263 1 LQIRNLTKTYKKgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 428 IPQKPTLF-----YDTLA--ANIKLGNPSASHEALEHAAKQAGalefineLPDGFNTLIGEqgegLSGGQKQRIALARAF 500
Cdd:cd03263 80 CPQFDALFdeltvREHLRfyARLKGLPKSEIKEEVELLLRVLG-------LTDKANKRART----LSGGMKRKLSLAIAL 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 1590405536 501 LKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVI 538
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSII 186
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
367-553 |
2.18e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.99 E-value: 2.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 367 NINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTtanISQLQQSIAWI----PQKPTLfydTLAAN 442
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID---DPDVAEACHYLghrnAMKPAL---TVAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 443 IKL------GNPSASHEALEhaakqAGALEFINELPDGFntligeqgegLSGGQKQRIALARAFLKHAPILVLDEPTAHL 516
Cdd:PRK13539 94 LEFwaaflgGEELDIAAALE-----AVGLAPLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 1590405536 517 DSQTEQLIQNAIAEY-AKNHLVITIAHRLNTVKNAKQL 553
Cdd:PRK13539 159 DAAAVALFAELIRAHlAQGGIVIAATHIPLGLPGAREL 196
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
346-571 |
2.28e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 79.39 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 346 NNTISIHDLNFSYPNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSI 425
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 426 AWIPQKP-------TLFYDTLAANIKLG-NPSASHEALEHAAKQAGALEFINELPdgfntligeqgEGLSGGQKQRIALA 497
Cdd:PRK13647 82 GLVFQDPddqvfssTVWDDVAFGPVNMGlDKDEVERRVEEALKAVRMWDFRDKPP-----------YHLSYGQKKRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1590405536 498 RAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIA-HRLNTVKN-AKQLIVMENGCIVQQGDFKALS 571
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGDKSLLT 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
363-566 |
2.62e-16 |
|
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: 82.16 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 363 EGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLG---FHP---EVIQHIS----------------------------- 407
Cdd:TIGR03269 14 EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdqYEPtsgRIIYHVAlcekcgyverpskvgepcpvcggtlepee 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 408 IDQQPLTTANISQLQQSIAWIPQKPTLFY--DTLAANIKLGNPSASHEALEHAAKQAGALEFINelpdgFNTLIGEQGEG 485
Cdd:TIGR03269 94 VDFWNLSDKLRRRIRKRIAIMLQRTFALYgdDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQ-----LSHRITHIARD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 486 LSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNH---LVITiAHRLNTVKN-AKQLIVMENGCI 561
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgisMVLT-SHWPEVIEDlSDKAIWLENGEI 247
|
....*
gi 1590405536 562 VQQGD 566
Cdd:TIGR03269 248 KEEGT 252
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
365-572 |
2.68e-16 |
|
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: 81.79 E-value: 2.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHP--EVIQHISIDQQPLTTANISQLQQS-IAWIPQKPTLFYD-TLA 440
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVPElSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 441 ANIKLGNPSASHEALEHAA---KQAGALEFINELPDGFNTL-IGEQGeglsGGQKQRIALARAFLKHAPILVLDEPTAHL 516
Cdd:TIGR02633 97 ENIFLGNEITLPGGRMAYNamyLRAKNLLRELQLDADNVTRpVGDYG----GGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1590405536 517 DSQTEQLIQNAIAEY-AKNHLVITIAHRLNTVKNAKQLI-VMENGCIVQQGDFKALSQ 572
Cdd:TIGR02633 173 TEKETEILLDIIRDLkAHGVACVYISHKLNEVKAVCDTIcVIRDGQHVATKDMSTMSE 230
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
41-306 |
3.30e-16 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 79.48 E-value: 3.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 41 AILMIAGA-------YLLAQTIHEV---MFEGRNLAQVTQYLWPLAGIILLRALFLALSERLSAFATLKIKSAIRQTLLD 110
Cdd:cd18563 5 FLLMLLGTalglvppYLTKILIDDVliqLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 111 KLTQLGPSYIEKNGQGATLNTLHNGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMILVG 190
Cdd:cd18563 85 HLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYFFW 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 191 HKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATRKELKQIARISDDFRHATLNVLKIAFLSSFALEFLATISVALV 270
Cdd:cd18563 165 KKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLGTLIV 244
|
250 260 270
....*....|....*....|....*....|....*...
gi 1590405536 271 AVIIGFRLFFGTLDFAT--GFVVLLLapEFYLPLRQLG 306
Cdd:cd18563 245 WYFGGRQVLSGTMTLGTlvAFLSYLG--MFYGPLQWLS 280
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
349-565 |
4.16e-16 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 77.26 E-value: 4.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYpNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPlTTANISQLQQsIAWI 428
Cdd:cd03268 1 LKTNDLTKTY-GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS-YQKNIEALRR-IGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 429 PQKPTlFYDTLAAniklgnpsasHEALEHAAKQAGAL-EFINELPD--GFNTLIGEQGEGLSGGQKQRIALARAFLKHAP 505
Cdd:cd03268 78 IEAPG-FYPNLTA----------RENLRLLARLLGIRkKRIDEVLDvvGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1590405536 506 ILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIA-HRLNTV-KNAKQLIVMENGCIVQQG 565
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSLRDQGITVLISsHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
349-570 |
5.40e-16 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 79.33 E-value: 5.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSNEGI---NNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQ---HISIDQQPLTTANISQLQ 422
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVkavDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGItsgEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 423 Q----SIAWIPQKPT-----LF--YDTLAANIKLGNPSASHEALEHAA---KQAG---ALEFINELPdgfntligeqGEg 485
Cdd:COG0444 82 KirgrEIQMIFQDPMtslnpVMtvGDQIAEPLRIHGGLSKAEARERAIellERVGlpdPERRLDRYP----------HE- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 486 LSGGQKQRIALARAFLKHAPILVLDEPTAHLD----SQTEQLIQNAIAEYaknHL-VITIAHRLNTVKN-AKQLIVMENG 559
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDvtiqAQILNLLKDLQREL---GLaILFITHDLGVVAEiADRVAVMYAG 227
|
250
....*....|.
gi 1590405536 560 CIVQQGDFKAL 570
Cdd:COG0444 228 RIVEEGPVEEL 238
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
377-566 |
5.47e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.96 E-value: 5.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 377 LVAIVGASGSGKSTLLDCMLGFHPEVIQhISIDQQPLTTANISQLQQSIAWIPQK-PTLF------YDTLAAniklgNPS 449
Cdd:COG4138 24 LIHLIGPNGAGKSTLLARMAGLLPGQGE-ILLNGRPLSDWSAAELARHRAYLSQQqSPPFampvfqYLALHQ-----PAG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 450 ASHEALEHAAKQ-AGALEFINELPDGFNTligeqgegLSGGQKQRIALARAFLK-------HAPILVLDEPTAHLDSQTE 521
Cdd:COG4138 98 ASSEAVEQLLAQlAEALGLEDKLSRPLTQ--------LSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVAQQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1590405536 522 QLIQNAIAEYAKNHL-VITIAHRLN-TVKNAKQLIVMENGCIVQQGD 566
Cdd:COG4138 170 AALDRLLRELCQQGItVVMSSHDLNhTLRHADRVWLLKQGKLVASGE 216
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
349-565 |
7.35e-16 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 79.07 E-value: 7.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSNEGIN---NINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQL---Q 422
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHalnNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 423 QSIAWIPQKptlFY----DTLAANIKLgnpsasheALEHAAKQAGALEF-INELPDgfntLIG---------EQgegLSG 488
Cdd:PRK11153 82 RQIGMIFQH---FNllssRTVFDNVAL--------PLELAGTPKAEIKArVTELLE----LVGlsdkadrypAQ---LSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 489 GQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNhLVIT---IAHRLNTVKN-AKQLIVMENGCIVQQ 564
Cdd:PRK11153 144 GQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRE-LGLTivlITHEMDVVKRiCDRVAVIDAGRLVEQ 222
|
.
gi 1590405536 565 G 565
Cdd:PRK11153 223 G 223
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
350-572 |
1.52e-15 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 76.02 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 350 SIHDLNFSYPNSnEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQS-IAWI 428
Cdd:TIGR03410 2 EVSNLNVYYGQS-HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 429 PQK----PTLfydTLAANIKLGnpsashealehAAKQAGALEFI-NELPDGFNTL---IGEQGEGLSGGQKQRIALARAF 500
Cdd:TIGR03410 81 PQGreifPRL---TVEENLLTG-----------LAALPRRSRKIpDEIYELFPVLkemLGRRGGDLSGGQQQQLAIARAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1590405536 501 LKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNH--LVITIAHRLNTVKN-AKQLIVMENGCIVQQGDFKALSQ 572
Cdd:TIGR03410 147 VTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGgmAILLVEQYLDFARElADRYYVMERGRVVASGAGDELDE 221
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
349-565 |
2.00e-15 |
|
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: 75.37 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNsNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTA-----NISQLQQ 423
Cdd:cd03301 1 VELENVTKRFGN-VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLppkdrDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 424 SIAWIPQKPTlfYDTLAANIKLGN--PSASHEALEHAAKQAGALEFINELPDGfntligeqgegLSGGQKQRIALARAFL 501
Cdd:cd03301 80 NYALYPHMTV--YDNIAFGLKLRKvpKDEIDERVREVAELLQIEHLLDRKPKQ-----------LSGGQRQRVALGRAIV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590405536 502 KHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITI--AH-RLNTVKNAKQLIVMENGCIVQQG 565
Cdd:cd03301 147 REPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIyvTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
363-565 |
2.10e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 76.75 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 363 EGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAWIPQKPTLFYD----- 437
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPSTSLNprqri 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 438 --TLAANIKLgNPSASHEALEHAAKQagALEFINELPDGFNTLigeqGEGLSGGQKQRIALARAFLKHAPILVLDEPTAH 515
Cdd:PRK15112 107 sqILDFPLRL-NTDLEPEQREKQIIE--TLRQVGLLPDHASYY----PHMLAPGQKQRLGLARALILRPKVIIADEALAS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1590405536 516 LD-SQTEQLIqNAIAEYAKNHLV--ITIAHRLNTVKN-AKQLIVMENGCIVQQG 565
Cdd:PRK15112 180 LDmSMRSQLI-NLMLELQEKQGIsyIYVTQHLGMMKHiSDQVLVMHQGEVVERG 232
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
368-532 |
2.15e-15 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 75.22 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 368 INLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISqLQQSIAWIPQKPTLfYDTLAA--NIKL 445
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDS-IARGLLYLGHAPGI-KTTLSVleNLRF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 446 GNPSASHEALEHAAKQAGAlefinelpDGFNTLIGEQgegLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQ 525
Cdd:cd03231 97 WHADHSDEQVEEALARVGL--------NGFEDRPVAQ---LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFA 165
|
....*..
gi 1590405536 526 NAIAEYA 532
Cdd:cd03231 166 EAMAGHC 172
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
367-553 |
3.93e-15 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 74.32 E-value: 3.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 367 NINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANiSQLQQSIAWIPQ----KPTLfydTLAAN 442
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQR-DEPHENILYLGHlpglKPEL---SALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 443 IKLGNP-SASHEALEHAAKQAGALEFINELPDGFntligeqgegLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTE 521
Cdd:TIGR01189 94 LHFWAAiHGGAQRTIEDALAAVGLTGFEDLPAAQ----------LSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGV 163
|
170 180 190
....*....|....*....|....*....|...
gi 1590405536 522 QLIQNAIAEY-AKNHLVITIAHRLNTVKNAKQL 553
Cdd:TIGR01189 164 ALLAGLLRAHlARGGIVLLTTHQDLGLVEAREL 196
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
357-584 |
4.82e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 78.23 E-value: 4.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 357 SYPNSNEGI---NNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQ----SIAWIP 429
Cdd:PRK10535 13 SYPSGEEQVevlKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQlrreHFGFIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 430 QKPTLF-YDTLAANIKLgnpSASHEALEHAAKQAGALEFINELpdGFNTLIGEQGEGLSGGQKQRIALARAFLKHAPILV 508
Cdd:PRK10535 93 QRYHLLsHLTAAQNVEV---PAVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVIL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590405536 509 LDEPTAHLDSQTEQLIQNAIAEY-AKNHLVITIAHRLNTVKNAKQLIVMENGCIVQQGDFKALSQQSGEFAKLLQTA 584
Cdd:PRK10535 168 ADEPTGALDSHSGEEVMAILHQLrDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQEKVNVAGGTEPVVNTA 244
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
349-590 |
4.92e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 75.46 E-value: 4.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYpNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCM-----LGFHPEVIQHISIDQQPL--TTANISQL 421
Cdd:PRK14258 8 IKVNNLSFYY-DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrmneLESEVRVEGRVEFFNQNIyeRRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 422 QQSIAWIPQKPTLF----YDTLAANIKL--GNPSASHEAL-EHAAKQAgalefinELPDGFNTLIGEQGEGLSGGQKQRI 494
Cdd:PRK14258 87 RRQVSMVHPKPNLFpmsvYDNVAYGVKIvgWRPKLEIDDIvESALKDA-------DLWDEIKHKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 495 ALARAFLKHAPILVLDEPTAHLDS----QTEQLIQNAiaeYAKNHLVITI-AHRLNTVKnakqlivmengcivQQGDFKA 569
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPiasmKVESLIQSL---RLRSELTMVIvSHNLHQVS--------------RLSDFTA 222
|
250 260
....*....|....*....|.
gi 1590405536 570 LSQqsGEFAKLLQTAEQGVTN 590
Cdd:PRK14258 223 FFK--GNENRIGQLVEFGLTK 241
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
349-566 |
5.71e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 76.80 E-value: 5.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYpNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLttANISQLQQSIAWI 428
Cdd:PRK11607 20 LEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL--SHVPPYQRPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 429 PQKPTLF-YDTLAANIKLGNPSASHEALEHAAKQAGALEFINelpdgFNTLIGEQGEGLSGGQKQRIALARAFLKHAPIL 507
Cdd:PRK11607 97 FQSYALFpHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVH-----MQEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1590405536 508 VLDEPTAHLDSQTEQLIQNA---IAEYAKNHLVITIAHRLNTVKNAKQLIVMENGCIVQQGD 566
Cdd:PRK11607 172 LLDEPMGALDKKLRDRMQLEvvdILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGE 233
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
350-570 |
6.75e-15 |
|
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: 74.25 E-value: 6.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 350 SIHDLNFSYPNSnEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQL-QQSIAWI 428
Cdd:COG0410 5 EVENLHAGYGGI-HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 429 PQKPTLFYD-TLAANIKLGnpsasHEALEHAAKQAGALEFINELpdgFNTL---IGEQGEGLSGGQKQRIALARAFLKHA 504
Cdd:COG0410 84 PEGRRIFPSlTVEENLLLG-----AYARRDRAEVRADLERVYEL---FPRLkerRRQRAGTLSGGEQQMLAIGRALMSRP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590405536 505 PILVLDEPTAHLDSQTEQLIQNAIAEYAKN-----------HLVITIAHRlntvknakqLIVMENGCIVQQGDFKAL 570
Cdd:COG0410 156 KLLLLDEPSLGLAPLIVEEIFEIIRRLNREgvtillveqnaRFALEIADR---------AYVLERGRIVLEGTAAEL 223
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
344-525 |
7.99e-15 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 74.01 E-value: 7.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 344 DANNTISIHDLNFSYPnSNEG----INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFhpEVIQH--ISIDQQPLTTAN 417
Cdd:COG4181 4 SSAPIIELRGLTKTVG-TGAGeltiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGL--DRPTSgtVRLAGQDLFALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 418 ISQL----QQSIAWIPQKPTLFyDTLAA--NIKL-----GNPSASHEA------------LEHAAKQagalefinelpdg 474
Cdd:COG4181 81 EDARarlrARHVGFVFQSFQLL-PTLTAleNVMLplelaGRRDARARArallervglghrLDHYPAQ------------- 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1590405536 475 fntligeqgegLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQT-EQLIQ 525
Cdd:COG4181 147 -----------LSGGEQQRVALARAFATEPAILFADEPTGNLDAATgEQIID 187
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
348-565 |
8.27e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 76.28 E-value: 8.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 348 TISIHDLNFSYPNSnEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQplttaNISQLQ---QS 424
Cdd:PRK10851 2 SIEIANIKKSFGRT-QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT-----DVSRLHardRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 425 IAWIPQKPTLF-YDTLAANIKLG--------NPSAshealeHAAKQ--AGALEFIN--ELPDGFNTligeqgeGLSGGQK 491
Cdd:PRK10851 76 VGFVFQHYALFrHMTVFDNIAFGltvlprreRPNA------AAIKAkvTQLLEMVQlaHLADRYPA-------QLSGGQK 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590405536 492 QRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQN---AIAEYAKNHLVITIAHRLNTVKNAKQLIVMENGCIVQQG 565
Cdd:PRK10851 143 QRVALARALAVEPQILLLDEPFGALDAQVRKELRRwlrQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAG 219
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
365-577 |
1.83e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 73.20 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFhpEVIQ--HISIDQQPLT--TANISQLQQSIAWIPQKPTLF-YDTL 439
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKL--EEITsgDLIVDGLKVNdpKVDERLIRQEAGMVFQQFYLFpHLTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 440 AANIKLGNPSASHEALEHAAKQAGAL-------EFINELPdgfntligeqGEgLSGGQKQRIALARAfLKHAPILVL-DE 511
Cdd:PRK09493 95 LENVMFGPLRVRGASKEEAEKQARELlakvglaERAHHYP----------SE-LSGGQQQRVAIARA-LAVKPKLMLfDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1590405536 512 PTAHLDSQTEQ---LIQNAIAEYAKNHLVITiaHRLNTV-KNAKQLIVMENGCIVQQGDFKAL-----SQQSGEF 577
Cdd:PRK09493 163 PTSALDPELRHevlKVMQDLAEEGMTMVIVT--HEIGFAeKVASRLIFIDKGRIAEDGDPQVLiknppSQRLQEF 235
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
365-565 |
1.97e-14 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 73.14 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQqsIAWIPQKPTLF-----YDTL 439
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERN--VGFVFQHYALFrhmtvFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 440 AANIKLGNPSASHEALEHAAKQAGALEFInELpDGFNTLIGEQgegLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQ 519
Cdd:cd03296 96 AFGLRVKPRSERPPEAEIRAKVHELLKLV-QL-DWLADRYPAQ---LSGGQRQRVALARALAVEPKVLLLDEPFGALDAK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1590405536 520 TEQLIQNAIAEYAK--NHLVITIAH-RLNTVKNAKQLIVMENGCIVQQG 565
Cdd:cd03296 171 VRKELRRWLRRLHDelHVTTVFVTHdQEEALEVADRVVVMNKGRIEQVG 219
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
353-544 |
2.36e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 73.28 E-value: 2.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 353 DLNFSYpNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCM---------------LGFHPEVIQHISIDQqplttan 417
Cdd:PRK14243 15 NLNVYY-GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrlndlipgfrvegkVTFHGKNLYAPDVDP------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 418 iSQLQQSIAWIPQKPTLF----YDTLAANIKL-GNPSASHEALEHAAKQAgALefINELPDGFNtligEQGEGLSGGQKQ 492
Cdd:PRK14243 87 -VEVRRRIGMVFQKPNPFpksiYDNIAYGARInGYKGDMDELVERSLRQA-AL--WDEVKDKLK----QSGLSLSGGQQQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1590405536 493 RIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIAHRL 544
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
349-565 |
2.53e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 73.19 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYpNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAWI 428
Cdd:COG4604 2 IEIKNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 429 PQKPTLfydtlaaNIKL---------------GNPSAshealEHAAKQAGALEFIN--ELPDGFntlIGEqgegLSGGQK 491
Cdd:COG4604 81 RQENHI-------NSRLtvrelvafgrfpyskGRLTA-----EDREIIDEAIAYLDleDLADRY---LDE----LSGGQR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1590405536 492 QRIALARAFLKHAPILVLDEPTAHLD----SQTEQLIQNAIAEYAKNhlVITIAHRLNTVKN-AKQLIVMENGCIVQQG 565
Cdd:COG4604 142 QRAFIAMVLAQDTDYVLLDEPLNNLDmkhsVQMMKLLRRLADELGKT--VVIVLHDINFASCyADHIVAMKDGRVVAQG 218
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
365-565 |
2.61e-14 |
|
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: 72.65 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTtaNISQLQQSIAWIPQKPTLF-YDTLAANI 443
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT--NLPPHKRPVNTVFQNYALFpHLTVFENI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 444 KLG------NPSASHEALEHAAKQAGALEFINELPDGfntligeqgegLSGGQKQRIALARAFLKHAPILVLDEPTAHLD 517
Cdd:cd03300 94 AFGlrlkklPKAEIKERVAEALDLVQLEGYANRKPSQ-----------LSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1590405536 518 SQTEQLIQNAIAEYAKNhLVITIAHRLNTVKNA----KQLIVMENGCIVQQG 565
Cdd:cd03300 163 LKLRKDMQLELKRLQKE-LGITFVFVTHDQEEAltmsDRIAVMNKGKIQQIG 213
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
356-565 |
2.63e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 73.16 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 356 FSYPNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTA------NISQLQQSIAWIP 429
Cdd:PRK14246 17 YLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGkdifqiDAIKLRKEVGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 430 QKPTLF-----YDTLAANIK---LGNPSASHEALEHAAKQAGALEfinELPDGFNTLIGEqgegLSGGQKQRIALARAFL 501
Cdd:PRK14246 97 QQPNPFphlsiYDNIAYPLKshgIKEKREIKKIVEECLRKVGLWK---EVYDRLNSPASQ----LSGGQQQRLTIARALA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1590405536 502 KHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIAHRLNTV-KNAKQLIVMENGCIVQQG 565
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWG 234
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
365-566 |
4.30e-14 |
|
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: 72.08 E-value: 4.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQL-QQSIAWIPQKPTLFYD-TLAAN 442
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIaRLGIGRTFQIPRLFPElTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 443 IKLGNPSASHEAL----------EHAAKQAGALEFInELPDGFNTLIGEqgegLSGGQKQRIALARAFLKHAPILVLDEP 512
Cdd:cd03219 96 VMVAAQARTGSGLllararreerEARERAEELLERV-GLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1590405536 513 TAHLDSQ-TEQLIqNAIAEYAKNHL-VITIAHRLNTVKN-AKQLIVMENGCIVQQGD 566
Cdd:cd03219 171 AAGLNPEeTEELA-ELIRELRERGItVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
359-545 |
4.30e-14 |
|
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: 75.82 E-value: 4.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 359 PNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTaNISQLQQSIAWIPQKPTLFYD- 437
Cdd:TIGR01257 940 PSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHl 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 438 TLAANIKLgnpsasHEALEHAAKQAGALEFINELPD-GFNTLIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHL 516
Cdd:TIGR01257 1019 TVAEHILF------YAQLKGRSWEEAQLEMEAMLEDtGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGV 1092
|
170 180
....*....|....*....|....*....
gi 1590405536 517 DSQTEQLIQNAIAEYAKNHLVITIAHRLN 545
Cdd:TIGR01257 1093 DPYSRRSIWDLLLKYRSGRTIIMSTHHMD 1121
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
358-539 |
4.91e-14 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 70.91 E-value: 4.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 358 YPNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPL--TTANISQLQQSIAWIPQKP--T 433
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdySRKGLLERRQRVGLVFQDPddQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 434 LFYDTLAANIKLG------NPSASHEALEHAAKQAGALEFINELPdgfntligeqgEGLSGGQKQRIALARAFLKHAPIL 507
Cdd:TIGR01166 81 LFAADVDQDVAFGplnlglSEAEVERRVREALTAVGASGLRERPT-----------HCLSGGEKKRVAIAGAVAMRPDVL 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 1590405536 508 VLDEPTAHLD----SQTEQLIQNAIAEyaKNHLVIT 539
Cdd:TIGR01166 150 LLDEPTAGLDpagrEQMLAILRRLRAE--GMTVVIS 183
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
365-566 |
6.56e-14 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 71.77 E-value: 6.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAWIPQK-----PTLFYDTL 439
Cdd:TIGR03873 17 VDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSRRARARRVALVEQDsdtavPLTVRDVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 440 A------ANIKLGNPSASHEALEHAAKQAGALEFINElpdGFNTLigeqgeglSGGQKQRIALARAFLKHAPILVLDEPT 513
Cdd:TIGR03873 97 AlgriphRSLWAGDSPHDAAVVDRALARTELSHLADR---DMSTL--------SGGERQRVHVARALAQEPKLLLLDEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1590405536 514 AHLDSQTEQLIQNAIAEYAKNHLVITIA-HRLN-TVKNAKQLIVMENGCIVQQGD 566
Cdd:TIGR03873 166 NHLDVRAQLETLALVRELAATGVTVVAAlHDLNlAASYCDHVVVLDGGRVVAAGP 220
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
345-520 |
6.88e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 71.35 E-value: 6.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 345 ANNTISIHDLNFSYPNSNEGIN---NINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQ- 420
Cdd:PRK10584 3 AENIVEVHHLKKSVGQGEHELSiltGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEAr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 421 ----------LQQSIAWIPQKPTLFYDTLAANIKLGNPSASHEALEHAAKQAGALEFINELPdgfntligeqgEGLSGGQ 490
Cdd:PRK10584 83 aklrakhvgfVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGE 151
|
170 180 190
....*....|....*....|....*....|
gi 1590405536 491 KQRIALARAFLKHAPILVLDEPTAHLDSQT 520
Cdd:PRK10584 152 QQRVALARAFNGRPDVLFADEPTGNLDRQT 181
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
349-565 |
9.85e-14 |
|
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: 71.27 E-value: 9.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYpNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGF-HPEVIQHISIDQQPLTTANISQLQQSIAW 427
Cdd:COG1119 4 LELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlPPTYGNDVRLFGERRGGEDVWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 428 --------IPQKPTL-------FYDTLaaniklG---NPSASHEAL-EHAAKQAGALEFINELpdgFNTLigeqgeglSG 488
Cdd:COG1119 83 vspalqlrFPRDETVldvvlsgFFDSI------GlyrEPTDEQRERaRELLELLGLAHLADRP---FGTL--------SQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 489 GQKQRIALARAFLKHAPILVLDEPTAHLD-SQTEQLIQnAIAEYAKNHL--VITIAHRLNTVKNA-KQLIVMENGCIVQQ 564
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDlGARELLLA-LLDKLAAEGAptLVLVTHHVEEIPPGiTHVLLLKDGRVVAA 224
|
.
gi 1590405536 565 G 565
Cdd:COG1119 225 G 225
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
365-571 |
1.04e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 72.04 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLG------------FHPEVIQHISIDQQPLTTA------------NISQ 420
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNAlllpdtgtiewiFKDEKNKKKTKEKEKVLEKlviqktrfkkikKIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 421 LQQSIAWIPQ--KPTLFYDTLAANIKLGNPS---ASHEALEHAAKQagaLEFINeLPDGFntlIGEQGEGLSGGQKQRIA 495
Cdd:PRK13651 103 IRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSmgvSKEEAKKRAAKY---IELVG-LDESY---LQRSPFELSGGQKRRVA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1590405536 496 LARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAE-YAKNHLVITIAHRL-NTVKNAKQLIVMENGCIVQQGD-FKALS 571
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLdNVLEWTKRTIFFKDGKIIKDGDtYDILS 254
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
350-542 |
1.09e-13 |
|
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: 73.82 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 350 SIHDLNFSYPNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGfhpeviqhisIDQQPLTTAnISQLQQSIAWIP 429
Cdd:TIGR03719 6 TMNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG----------VDKDFNGEA-RPQPGIKVGYLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 430 QKPTLfyD---TLAANIKLGnpsashealehAAKQAGALEFINEL-------PDGFNTLIGEQGE--------------- 484
Cdd:TIGR03719 75 QEPQL--DptkTVRENVEEG-----------VAEIKDALDRFNEIsakyaepDADFDKLAAEQAElqeiidaadawdlds 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590405536 485 -------------------GLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNhlVITIAH 542
Cdd:TIGR03719 142 qleiamdalrcppwdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGT--VVAVTH 216
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
349-543 |
1.20e-13 |
|
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: 69.10 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLdcmlgfhpEVIQHIsidqQPLTTANISQLQQS-IAW 427
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLF--------RALAGL----WPWGSGRIGMPEGEdLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 428 IPQKPtlfYdtlaaniklgnpsashealehaakqagalefineLPDGfnTLiGEQ-----GEGLSGGQKQRIALARAFLk 502
Cdd:cd03223 69 LPQRP---Y----------------------------------LPLG--TL-REQliypwDDVLSGGEQQRLAFARLLL- 107
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1590405536 503 HAP-ILVLDEPTAHLDSQTEqliqNAIAEYAKNHL--VITIAHR 543
Cdd:cd03223 108 HKPkFVFLDEATSALDEESE----DRLYQLLKELGitVISVGHR 147
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
351-517 |
1.24e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.56 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 351 IHDLNFSYPnSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGfhpeviqhisidQQPLTTANIS-QLQQSIAWIP 429
Cdd:COG0488 1 LENLSKSFG-GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAG------------ELEPDSGEVSiPKGLRIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 430 QKPTLF-----YDT-LAANIKLGNPSASHEALEHA--------AKQAGALEFINEL-------------------PDGFN 476
Cdd:COG0488 68 QEPPLDddltvLDTvLDGDAELRALEAELEELEAKlaepdedlERLAELQEEFEALggweaearaeeilsglgfpEEDLD 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1590405536 477 TLIGEqgegLSGGQKQRIALARAFLKHAPILVLDEPTAHLD 517
Cdd:COG0488 148 RPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
349-566 |
2.01e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 70.79 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGF-HPeviQHISIDQQPLTTANISQLQ---QS 424
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLlRP---QKGKVLVSGIDTGDFSKLQgirKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 425 IAWIPQKP-TLFYD-TLAANIKLGN------PSASHEALEHAAKQAGALEFINELPdgfntligeqgEGLSGGQKQRIAL 496
Cdd:PRK13644 79 VGIVFQNPeTQFVGrTVEEDLAFGPenlclpPIEIRKRVDRALAEIGLEKYRHRSP-----------KTLSGGQGQCVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1590405536 497 ARAFLKHAPILVLDEPTAHLDSQT-EQLIQNAIAEYAKNHLVITIAHRLNTVKNAKQLIVMENGCIVQQGD 566
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
32-306 |
3.14e-13 |
|
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: 70.54 E-value: 3.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 32 LSIALGTVNAILMIAGAYLLAQTIHEVMFEGRnlaqvTQYLWPLAGII----LLRALFLALSERLSAFATLKIKSAIRQT 107
Cdd:cd18542 3 LAILALLLATALNLLIPLLIRRIIDSVIGGGL-----RELLWLLALLIlgvaLLRGVFRYLQGYLAEKASQKVAYDLRND 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 108 LLDKLTQLGPSYIEKNGQGATLNTLHNGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMI 187
Cdd:cd18542 78 LYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 188 LVGHKAEALNQKRWQQLAVL---------GNyffdRVqgltqLKLFNATRKELKQIARISDDFRHATLNVLKIAFLSSFA 258
Cdd:cd18542 158 VFFKKVRPAFEEIREQEGELntvlqenltGV----RV-----VKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPL 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1590405536 259 LEFLATISVALVAVIIGF-----RLFFGTLDFATGFVVLLLapefyLPLRQLG 306
Cdd:cd18542 229 MDFLSGLQIVLVLWVGGYlvingEITLGELVAFISYLWMLI-----WPVRQLG 276
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
348-572 |
3.55e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 69.82 E-value: 3.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 348 TISIHDLNFSYPNSNEgINNINLTLPSTGLVAIVGASGSGKSTLLDcMLGFH-PEVIQHISIDQQPLTTANISQLQQSIA 426
Cdd:PRK10575 11 TFALRNVSFRVPGRTL-LHPLSLTFPAGKVTGLIGHNGSGKSTLLK-MLGRHqPPSEGEILLDAQPLESWSSKAFARKVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 427 WIPQK-PTLFYDTLAANIKLGN----------PSASHEALEHAAKQAGALEFINELPDgfntligeqgeGLSGGQKQRIA 495
Cdd:PRK10575 89 YLPQQlPAAEGMTVRELVAIGRypwhgalgrfGAADREKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 496 LARAFLKHAPILVLDEPTAHLD--SQTE--QLIQNAIAEyaKNHLVITIAHRLN-TVKNAKQLIVMENGCIVQQGDFKAL 570
Cdd:PRK10575 158 IAMLVAQDSRCLLLDEPTSALDiaHQVDvlALVHRLSQE--RGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAEL 235
|
..
gi 1590405536 571 SQ 572
Cdd:PRK10575 236 MR 237
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
365-569 |
4.66e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.15 E-value: 4.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANI-SQLQQSIAWIPQKPTLF-----YDT 438
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFrrlsvYDN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 439 LAANIKLGNPSASHEALEHAakqagalefiNELPDGFNT--LIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHL 516
Cdd:PRK10895 99 LMAVLQIRDDLSAEQREDRA----------NELMEEFHIehLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1590405536 517 DSQTEQLIQNAIAEYAKNHLVITIahrlnTVKNAKQ-LIVMENGCIVQQGDFKA 569
Cdd:PRK10895 169 DPISVIDIKRIIEHLRDSGLGVLI-----TDHNVREtLAVCERAYIVSQGHLIA 217
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
365-584 |
5.64e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 69.33 E-value: 5.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQ---LQQSIAWIpqkptlFYDTLAA 441
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrkaFRRDIQMV------FQDSISA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 442 NiklgNPSAS-----HEALEH------AAKQAGALEFIN--ELPDGFNTLIGEQgegLSGGQKQRIALARAFLKHAPILV 508
Cdd:PRK10419 102 V----NPRKTvreiiREPLRHllsldkAERLARASEMLRavDLDDSVLDKRPPQ---LSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 509 LDEPTAHLD----SQTEQLIQNAIAEYAKNHLVITiaHRLNTVKN-AKQLIVMENGCIVQQ---GDFKALSQQSGefaKL 580
Cdd:PRK10419 175 LDEAVSNLDlvlqAGVIRLLKKLQQQFGTACLFIT--HDLRLVERfCQRVMVMDNGQIVETqpvGDKLTFSSPAG---RV 249
|
....
gi 1590405536 581 LQTA 584
Cdd:PRK10419 250 LQNA 253
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
366-566 |
8.25e-13 |
|
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: 70.87 E-value: 8.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 366 NNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHP---EviqhISIDQQPLTTANISQLQ---QSIAWIPQKPtlfY--- 436
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPsegE----IRFDGQDLDGLSRRALRplrRRMQVVFQDP---Fgsl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 437 -------DTLAANIKLGNPSASHEALEHAAKQAgaLEFINELPDGFNTLIGEqgegLSGGQKQRIALARAFLKHAPILVL 509
Cdd:COG4172 376 sprmtvgQIIAEGLRVHGPGLSAAERRARVAEA--LEEVGLDPAARHRYPHE----FSGGQRQRIAIARALILEPKLLVL 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1590405536 510 DEPTAHLD----SQTEQLIQNAIAEYAKNHLVITiaHRLNTVKN-AKQLIVMENGCIVQQGD 566
Cdd:COG4172 450 DEPTSALDvsvqAQILDLLRDLQREHGLAYLFIS--HDLAVVRAlAHRVMVMKDGKVVEQGP 509
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
380-566 |
9.54e-13 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 69.44 E-value: 9.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 380 IVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTtaNISQLQQSIAWIPQKPTLF-YDTLAANIKLGNPSASHEALEHA 458
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT--NVPPHLRHINMVFQSYALFpHMTVEENVAFGLKMRKVPRAEIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 459 AKQAGALEFINelpdgfntlIGEQGEG----LSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQnaiaeyakn 534
Cdd:TIGR01187 79 PRVLEALRLVQ---------LEEFADRkphqLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQ--------- 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1590405536 535 HLVITIAHRL------------NTVKNAKQLIVMENGCIVQQGD 566
Cdd:TIGR01187 141 LELKTIQEQLgitfvfvthdqeEAMTMSDRIAIMRKGKIAQIGT 184
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
360-565 |
1.16e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 68.50 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 360 NSNEGINNINLTLPSTGLVAIVGASGSGKSTLL---------DCMLGFHPEVIQHiSIDQQPLTTANISQLQQSIAWIPQ 430
Cdd:PRK09984 15 NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsglitgDKSAGSHIELLGR-TVQREGRLARDIRKSRANTGYIFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 431 KPTLFYD-TLAANIKLG---------------NPSASHEALEhAAKQAGALEFINelpdgfntligEQGEGLSGGQKQRI 494
Cdd:PRK09984 94 QFNLVNRlSVLENVLIGalgstpfwrtcfswfTREQKQRALQ-ALTRVGMVHFAH-----------QRVSTLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1590405536 495 ALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNH---LVITIAHRLNTVKNAKQLIVMENGCIVQQG 565
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgitVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
50-321 |
1.32e-12 |
|
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: 68.66 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 50 LLAQTIHEVMFEGRNLAQVTQYLWPLAGIILLRALFLALSERLSAFATLKIKSAIRQTLLDKLTQLGPSYIEKNGQGATL 129
Cdd:cd18576 17 LLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 130 NTLHNGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMILVGHKAEALNQKRWQQLAVLGN 209
Cdd:cd18576 97 SRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 210 YFFDRVQGLTQLKLFNATRKELKQIARISDDFRHATLNVLKI-AFLSSFaLEFLATISVALVaVIIGFRLFF-GTLDFAT 287
Cdd:cd18576 177 IVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIrALFSSF-IIFLLFGAIVAV-LWYGGRLVLaGELTAGD 254
|
250 260 270
....*....|....*....|....*....|....
gi 1590405536 288 GFVVLLLAPEFYLPLRQLGSHYhARLQGISAAAD 321
Cdd:cd18576 255 LVAFLLYTLFIAGSIGSLADLY-GQLQKALGASE 287
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
365-542 |
1.54e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 67.29 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTtanisqlqqsiawIPQKPTLFyDTLAaniK 444
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQ-------------FGREASLI-DAIG---R 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 445 LGNPSASHEALeHAAKQAGALEFINELPDgfntligeqgegLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLI 524
Cdd:COG2401 109 KGDFKDAVELL-NAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRV 175
|
170 180
....*....|....*....|.
gi 1590405536 525 QNAIAEYAKNH---LVITIAH 542
Cdd:COG2401 176 ARNLQKLARRAgitLVVATHH 196
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
367-539 |
1.62e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 67.80 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 367 NINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLT--TANISQLQQSIAWIPQKPTLfydtlaANIK 444
Cdd:PRK11248 19 DINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpGAERGVVFQNEGLLPWRNVQ------DNVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 445 LGNPSAsheALEHAAKQAGALEFINelpdgfntLIGEQGEG------LSGGQKQRIALARAFLKHAPILVLDEPTAHLDS 518
Cdd:PRK11248 93 FGLQLA---GVEKMQRLEIAHQMLK--------KVGLEGAEkryiwqLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
170 180
....*....|....*....|....*
gi 1590405536 519 QTEQLIQNAI----AEYAKNHLVIT 539
Cdd:PRK11248 162 FTREQMQTLLlklwQETGKQVLLIT 186
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
365-559 |
2.27e-12 |
|
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: 66.72 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQ--QSIAWIPQKPTlfYDTLAAN 442
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVvfQNYSLLPWLTV--RENIALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 443 IKLGNPSASHEALEHAAKQAGALEFINELPDGFntlIGEqgegLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQ 522
Cdd:TIGR01184 79 VDRVLPDLSKSERRAIVEEHIALVGLTEAADKR---PGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1590405536 523 LIQNAIAEYAKNH--LVITIAHRLN-TVKNAKQLIVMENG 559
Cdd:TIGR01184 152 NLQEELMQIWEEHrvTVLMVTHDVDeALLLSDRVVMLTNG 191
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
365-530 |
3.31e-12 |
|
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: 66.41 E-value: 3.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQ-LQQSIAWIPQKPTLFYD-TLAAN 442
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKrARLGIGYLPQEASIFRKlTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 443 IKLgnpsasheALEHAAK-QAGALEFINELPDGFN--TLIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQ 519
Cdd:cd03218 96 ILA--------VLEIRGLsKKEREEKLEELLEEFHitHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPI 167
|
170
....*....|.
gi 1590405536 520 TEQLIQNAIAE 530
Cdd:cd03218 168 AVQDIQKIIKI 178
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
368-565 |
3.53e-12 |
|
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: 66.24 E-value: 3.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 368 INLTLPSTGLVAIVGASGSGKSTLLDCMLG-FHPE----VIQHISIDQQPLttanisQLQQSIAWIPQKPTLfYDTLAAN 442
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGlLEPDagfaTVDGFDVVKEPA------EARRRLGFVSDSTGL-YDRLTAR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 443 IKLGNPSASHEALEHAAKQAgalefINELPD--GFNTLIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQT 520
Cdd:cd03266 97 ENLEYFAGLYGLKGDELTAR-----LEELADrlGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1590405536 521 EQLIQNAIAEY-AKNHLVITIAHRLNTVKN-AKQLIVMENGCIVQQG 565
Cdd:cd03266 172 TRALREFIRQLrALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
367-565 |
3.70e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 66.93 E-value: 3.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 367 NINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQSIAWIPQKPTLFYDTLAANIkLG 446
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQEL-VA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 447 NPSASHEAL------EHAAKQAGALEfinelPDGFNTLIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQT 520
Cdd:PRK10253 104 RGRYPHQPLftrwrkEDEEAVTKAMQ-----ATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISH 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1590405536 521 EQLIQNAIAEY--AKNHLVITIAHRLN-TVKNAKQLIVMENGCIVQQG 565
Cdd:PRK10253 179 QIDLLELLSELnrEKGYTLAAVLHDLNqACRYASHLIALREGKIVAQG 226
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
368-565 |
3.89e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.92 E-value: 3.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 368 INLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQQ-SIAWIPQKPTLFYD-TLAANIKL 445
Cdd:PRK15439 30 IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQlGIYLVPQEPLLFPNlSVKENILF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 446 GNPsashealEHAAKQAGALEFINELPDGFNtlIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLD-SQTEQLI 524
Cdd:PRK15439 110 GLP-------KRQASMQKMKQLLAALGCQLD--LDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTpAETERLF 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1590405536 525 QNAIAEYAKNHLVITIAHRLNTVKN-AKQLIVMENGCIVQQG 565
Cdd:PRK15439 181 SRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSG 222
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
365-570 |
5.42e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 67.30 E-value: 5.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTAN---ISQLQQSIAWIPQKPtlfYDTLAA 441
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNP---YGSLNP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 442 NIK----LGNPSASHEALEHAAKQAGAL----------EFINELPDGFntligeqgeglSGGQKQRIALARAFLKHAPIL 507
Cdd:PRK11308 108 RKKvgqiLEEPLLINTSLSAAERREKALammakvglrpEHYDRYPHMF-----------SGGQRQRIAIARALMLDPDVV 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1590405536 508 VLDEPTAHLD----SQTEQLIQNAIAEYAKNHLVITiaHRLNTVKN-AKQLIVMENGCIVQQGDFKAL 570
Cdd:PRK11308 177 VADEPVSALDvsvqAQVLNLMMDLQQELGLSYVFIS--HDLSVVEHiADEVMVMYLGRCVEKGTKEQI 242
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
365-518 |
5.42e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.54 E-value: 5.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHP---EVIQHISIDQQPLttaNISQLQQSIAWIPQK----PTL-FY 436
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPI---DAKEMRAISAYVQQDdlfiPTLtVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 437 DTL--AANIKLGNPSASHEalehaaKQAGALEFINE--LPDGFNTLIGEQG--EGLSGGQKQRIALARAFLKHAPILVLD 510
Cdd:TIGR00955 118 EHLmfQAHLRMPRRVTKKE------KRERVDEVLQAlgLRKCANTRIGVPGrvKGLSGGERKRLAFASELLTDPPLLFCD 191
|
....*...
gi 1590405536 511 EPTAHLDS 518
Cdd:TIGR00955 192 EPTSGLDS 199
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
34-283 |
6.15e-12 |
|
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: 66.67 E-value: 6.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 34 IALGTVNAILMIAgAYLLAQTIHEVMFEGRNLAQVTQYLWPLAGIILLRALFLALSERLSAFATLKIKSAIRQTLLDKLT 113
Cdd:cd18541 6 LFLILVDLLQLLI-PRIIGRAIDALTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 114 QLGPSYIEKNGQGATLNTLHNGVEALHDYYAkylPGVAYSA---LIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMILVG 190
Cdd:cd18541 85 TLSPSFYQKNRTGDLMARATNDLNAVRMALG---PGILYLVdalFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 191 HKAEALNQKRWQQLAVLgnyfFDRVQ----GLTQLKLFNATRKELKQIARISDDFRHATLNVLKI-AFLSSFaLEFLATI 265
Cdd:cd18541 162 KKIHKRFRKVQEAFSDL----SDRVQesfsGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVdALFFPL-IGLLIGL 236
|
250
....*....|....*...
gi 1590405536 266 SVALVAVIIGFRLFFGTL 283
Cdd:cd18541 237 SFLIVLWYGGRLVIRGTI 254
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
345-570 |
6.19e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 66.15 E-value: 6.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 345 ANNTISIHDLNFSYpNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCM----------LGFHPEVIQHISIDQQPLT 414
Cdd:PRK10619 2 SENKLNVIDLHKRY-GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCInflekpsegsIVVNGQTINLVRDKDGQLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 415 TANISQLQ---QSIAWIPQK------PTLFYDTLAANIKLGNPSaSHEALEHAAKqagaleFINELPdgfntlIGEQGEG 485
Cdd:PRK10619 81 VADKNQLRllrTRLTMVFQHfnlwshMTVLENVMEAPIQVLGLS-KQEARERAVK------YLAKVG------IDERAQG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 486 -----LSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQT--EQL-IQNAIAEYAKNHLVITiaHRLNTVKN-AKQLIVM 556
Cdd:PRK10619 148 kypvhLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELvgEVLrIMQQLAEEGKTMVVVT--HEMGFARHvSSHVIFL 225
|
250
....*....|....
gi 1590405536 557 ENGCIVQQGDFKAL 570
Cdd:PRK10619 226 HQGKIEEEGAPEQL 239
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
349-588 |
8.90e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 66.30 E-value: 8.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSY-PNS---NEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTAN----ISQ 420
Cdd:PRK13643 2 IKFEKVNYTYqPNSpfaSRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 421 LQQSIAWIPQKP--TLFYDTLAANIKLG--NPSASHEALEHAAkqAGALEFInelpdGFNTLIGEQGE-GLSGGQKQRIA 495
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGpqNFGIPKEKAEKIA--AEKLEMV-----GLADEFWEKSPfELSGGQMRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 496 LARAFLKHAPILVLDEPTAHLDSQTE-QLIQNAIAEYAKNHLVITIAHRLNTVKN-AKQLIVMENGCIVQQGDFKALSQQ 573
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARiEMMQLFESIHQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQE 234
|
250
....*....|....*
gi 1590405536 574 sgefAKLLQTAEQGV 588
Cdd:PRK13643 235 ----VDFLKAHELGV 245
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
362-573 |
1.34e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 67.04 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 362 NEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLgfhpEVIQ---HISIDQQPLTTANISQL---QQSIAWIPQKPtlf 435
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTTGLALL----RLINsqgEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDP--- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 436 YDTLaaniklgNPSAS------------HEALEHAAKQAGALEFINEL---PDGFNTLIGEqgegLSGGQKQRIALARAF 500
Cdd:PRK15134 372 NSSL-------NPRLNvlqiieeglrvhQPTLSAAQREQQVIAVMEEVgldPETRHRYPAE----FSGGQRQRIAIARAL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 501 LKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLV--ITIAHRLNTVKN-AKQLIVMENGCIVQQGD----FKALSQQ 573
Cdd:PRK15134 441 ILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRAlCHQVIVLRQGEVVEQGDcervFAAPQQE 520
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
366-548 |
2.12e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 66.59 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 366 NNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHP----EviqhISIDQQPLTTANISQ-LQQSIAWIPQKPTLFyDTL- 439
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQpdsgE----ILIDGKPVRIRSPRDaIALGIGMVHQHFMLV-PNLt 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 440 -AANIKLGNPSASHEALEHAAKQAGALEFINELpdGF----NTLIGEqgegLSGGQKQRIALARAFLKHAPILVLDEPTA 514
Cdd:COG3845 97 vAENIVLGLEPTKGGRLDRKAARARIRELSERY--GLdvdpDAKVED----LSVGEQQRVEILKALYRGARILILDEPTA 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 1590405536 515 HLDSQ-TEQLIQnAIAEYAKNHL-VITIAHRLNTVK 548
Cdd:COG3845 171 VLTPQeADELFE-ILRRLAAEGKsIIFITHKLREVM 205
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
353-566 |
2.20e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 64.64 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 353 DLNFSYPNSnEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPL--TTANISQLQQSIAWIPQ 430
Cdd:PRK13638 6 DLWFRYQDE-PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdySKRGLLALRQQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 431 KP--TLFYDTLAANI-----KLGNPSAshealEHAAKQAGALefinelpdgfnTLIGEQG------EGLSGGQKQRIALA 497
Cdd:PRK13638 85 DPeqQIFYTDIDSDIafslrNLGVPEA-----EITRRVDEAL-----------TLVDAQHfrhqpiQCLSHGQKKRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1590405536 498 RAFLKHAPILVLDEPTAHLD----SQTEQLIQNAIAEyaKNHLVITiAHRLNTVKNAKQLI-VMENGCIVQQGD 566
Cdd:PRK13638 149 GALVLQARYLLLDEPTAGLDpagrTQMIAIIRRIVAQ--GNHVIIS-SHDIDLIYEISDAVyVLRQGQILTHGA 219
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
365-572 |
2.21e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 64.34 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKStlLDC--MLGFHPEVIQ----HISIDQQPLTTANISQlqQSIAWIPQKPTLFY-- 436
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKS--LTCaaALGILPAGVRqtagRVLLDGKPVAPCALRG--RKIATIMQNPRSAFnp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 437 ---------DTLAANIKLGNPSASHEALEhaakqAGALEFINELPDGFNTligeqgeGLSGGQKQRIALARAFLKHAPIL 507
Cdd:PRK10418 95 lhtmhtharETCLALGKPADDATLTAALE-----AVGLENAARVLKLYPF-------EMSGGMLQRMMIALALLCEAPFI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 508 VLDEPTAHLD--SQTE--QLIQNAIAEYAKNHLVITiaHRLNTV-KNAKQLIVMENGCIVQQGDFKALSQ 572
Cdd:PRK10418 163 IADEPTTDLDvvAQARilDLLESIVQKRALGMLLVT--HDMGVVaRLADDVAVMSHGRIVEQGDVETLFN 230
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
377-565 |
2.27e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.18 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 377 LVAIVGASGSGKSTLLDCMLGFHPEVIQhISIDQQPLTTANISQLQQSIAWIPQK-------PTLFYDTLaaniklgnps 449
Cdd:PRK03695 24 ILHLVGPNGAGKSTLLARMAGLLPGSGS-IQFAGQPLEAWSAAELARHRAYLSQQqtppfamPVFQYLTL---------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 450 aSHEALEHAAKQAGALEFINE---LPDGFNTLIGEqgegLSGGQKQRIALARAFLK-------HAPILVLDEPTAHLDSQ 519
Cdd:PRK03695 93 -HQPDKTRTEAVASALNEVAEalgLDDKLGRSVNQ----LSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1590405536 520 TEQLIQNAIAEYAKNHLVITIA-HRLN-TVKNAKQLIVMENGCIVQQG 565
Cdd:PRK03695 168 QQAALDRLLSELCQQGIAVVMSsHDLNhTLRHADRVWLLKQGKLLASG 215
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
365-565 |
2.35e-11 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 63.57 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISqlqqSIAWIPQKPTLfYDTLAA--N 442
Cdd:TIGR03740 16 VNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDLH----KIGSLIESPPL-YENLTAreN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 443 IKLgnpsasHEALEHAAKQAgalefINELPDGFN-TLIGEQGEG-LSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQT 520
Cdd:TIGR03740 91 LKV------HTTLLGLPDSR-----IDEVLNIVDlTNTGKKKAKqFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDPIG 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1590405536 521 EQLIQNAIAEYAKNHLVITI-AHRLNTVKN-AKQLIVMENGCIVQQG 565
Cdd:TIGR03740 160 IQELRELIRSFPEQGITVILsSHILSEVQQlADHIGIISEGVLGYQG 206
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
348-559 |
2.45e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.15 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 348 TISIHDLNFSYPNSNEGINNINLTLPSTGLVAIVGASGSGKSTLldCML--GFHPEVIQHISIDQQPLTTANISQLQQSI 425
Cdd:PRK10522 322 TLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTL--AMLltGLYQPQSGEILLDGKPVTAEQPEDYRKLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 426 AWIPQKPTLFYDTLAANIKLGNPSASHEALEHaakqagaLEFIN--ELPDGFNTLIgeqgeGLSGGQKQRIALARAFLKH 503
Cdd:PRK10522 400 SAVFTDFHLFDQLLGPEGKPANPALVEKWLER-------LKMAHklELEDGRISNL-----KLSKGQKKRLALLLALAEE 467
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1590405536 504 APILVLDEPTAHLDSQTEQLIQNAIAEY--AKNHLVITIAHRLNTVKNAKQLIVMENG 559
Cdd:PRK10522 468 RDILLLDEWAADQDPHFRREFYQVLLPLlqEMGKTIFAISHDDHYFIHADRLLEMRNG 525
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
349-570 |
3.38e-11 |
|
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: 65.86 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSNEG---INNINLTLPSTGLVAIVGASGSGKS-TLLdCMLGFHPEVIQH----ISIDQQPLTTANISQ 420
Cdd:COG4172 7 LSVEDLSVAFGQGGGTveaVKGVSFDIAAGETLALVGESGSGKSvTAL-SILRLLPDPAAHpsgsILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 421 LQQ----SIAWIPQKPT-----LF--YDTLAANIKLgnpsasHEALEHAAKQAGALEFINE--LPDGfNTLIGE---Qge 484
Cdd:COG4172 86 LRRirgnRIAMIFQEPMtslnpLHtiGKQIAEVLRL------HRGLSGAAARARALELLERvgIPDP-ERRLDAyphQ-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 485 gLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNH----LVITiaHRLNTVKN-AKQLIVMENG 559
Cdd:COG4172 157 -LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELgmalLLIT--HDLGVVRRfADRVAVMRQG 233
|
250
....*....|.
gi 1590405536 560 CIVQQGDFKAL 570
Cdd:COG4172 234 EIVEQGPTAEL 244
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
365-556 |
3.55e-11 |
|
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: 62.34 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLdcmlgfhpeviqhisidQQPLTTANISQLQQSIAWIPQKPTLFYDTLAANIK 444
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV-----------------NEGLYASGKARLISFLPKFSRNKLIFIDQLQFLID 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 445 LGnpsashealehaakqagalefINELPdgfntlIGEQGEGLSGGQKQRIALARAFLKHAP--ILVLDEPTAHLDSQTEQ 522
Cdd:cd03238 74 VG---------------------LGYLT------LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180 190
....*....|....*....|....*....|....*
gi 1590405536 523 LIQNAIAEY-AKNHLVITIAHRLNTVKNAKQLIVM 556
Cdd:cd03238 127 QLLEVIKGLiDLGNTVILIEHNLDVLSSADWIIDF 161
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
366-547 |
4.29e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 65.58 E-value: 4.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 366 NNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPeviqH------ISIDQQPLTTANISQ--------LQQSIAWIPqk 431
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYP----HgsyegeILFDGEVCRFKDIRDsealgiviIHQELALIP-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 432 ptlfYDTLAANIKLGNPSAS------HEALEHAA---KQAGalefINELPDgfnTLIGEQGEGlsggQKQRIALARAFLK 502
Cdd:NF040905 92 ----YLSIAENIFLGNERAKrgvidwNETNRRARellAKVG----LDESPD---TLVTDIGVG----KQQLVEIAKALSK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1590405536 503 HAPILVLDEPTAHL-DSQTEQLIqNAIAEYaKNHLV--ITIAHRLNTV 547
Cdd:NF040905 157 DVKLLILDEPTAALnEEDSAALL-DLLLEL-KAQGItsIIISHKLNEI 202
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
359-562 |
4.44e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 63.57 E-value: 4.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 359 PNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLT-------TANISQLQQSiawiPQK 431
Cdd:COG1101 16 VNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTklpeykrAKYIGRVFQD----PMM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 432 ---PTLfydTLAANIKLG---------NPSASHEALEHAAKQAGALEfiNELPDGFNTLIGEqgegLSGGQKQRIALARA 499
Cdd:COG1101 92 gtaPSM---TIEENLALAyrrgkrrglRRGLTKKRRELFRELLATLG--LGLENRLDTKVGL----LSGGQRQALSLLMA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1590405536 500 FLKHAPILVLDEPTAHLDSQTEQLI----QNAIAEyakNHL-VITIAHrlntvkNAKQ-------LIVMENGCIV 562
Cdd:COG1101 163 TLTKPKLLLLDEHTAALDPKTAALVleltEKIVEE---NNLtTLMVTH------NMEQaldygnrLIMMHEGRII 228
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
29-309 |
4.50e-11 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 64.03 E-value: 4.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 29 WLKLSIALGTVNAILMIAGAYLLAQTIHEVMFEGrNLAQVTQYLWPLAGIILLRALFLALSERLSAFATLKIKSAIRQTL 108
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLIKIAIDEYIPNG-DLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 109 LDKLTQLGPSYIEKNGQGATLNTLHNGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMIL 188
Cdd:cd18545 80 FSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 189 VGHKAealnQKRWQQ----LAVLGNYFFDRVQGLTQLKLFNATRKELKQIARISDDFRHATLNVLKIAFLSSFALEFLAT 264
Cdd:cd18545 160 LRRRA----RKAWQRvrkkISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISA 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1590405536 265 ISVALVAVIIGFRLFFGTLDFATGFVVLLLAPEFYLPLRQLGSHY 309
Cdd:cd18545 236 LGTALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFY 280
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
346-566 |
4.85e-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: 65.21 E-value: 4.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 346 NNTISIHDLNFSYPNSNEG----INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHP----EVIQHISIDQQPLT--- 414
Cdd:TIGR03269 277 EPIIKVRNVSKRYISVDRGvvkaVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEptsgEVNVRVGDEWVDMTkpg 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 415 -------TANISQLQQSIAWIPQKPTLFYDTLAANIKLGNPSASHEALeHAAKQAG-----ALEFINELPDGfntligeq 482
Cdd:TIGR03269 357 pdgrgraKRYIGILHQEYDLYPHRTVLDNLTEAIGLELPDELARMKAV-ITLKMVGfdeekAEEILDKYPDE-------- 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 483 gegLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAI--AEYAKNHLVITIAHRLNTVKN-AKQLIVMENG 559
Cdd:TIGR03269 428 ---LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDvCDRAALMRDG 504
|
....*..
gi 1590405536 560 CIVQQGD 566
Cdd:TIGR03269 505 KIVKIGD 511
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
350-556 |
6.34e-11 |
|
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: 61.22 E-value: 6.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 350 SIHDLNF-SYPnsnegINNInLTLPSTGLVAIVGASGSGKSTLLDCmlgfhpeviqhisidqqplttanisqlqqsIAWI 428
Cdd:cd03227 1 KIVLGRFpSYF-----VPND-VTFGEGSLTIITGPNGSGKSTILDA------------------------------IGLA 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 429 pqkptLFYDTLAANIKLGNPSASHEALEHAakqagalEFINELPdgfntligeqgeGLSGGQKQRIALARAF----LKHA 504
Cdd:cd03227 45 -----LGGAQSATRRRSGVKAGCIVAAVSA-------ELIFTRL------------QLSGGEKELSALALILalasLKPR 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1590405536 505 PILVLDEPTAHLDSQTEQLIQNAIAEYAKNH-LVITIAHRLNTVKNAKQLIVM 556
Cdd:cd03227 101 PLYILDEIDRGLDPRDGQALAEAILEHLVKGaQVIVITHLPELAELADKLIHI 153
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
349-565 |
1.08e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 63.43 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYpNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTtaNISQLQQSIAWI 428
Cdd:PRK09452 15 VELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT--HVPAENRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 429 PQKPTLF-YDTLAANIKLGNPSASHEALEHAAKQAGAL------EFINELPdgfntligeqgEGLSGGQKQRIALARAFL 501
Cdd:PRK09452 92 FQSYALFpHMTVFENVAFGLRMQKTPAAEITPRVMEALrmvqleEFAQRKP-----------HQLSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1590405536 502 KHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNhLVIT---IAH-RLNTVKNAKQLIVMENGCIVQQG 565
Cdd:PRK09452 161 NKPKVLLLDESLSALDYKLRKQMQNELKALQRK-LGITfvfVTHdQEEALTMSDRIVVMRDGRIEQDG 227
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
363-565 |
1.24e-10 |
|
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: 61.96 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 363 EGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLG-FHP-----EVIQHISIDQQPLTTANISQLqqsiawIPQKPTLFY 436
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGlLQPtsgevRVAGLVPWKRRKKFLRRIGVV------FGQKTQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 437 DTlaaniklgnPSASHEALEHAAKQAGALEF---INELPDGFNT--LIGEQGEGLSGGQKQRIALARAFLkHAP-ILVLD 510
Cdd:cd03267 109 DL---------PVIDSFYLLAAIYDLPPARFkkrLDELSELLDLeeLLDTPVRQLSLGQRMRAEIAAALL-HEPeILFLD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1590405536 511 EPTAHLDSQTEQLIQNAIAEYAKNH--LVITIAHRLNTV-KNAKQLIVMENGCIVQQG 565
Cdd:cd03267 179 EPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIeALARRVLVIDKGRLLYDG 236
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
32-318 |
1.27e-10 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 62.51 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 32 LSIALGTVNAILMIAGAYLLAQTIHEVMfegrnLAQVTQYLWPLAGI----ILLRALFLALSERLSAFATLKIKSAIRQT 107
Cdd:cd18546 3 LALLLVVVDTAASLAGPLLVRYGIDSGV-----RAGDLGVLLLAAAAylavVLAGWVAQRAQTRLTGRTGERLLYDLRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 108 LLDKLTQLGPSYIEKNGQGATLNTLHNGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMI 187
Cdd:cd18546 78 VFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 188 LVGHKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATRKELKQIARISDDFRHATLNVLKIAFLSSFALEFLATISV 267
Cdd:cd18546 158 WFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLAT 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1590405536 268 ALVAVIIGFRLFFGTLDFATGFVVLLLAPEFYLPLRQLGSHYHARLQGISA 318
Cdd:cd18546 238 AAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAA 288
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
367-565 |
1.65e-10 |
|
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: 61.86 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 367 NINLTLPSTGLVAIVGASGSGKSTLLDCMLgfHPEVIQHISI-DQQPLTTANISQLQQ--SIAWIPQKP----------- 432
Cdd:cd03271 13 NIDVDIPLGVLTCVTGVSGSGKSSLINDTL--YPALARRLHLkKEQPGNHDRIEGLEHidKVIVIDQSPigrtprsnpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 433 ---------TLFYD----------TLAanIKLGNPSAS-------HEALEHAAKQAGALEFINELPD---GFNTLiGEQG 483
Cdd:cd03271 91 ytgvfdeirELFCEvckgkrynreTLE--VRYKGKSIAdvldmtvEEALEFFENIPKIARKLQTLCDvglGYIKL-GQPA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 484 EGLSGGQKQRIALARAFLKHAP---ILVLDEPTAHLDSQ-TEQLIQNAIAEYAKNHLVITIAHRLNTVKNAKQLIVM--- 556
Cdd:cd03271 168 TTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHdVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLgpe 247
|
250
....*....|..
gi 1590405536 557 ---ENGCIVQQG 565
Cdd:cd03271 248 ggdGGGQVVASG 259
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
361-564 |
1.74e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 61.37 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 361 SNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTT---ANISQLQ-QSIAWIPQKPTLFY 436
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssAAKAELRnQKLGFIYQFHHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 437 D-----TLAANIKLGNpSASHEALEHAAKQAGALefinelpdGFNTLIGEQGEGLSGGQKQRIALARAFLKHaPILVL-D 510
Cdd:PRK11629 101 DftaleNVAMPLLIGK-KKPAEINSRALEMLAAV--------GLEHRANHRPSELSGGERQRVAIARALVNN-PRLVLaD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1590405536 511 EPTAHLDSQTEQLIQNAIAEYAKNH----LVITiaHRLNTVKNAKQLIVMENGCIVQQ 564
Cdd:PRK11629 171 EPTGNLDARNADSIFQLLGELNRLQgtafLVVT--HDLQLAKRMSRQLEMRDGRLTAE 226
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
66-306 |
2.02e-10 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 62.20 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 66 AQVTQYLWPLAGIILLRALFLALSERLSAFA----TLKIKSAIRQTLLDKLTQLGPSYIEKNGQGATLNTLHNGVEALHD 141
Cdd:cd18565 47 ADPRGQLWLLGGLTVAAFLLESLFQYLSGVLwrrfAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLER 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 142 YYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMILVGHKAEALNQKRWQQLAVLGNYFFDRVQGLTQL 221
Cdd:cd18565 127 FLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVI 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 222 KLFNATRKELKQIARISDDFRHATLNVLKIAFLSSFALEFLATISVALVAVIIGFRLFFGTLDFATG-----FVV-LLLA 295
Cdd:cd18565 207 KAFTAEDFERERVADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVLDGPPLFTGTltvgtLVTfLFYT 286
|
250
....*....|.
gi 1590405536 296 PEFYLPLRQLG 306
Cdd:cd18565 287 QRLLWPLTRLG 297
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
365-534 |
2.28e-10 |
|
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: 59.75 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQ-LQQSIAWIPQKPtlfydtlaani 443
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVPEDR----------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 444 klgnpsashealehaaKQAGALEfinELPDGFNTLIGEQgegLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQL 523
Cdd:cd03215 85 ----------------KREGLVL---DLSVAENIALSSL---LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
170
....*....|.
gi 1590405536 524 IQNAIAEYAKN 534
Cdd:cd03215 143 IYRLIRELADA 153
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
365-565 |
2.91e-10 |
|
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: 60.37 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANisqlQQSIAWIPQKPTLFYDTLAANIK 444
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLPEERGLYPKMKVIDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 445 LgnPSASHEALEHAAKQAGALEFIN--ELPDGFNTLIgeqgEGLSGGQKQRIALARAFLkHAP-ILVLDEPTAHLDSQTE 521
Cdd:cd03269 92 V--YLAQLKGLKKEEARRRIDEWLErlELSEYANKRV----EELSKGNQQKVQFIAAVI-HDPeLLILDEPFSGLDPVNV 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1590405536 522 QLIQNAIAEYA-KNHLVITIAHRLNTVKN-AKQLIVMENGCIVQQG 565
Cdd:cd03269 165 ELLKDVIRELArAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
379-547 |
3.83e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 62.24 E-value: 3.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 379 AIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANI-SQLQQSIAWIPQKPTLFYD-TLAANIKLGNPSASHEALE 456
Cdd:PRK11288 34 ALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTtAALAAGVAIIYQELHLVPEmTVAENLYLGQLPHKGGIVN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 457 HAAKQAGALEFINELPDGF--NTLIGEqgegLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQ-TEQLIQNAIAEYAK 533
Cdd:PRK11288 114 RRLLNYEAREQLEHLGVDIdpDTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTSSLSAReIEQLFRVIRELRAE 189
|
170
....*....|....
gi 1590405536 534 NHLVITIAHRLNTV 547
Cdd:PRK11288 190 GRVILYVSHRMEEI 203
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
348-517 |
4.37e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 61.78 E-value: 4.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 348 TISIHDLNFSYPNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFhpEVIQ--HISIDQQPLTtaNISQLQQSI 425
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGL--ERITsgEIWIGGRVVN--ELEPADRDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 426 AWIPQKPTLF-----YDTLAANIKL-GNPSASHEA-LEHAAKqagALEfINELPDgfntligEQGEGLSGGQKQRIALAR 498
Cdd:PRK11650 79 AMVFQNYALYphmsvRENMAYGLKIrGMPKAEIEErVAEAAR---ILE-LEPLLD-------RKPRELSGGQRQRVAMGR 147
|
170
....*....|....*....
gi 1590405536 499 AFLKHAPILVLDEPTAHLD 517
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNLD 166
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
350-542 |
6.60e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 61.67 E-value: 6.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 350 SIHDLNFSYPNSNEGINNINLT-LPSTGlVAIVGASGSGKSTLLDCMLGfhpeviqhisIDQQPLTTAnisQLQQ--SIA 426
Cdd:PRK11819 8 TMNRVSKVVPPKKQILKDISLSfFPGAK-IGVLGLNGAGKSTLLRIMAG----------VDKEFEGEA---RPAPgiKVG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 427 WIPQKPTLfydtlaaniklgNPSAS-HEALEHA-AKQAGALEFINEL-------PDGFNTLIGEQGE------------- 484
Cdd:PRK11819 74 YLPQEPQL------------DPEKTvRENVEEGvAEVKAALDRFNEIyaayaepDADFDALAAEQGElqeiidaadawdl 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1590405536 485 ---------------------GLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNhlVITIAH 542
Cdd:PRK11819 142 dsqleiamdalrcppwdakvtKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGT--VVAVTH 218
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
364-565 |
7.31e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 61.20 E-value: 7.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 364 GINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQ-----------QSIAWIPQKP 432
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrkkiamvfQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 433 TLfyDTLAANIKLGNPSAS--HEALEHAAKQAGALEFINELPDGfntligeqgegLSGGQKQRIALARAFLKHAPILVLD 510
Cdd:PRK10070 123 VL--DNTAFGMELAGINAEerREKALDALRQVGLENYAHSYPDE-----------LSGGMRQRVGLARALAINPDILLMD 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1590405536 511 EPTAHLDSQTEQLIQNAIAEYAKNH--LVITIAHRLN-TVKNAKQLIVMENGCIVQQG 565
Cdd:PRK10070 190 EAFSALDPLIRTEMQDELVKLQAKHqrTIVFISHDLDeAMRIGDRIAIMQNGEVVQVG 247
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
365-566 |
7.88e-10 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 59.67 E-value: 7.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHP----EviqhISIDQQPLTTANISQL-QQSIAWIPQKPTLFYD-T 438
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRptsgR----ILFDGRDITGLPPHRIaRLGIARTFQNPRLFPElT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 439 LAANIKLG---------------NPSASHEALEHAAKQAGALEFInelpdGFNTLIGEQGEGLSGGQKQRIALARAFLKH 503
Cdd:COG0411 96 VLENVLVAaharlgrgllaallrLPRARREEREARERAEELLERV-----GLADRADEPAGNLSYGQQRRLEIARALATE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590405536 504 APILVLDEPTAHLDSQ-TEQLIQnAIAEYAKNHL--VITIAHRLNTVKN-AKQLIVMENGCIVQQGD 566
Cdd:COG0411 171 PKLLLLDEPAAGLNPEeTEELAE-LIRRLRDERGitILLIEHDMDLVMGlADRIVVLDFGRVIAEGT 236
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
349-565 |
1.05e-09 |
|
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: 58.92 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYpNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHP-----EVIQHISIDQQPLTtanisqLQQ 423
Cdd:cd03265 1 IEVENLVKKY-GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKptsgrATVAGHDVVREPRE------VRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 424 SIAWIPQKPTL-----FYDTLAANIKL-GNPSAshEALEHAAKqagALEFInELPDGFNTLIGEqgegLSGGQKQRIALA 497
Cdd:cd03265 74 RIGIVFQDLSVddeltGWENLYIHARLyGVPGA--ERRERIDE---LLDFV-GLLEAADRLVKT----YSGGMRRRLEIA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1590405536 498 RAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLViTIAHRLNTVKNAKQL----IVMENGCIVQQG 565
Cdd:cd03265 144 RSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGM-TILLTTHYMEEAEQLcdrvAIIDHGRIIAEG 214
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
365-570 |
1.07e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 59.72 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQH-ISID-----QQPLTTANISQLQQSIAWIPQKPTLFYDT 438
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrYSGDvllggRSIFNYRDVLEFRRRVGMLFQRPNPFPMS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 439 LAANIKLGnpSASHEALEHAAKQAGALEFINE--LPDGFNTLIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHL 516
Cdd:PRK14271 117 IMDNVLAG--VRAHKLVPRKEFRGVAQARLTEvgLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSAL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1590405536 517 DSQTEQLIQNAIAEYAKNHLVITIAHRL-NTVKNAKQLIVMENGCIVQQGDFKAL 570
Cdd:PRK14271 195 DPTTTEKIEEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
348-517 |
1.13e-09 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 59.43 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 348 TISIHDLNFSYpNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCM----------LGFHPEVIQHISIDQQPLTTAN 417
Cdd:COG4598 8 ALEVRDLHKSF-GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCInlletpdsgeIRVGGEEIRLKPDRDGELVPAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 418 ISQLQQ---SIAWIPQKPTLF-YDTLAANIK------LGNPSAshEALEHAAK---QAGALEFINELPdgfntligeqgE 484
Cdd:COG4598 87 RRQLQRirtRLGMVFQSFNLWsHMTVLENVIeapvhvLGRPKA--EAIERAEAllaKVGLADKRDAYP-----------A 153
|
170 180 190
....*....|....*....|....*....|...
gi 1590405536 485 GLSGGQKQRIALARAFLKHAPILVLDEPTAHLD 517
Cdd:COG4598 154 HLSGGQQQRAAIARALAMEPEVMLFDEPTSALD 186
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
377-535 |
1.16e-09 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 58.96 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 377 LVAIVGASGSGKSTLLDCMLG-FHPEViqhisidqqplttANISQLQQSIAWIPQK-----PTLFYDTLAANIKlgnpsa 450
Cdd:cd03237 27 VIGILGPNGIGKTTFIKMLAGvLKPDE-------------GDIEIELDTVSYKPQYikadyEGTVRDLLSSITK------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 451 shEALEHAakqagalEFINEL--PDGFNTLIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAI 528
Cdd:cd03237 88 --DFYTHP-------YFKTEIakPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVI 158
|
....*..
gi 1590405536 529 AEYAKNH 535
Cdd:cd03237 159 RRFAENN 165
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
343-566 |
1.30e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.02 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 343 IDANNTISIHDLNFSYPNSNE---GINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTAN-- 417
Cdd:PRK10261 7 LDARDVLAVENLNIAFMQEQQkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrq 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 418 -ISQLQQS-----------IAWIPQKPT-----LFY--DTLAANIKLGNPSASHEALEHAAKQagaLEFInELPDGfNTL 478
Cdd:PRK10261 87 vIELSEQSaaqmrhvrgadMAMIFQEPMtslnpVFTvgEQIAESIRLHQGASREEAMVEAKRM---LDQV-RIPEA-QTI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 479 IGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLD----SQTEQLIQNAIAEYAKNhlVITIAHRLNTVKN-AKQL 553
Cdd:PRK10261 162 LSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDvtiqAQILQLIKVLQKEMSMG--VIFITHDMGVVAEiADRV 239
|
250
....*....|...
gi 1590405536 554 IVMENGCIVQQGD 566
Cdd:PRK10261 240 LVMYQGEAVETGS 252
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
382-529 |
1.36e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 58.32 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 382 GASGSGKSTLLDCMLGF-HPEViQHISIDQQPLTTANISQLqqsIAWIPQKPTLFYDtLAANIKLGNPSASHEalEHAAK 460
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLlHVES-GQIQIDGKTATRGDRSRF---MAYLGHLPGLKAD-LSTLENLHFLCGLHG--RRAKQ 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1590405536 461 QAGALEFINELPDGFNTLIGEqgegLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIA 529
Cdd:PRK13543 117 MPGSALAIVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMIS 181
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
365-539 |
1.75e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 60.33 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGfhpeviqhisidqqplttanisQLQqsiawiPQKPTLfydTLAANIK 444
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITG----------------------QEQ------PDSGTI---EIGETVK 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 445 LGNPSASHEALEhAAKQ-----AGALEFIN----ELPD-----GFNTLIGEQ----GEgLSGGQKQRIALARAFLKHAPI 506
Cdd:TIGR03719 387 LAYVDQSRDALD-PNKTvweeiSGGLDIIKlgkrEIPSrayvgRFNFKGSDQqkkvGQ-LSGGERNRVHLAKTLKSGGNV 464
|
170 180 190
....*....|....*....|....*....|...
gi 1590405536 507 LVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVIT 539
Cdd:TIGR03719 465 LLLDEPTNDLDVETLRALEEALLNFAGCAVVIS 497
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
367-566 |
2.25e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 59.50 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 367 NINLTLPSTGLVAIVGASGSGKSTLLDCMLGF-HPEViQHISIDQQPLTTA----NISQLQQSIAWIPQKPTLF--YdTL 439
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLtRPQK-GRIVLNGRVLFDAekgiCLPPEKRRIGYVFQDARLFphY-KV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 440 AANIKLGnpsASHEALEHAAKQAGALefinelpdGFNTLIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQ 519
Cdd:PRK11144 94 RGNLRYG---MAKSMVAQFDKIVALL--------GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1590405536 520 TEQLIQNAIAEYAK--NHLVITIAHRLNTV-KNAKQLIVMENGCIVQQGD 566
Cdd:PRK11144 163 RKRELLPYLERLAReiNIPILYVSHSLDEIlRLADRVVVLEQGKVKAFGP 212
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
356-570 |
2.27e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 59.33 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 356 FSYPNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQL---QQSIAWIPQKP 432
Cdd:PRK15079 28 WQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravRSDIQMIFQDP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 433 -------TLFYDTLAANIKLGNPSASHEALEHAAK----QAGALE-FINELPDGFntligeqgeglSGGQKQRIALARAF 500
Cdd:PRK15079 108 laslnprMTIGEIIAEPLRTYHPKLSRQEVKDRVKammlKVGLLPnLINRYPHEF-----------SGGQCQRIGIARAL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1590405536 501 LKHAPILVLDEPTAHLD----SQTEQLIQNAIAEYAKNhlVITIAHRLNTVKN-AKQLIVMENGCIVQQGDFKAL 570
Cdd:PRK15079 177 ILEPKLIICDEPVSALDvsiqAQVVNLLQQLQREMGLS--LIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
68-321 |
2.81e-09 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 58.60 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 68 VTQYLWPLAGIILLRALFLALSERLSAFATLKIKSAIRQTLLDKLTQLGPSYIEKNGQGATLNTLHNGVEALHDYYAKYL 147
Cdd:cd18551 35 SGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 148 PGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMILVGHKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNAT 227
Cdd:cd18551 115 PQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 228 RKElkqIARISDDFRHATLNVLKIAFLSSFA--LEFLAtISVALVAVII--GFRLFFGTLDFAT--GFVVLLlapeFYL- 300
Cdd:cd18551 195 ERE---TKRGGEAAERLYRAGLKAAKIEALIgpLMGLA-VQLALLVVLGvgGARVASGALTVGTlvAFLLYL----FQLi 266
|
250 260
....*....|....*....|..
gi 1590405536 301 -PLRQLGSHYhARLQGISAAAD 321
Cdd:cd18551 267 tPLSQLSSFF-TQLQKALGALE 287
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
363-570 |
3.47e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 57.58 E-value: 3.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 363 EGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGfHPEVIQ-HISIDQQPLT---TANIsqLQQSIAWIPQKPTLFYD- 437
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCG-DPRATSgRIVFDGKDITdwqTAKI--MREAVAIVPEGRRVFSRm 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 438 TLAANIKLGNPSASHEALEHAAKQAGALefineLPDGFNTLIGEQGEgLSGGQKQRIALARAFLKHAPILVLDEPTAHLD 517
Cdd:PRK11614 96 TVEENLAMGGFFAERDQFQERIKWVYEL-----FPRLHERRIQRAGT-MSGGEQQMLAIGRALMSQPRLLLLDEPSLGLA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 518 SQTEQLIQNAIAEYAKNHLVITIAHrlntvKNAKQLI-------VMENGCIVQQGDFKAL 570
Cdd:PRK11614 170 PIIIQQIFDTIEQLREQGMTIFLVE-----QNANQALkladrgyVLENGHVVLEDTGDAL 224
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
349-543 |
4.23e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.50 E-value: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYpNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTaNISQLQQSIAWI 428
Cdd:PRK13540 2 LDVIELDFDY-HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 429 PQKPTLF-YDTLAANIKLGNPSAShealehaakqaGALEfINELPDGFNT--LIGEQGEGLSGGQKQRIALARAFLKHAP 505
Cdd:PRK13540 80 GHRSGINpYLTLRENCLYDIHFSP-----------GAVG-ITELCRLFSLehLIDYPCGLLSSGQKRQVALLRLWMSKAK 147
|
170 180 190
....*....|....*....|....*....|....*....
gi 1590405536 506 ILVLDEPTAHLDSQTEQLIQNAIAEY-AKNHLVITIAHR 543
Cdd:PRK13540 148 LWLLDEPLVALDELSLLTIITKIQEHrAKGGAVLLTSHQ 186
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
349-570 |
7.02e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 58.56 E-value: 7.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSNEG---INNINLTLPSTGLVAIVGASGSGKS-TLLDCM-LGFHPEVIQ---HISIDQQPLTTANISQ 420
Cdd:PRK15134 6 LAIENLSVAFRQQQTVrtvVNDVSLQIEAGETLALVGESGSGKSvTALSILrLLPSPPVVYpsgDIRFHGESLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 421 LQQ----SIAWIPQKPTL-----------FYDTLAANIKLGNPSASHEALE--------HAAKQagalefINELPdgfnt 477
Cdd:PRK15134 86 LRGvrgnKIAMIFQEPMVslnplhtlekqLYEVLSLHRGMRREAARGEILNcldrvgirQAAKR------LTDYP----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 478 ligeqgEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLD----SQTEQLIQNAIAEYAKNHLVITiaHRLNTVKN-AKQ 552
Cdd:PRK15134 155 ------HQLSGGERQRVMIAMALLTRPELLIADEPTTALDvsvqAQILQLLRELQQELNMGLLFIT--HNLSIVRKlADR 226
|
250
....*....|....*...
gi 1590405536 553 LIVMENGCIVQQGDFKAL 570
Cdd:PRK15134 227 VAVMQNGRCVEQNRAATL 244
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
375-542 |
8.52e-09 |
|
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: 55.69 E-value: 8.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 375 TGLVAIVGASGSGKSTLLDCML-GFHPEVIQH-ISIDQQP-LTTANISQLQQSIAwipqkptlFYDTLAANIKLgnpSAS 451
Cdd:cd03240 22 SPLTLIVGQNGAGKTTIIEALKyALTGELPPNsKGGAHDPkLIREGEVRAQVKLA--------FENANGKKYTI---TRS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 452 HEALEHAAkqagaleFINElpDGFNTLIGEQGEGLSGGQKQ------RIALARAFLKHAPILVLDEPTAHLDSQ--TEQL 523
Cdd:cd03240 91 LAILENVI-------FCHQ--GESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEniEESL 161
|
170 180
....*....|....*....|..
gi 1590405536 524 IQnaIAEYAK---NHLVITIAH 542
Cdd:cd03240 162 AE--IIEERKsqkNFQLIVITH 181
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
270-520 |
9.59e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.58 E-value: 9.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 270 VAVIIGFRLFFgtldfatgFVVLLLAPEFYLPLRQLG--------SHYHARLQGISAAADMLIILNAP----LPENDDSH 337
Cdd:TIGR00956 672 FGIIIGFTVFF--------FFVYILLTEFNKGAKQKGeilvfrrgSLKRAKKAGETSASNKNDIEAGEvlgsTDLTDESD 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 338 TANINIDAN-----NTISIHDLNFSYPNSNEG---INNIN-LTLPSTgLVAIVGASGSGKSTLLDC-------------- 394
Cdd:TIGR00956 744 DVNDEKDMEkesgeDIFHWRNLTYEVKIKKEKrviLNNVDgWVKPGT-LTALMGASGAGKTTLLNVlaervttgvitggd 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 395 -MLGFHPeviqhisIDqqplttaniSQLQQSIAWIPQKptlfydtlaaNIKLGNpSASHEALEHAA--KQAGAL------ 465
Cdd:TIGR00956 823 rLVNGRP-------LD---------SSFQRSIGYVQQQ----------DLHLPT-STVRESLRFSAylRQPKSVsksekm 875
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1590405536 466 EFIN------ELPDGFNTLIGEQGEGLSGGQKQRIALARAFL-KHAPILVLDEPTAHLDSQT 520
Cdd:TIGR00956 876 EYVEevikllEMESYADAVVGVPGEGLNVEQRKRLTIGVELVaKPKLLLFLDEPTSGLDSQT 937
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
365-565 |
9.73e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 56.54 E-value: 9.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPL---------------TTANISQLQQSIA--- 426
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpghqiarmgvvrTFQHVRLFREMTVien 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 427 -WIPQKPTLFYDTLAANIKLgnPS---ASHEALEHAA---KQAGALEFINElpdgfntligeQGEGLSGGQKQRIALARA 499
Cdd:PRK11300 101 lLVAQHQQLKTGLFSGLLKT--PAfrrAESEALDRAAtwlERVGLLEHANR-----------QAGNLAYGQQRRLEIARC 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1590405536 500 FLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNH--LVITIAHRLNTVKNAKQLI-VMENGCIVQQG 565
Cdd:PRK11300 168 MVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVMGISDRIyVVNQGTPLANG 236
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
378-570 |
1.23e-08 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 57.05 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 378 VAIVGASGSGKSTLLDCMLGFHP----EVIqhisIDQQPLTTANISQLQ---QSIAWIPQKP--------TLfYDTLAAN 442
Cdd:COG4608 47 LGLVGESGCGKSTLGRLLLRLEEptsgEIL----FDGQDITGLSGRELRplrRRMQMVFQDPyaslnprmTV-GDIIAEP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 443 IKLgNPSASHEALEHAAKQAGAL-----EFINELPDGFntligeqgeglSGGQKQRIALARAFLKHAPILVLDEPTAHLD 517
Cdd:COG4608 122 LRI-HGLASKAERRERVAELLELvglrpEHADRYPHEF-----------SGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1590405536 518 -SqteqlIQ----NAIAEYaKNHLVIT---IAHRLNTVKN-AKQLIVMENGCIVQQGDFKAL 570
Cdd:COG4608 190 vS-----IQaqvlNLLEDL-QDELGLTylfISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
360-568 |
1.26e-08 |
|
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: 55.23 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 360 NSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFH-PEVIQ-HISIDQQPLTTANI---SQLQQSIAWipQKPTL 434
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkYEVTEgEILFKGEDITDLPPeerARLGIFLAF--QYPPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 435 FydtlaANIKLGNpsashealehaakqagaleFINELpdgfntligeqGEGLSGGQKQRIALARAFLKHAPILVLDEPTA 514
Cdd:cd03217 89 I-----PGVKNAD-------------------FLRYV-----------NEGFSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1590405536 515 HLDSQTEQLIQNAIAEYAKNH---LVITIAHRLNTVKNAKQLIVMENGCIVQQGDFK 568
Cdd:cd03217 134 GLDIDALRLVAEVINKLREEGksvLIITHYQRLLDYIKPDRVHVLYDGRIVKSGDKE 190
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
366-518 |
1.43e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 56.96 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 366 NNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQ-----PLTTANISQLQQSIAWIPQKPTlfYDTLA 440
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmndvPPAERGVGMVFQSYALYPHLSV--AENMS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 441 ANIKLGNPSASH--EALEHAAK--QAGALefinelpdgfntlIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHL 516
Cdd:PRK11000 98 FGLKLAGAKKEEinQRVNQVAEvlQLAHL-------------LDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
|
..
gi 1590405536 517 DS 518
Cdd:PRK11000 165 DA 166
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
367-534 |
1.56e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.20 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 367 NINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANiSQLQQSIAWIPQ----KPTLF-YDTLAA 441
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR-DEYHQDLLYLGHqpgiKTELTaLENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 442 NIKLGNPsASHEALEHAAKQAGALEFiNELPDGFntligeqgegLSGGQKQRIALARAFLKHAPILVLDEP-TAhLDSQT 520
Cdd:PRK13538 98 YQRLHGP-GDDEALWEALAQVGLAGF-EDVPVRQ----------LSAGQQRRVALARLWLTRAPLWILDEPfTA-IDKQG 164
|
170
....*....|....
gi 1590405536 521 EQLIQNAIAEYAKN 534
Cdd:PRK13538 165 VARLEALLAQHAEQ 178
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
365-567 |
1.79e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.25 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQ-HISIDQQPLTTANISQ-LQQSIAWIPQK-------PTLf 435
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWEgEIFIDGKPVKIRNPQQaIAQGIAMVPEDrkrdgivPVM- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 436 ydTLAANIKLGNPS--ASHEALEHAAKQAGALEFINEL------PDgfnTLIGeqgeGLSGGQKQRIALARAFLKHAPIL 507
Cdd:PRK13549 357 --GVGKNITLAALDrfTGGSRIDDAAELKTILESIQRLkvktasPE---LAIA----RLSGGNQQKAVLAKCLLLNPKIL 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1590405536 508 VLDEPTAHLDSQTEQLIQNAIAEYAKNHL-VITIAHRLNTVKN-AKQLIVMENGCIvqQGDF 567
Cdd:PRK13549 428 ILDEPTRGIDVGAKYEIYKLINQLVQQGVaIIVISSELPEVLGlSDRVLVMHEGKL--KGDL 487
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
380-524 |
2.06e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 55.97 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 380 IVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANiSQLQQSIAWIPQKPTLFYD-TLAANIKLGNPSASHEALEHA 458
Cdd:PRK13537 38 LLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA-RHARQRVGVVPQFDNLDPDfTVRENLLVFGRYFGLSAAAAR 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1590405536 459 AKQAGALEFInELPDGFNTLIGEqgegLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLI 524
Cdd:PRK13537 117 ALVPPLLEFA-KLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLM 177
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
365-570 |
2.77e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 55.99 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTtANISQLQQSIAWIPQKPTLFYD-TLAANI 443
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP-ARARLARARIGVVPQFDNLDLEfTVRENL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 444 KLGNPSASHEALEHAAKQAGALEFInELPDGFNTLIGEqgegLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQL 523
Cdd:PRK13536 136 LVFGRYFGMSTREIEAVIPSLLEFA-RLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHL 210
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1590405536 524 IQNAI-AEYAKNHLVITIAHRLNTVKN-AKQLIVMENGCIVQQGDFKAL 570
Cdd:PRK13536 211 IWERLrSLLARGKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHAL 259
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
365-565 |
2.81e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 55.22 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPE--------VIQHISIDQQPLTTANISQLQQSIAWIPQKPTLFY 436
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGggaprgarVTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 437 DTLAANI-KLGN-PSASHE-ALEHA----AKQAGALEfinelpdGFNTLIGEQGEGLSGGQKQRIALARAFLKHAP---- 505
Cdd:PRK13547 97 AFSAREIvLLGRyPHARRAgALTHRdgeiAWQALALA-------GATALVGRDVTTLSGGELARVQFARVLAQLWPphda 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1590405536 506 -----ILVLDEPTAHLD-SQTEQLIQNAIAEYAKNHL-VITIAHRLN-TVKNAKQLIVMENGCIVQQG 565
Cdd:PRK13547 170 aqpprYLLLDEPTAALDlAHQHRLLDTVRRLARDWNLgVLAIVHDPNlAARHADRIAMLADGAIVAHG 237
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
327-525 |
2.95e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.56 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 327 NAPLPENDDSHTANINIDANNTISIHDLNFSYpNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPeviQHI 406
Cdd:PRK10938 239 GVQLPEPDEPSARHALPANEPRIVLNNGVVSY-NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHP---QGY 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 407 SID-----QQPLTTANISQLQQSIAWIPQKPTLFY--DTLAANIKL-------GNPSASHEALEHAAKQAGALEfinelp 472
Cdd:PRK10938 315 SNDltlfgRRRGSGETIWDIKKHIGYVSSSLHLDYrvSTSVRNVILsgffdsiGIYQAVSDRQQKLAQQWLDIL------ 388
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1590405536 473 dGFNTLIGEQG-EGLSGGQkQRIAL-ARAFLKHAPILVLDEPTAHLDSQTEQLIQ 525
Cdd:PRK10938 389 -GIDKRTADAPfHSLSWGQ-QRLALiVRALVKHPTLLILDEPLQGLDPLNRQLVR 441
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
361-538 |
3.11e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.17 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 361 SNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQ-LQQSIAWIPQkptlfyD-- 437
Cdd:PRK10762 264 SGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANGIVYISE------Drk 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 438 ----TLAANIK-------LGNPSASHEALEHAAKQAGALEFInelpDGFN--TLIGEQGEG-LSGGQKQRIALARAFLKH 503
Cdd:PRK10762 338 rdglVLGMSVKenmsltaLRYFSRAGGSLKHADEQQAVSDFI----RLFNikTPSMEQAIGlLSGGNQQKVAIARGLMTR 413
|
170 180 190
....*....|....*....|....*....|....*
gi 1590405536 504 APILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVI 538
Cdd:PRK10762 414 PKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSI 448
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
486-531 |
3.69e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.50 E-value: 3.69e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1590405536 486 LSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEY 531
Cdd:PRK11147 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSY 486
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
71-284 |
5.26e-08 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 54.79 E-value: 5.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 71 YLWPLAGIILLrALFLALS---ERL-SAFATLKIKSAIRQTLLDKLTQLGPSYIEKNGQGATLNTLHNGVEALHDYYAK- 145
Cdd:cd18585 34 YFTPAAGVRGF-AITRTAGrygERLvSHDATFRLLSNLRVWFYRKLEPLAPARLQKYRSGDLLNRIVADIDTLDNLYLRv 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 146 YLPGVAysALIplAILVVIFPTDY-------KAGLIFLLTAPLIPFFMILVGHK-AEALNQKRwqqlAVLGNYFFDRVQG 217
Cdd:cd18585 113 LSPPVV--ALL--VILATILFLAFfspalalILLAGLLLAGVVIPLLFYRLGKKiGQQLVQLR----AELRTELVDGLQG 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590405536 218 LTQLKLFNATRKELKQIARISDDFRHATLNVLKIAFLSSFALEFLATISVALVAVIIGFRLFFGTLD 284
Cdd:cd18585 185 MAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGLSQALMILLSGLTVWLVLWLGAPLVQNGALD 251
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
349-541 |
5.78e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 53.73 E-value: 5.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISI---DQQPLTTANISQLQQSI 425
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFsghDITRLKNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 426 AWIPQKPTLF-----YDTLAanIKLGNPSASHEALEHaaKQAGALEFINELPDGFNTLIGeqgegLSGGQKQRIALARAF 500
Cdd:PRK10908 82 GMIFQDHHLLmdrtvYDNVA--IPLIIAGASGDDIRR--RVSAALDKVGLLDKAKNFPIQ-----LSGGEQQRVGIARAV 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1590405536 501 LKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIA 541
Cdd:PRK10908 153 VNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMA 193
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
365-573 |
6.65e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 55.22 E-value: 6.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQ-HISIDQQPLTTANISQ-LQQSIAWIPQK-------PTLf 435
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFEgNVFINGKPVDIRNPAQaIRAGIAMVPEDrkrhgivPIL- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 436 ydTLAANIKLG--NPSASHEALEHAAKQAGALEFINEL------PDgfnTLIGeqgeGLSGGQKQRIALARAFLKHAPIL 507
Cdd:TIGR02633 355 --GVGKNITLSvlKSFCFKMRIDAAAELQIIGSAIQRLkvktasPF---LPIG----RLSGGNQQKAVLAKMLLTNPRVL 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 508 VLDEPTAHLDSQTEQLIQNAIAEYAKNHL-VITIAHRLNTVKN-AKQLIVMENGCIvqQGDF--KALSQQ 573
Cdd:TIGR02633 426 ILDEPTRGVDVGAKYEIYKLINQLAQEGVaIIVVSSELAEVLGlSDRVLVIGEGKL--KGDFvnHALTQE 493
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
303-547 |
7.48e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.25 E-value: 7.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 303 RQLGSHYHARLQGISAAadmliilNAPLPENDDSHtaNINIDANNTISIHDLNFSYP-NSNEGINNINLTLPSTGLVAIV 381
Cdd:PLN03073 139 RQREVQYQAHVAEMEAA-------KAGMPGVYVNH--DGNGGGPAIKDIHMENFSISvGGRDLIVDASVTLAFGRHYGLV 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 382 GASGSGKSTLLDCMlGFH-----PEVIQHISIDQ----------QPLTTANISQ---LQQSIAWIPQKPTLFYDTLAANI 443
Cdd:PLN03073 210 GRNGTGKTTFLRYM-AMHaidgiPKNCQILHVEQevvgddttalQCVLNTDIERtqlLEEEAQLVAQQRELEFETETGKG 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 444 KLGNPSASH-----EALEHAAKQagaLEFINEL---PDGFNTLIG---------EQGEGLSGGQKQRIALARAFLKHAPI 506
Cdd:PLN03073 289 KGANKDGVDkdavsQRLEEIYKR---LELIDAYtaeARAASILAGlsftpemqvKATKTFSGGWRMRIALARALFIEPDL 365
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1590405536 507 LVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIAHR-LNTV 547
Cdd:PLN03073 366 LLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREfLNTV 407
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
350-565 |
1.16e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 53.39 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 350 SIHDLNFSYPNSNeGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLG-FHPEV--IQHISIDQQPLTTANISQLQQSI- 425
Cdd:PRK11701 8 SVRGLTKLYGPRK-GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSArLAPDAgeVHYRMRDGQLRDLYALSEAERRRl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 426 ---AW--IPQKPTlfyDTL------AANI--KLGNPSASH------EALEHAAKQAGALEFINELPDGFntligeqgegl 486
Cdd:PRK11701 87 lrtEWgfVHQHPR---DGLrmqvsaGGNIgeRLMAVGARHygdiraTAGDWLERVEIDAARIDDLPTTF----------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 487 SGGQKQRIALARAFLKHaPILVL-DEPTAHLDSQTE----QLIQNAIAEYaknHL-VITIAHRLNTVKN-AKQLIVMENG 559
Cdd:PRK11701 153 SGGMQQRLQIARNLVTH-PRLVFmDEPTGGLDVSVQarllDLLRGLVREL---GLaVVIVTHDLAVARLlAHRLLVMKQG 228
|
....*.
gi 1590405536 560 CIVQQG 565
Cdd:PRK11701 229 RVVESG 234
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
365-517 |
1.32e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 53.19 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFhpeviqhisidQQPLTTANISQLQQSIAWIPQKptLFYD-TLAANI 443
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGL-----------VAPDEGVIKRNGKLRIGYVPQK--LYLDtTLPLTV 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1590405536 444 KlgnpsaSHEALEHAAKQAGALEFINELPDGFntLIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLD 517
Cdd:PRK09544 87 N------RFLRLRPGTKKEDILPALKRVQAGH--LIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
365-573 |
1.44e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.41 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQP---LTTANISQLQQSIawIPQK---------- 431
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynkLDHKLAAQLGIGI--IYQElsvideltvl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 432 PTLFYDTLAANIKLGNPSASHEALEhaaKQAGALEFINELPDGFNTLIGEqgegLSGGQKQRIALARAFLKHAPILVLDE 511
Cdd:PRK09700 99 ENLYIGRHLTKKVCGVNIIDWREMR---VRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1590405536 512 PTAHL-DSQTEQL--IQNAIAEYAKNhlVITIAHRLNTVKN-AKQLIVMENGCIVQQGDFKALSQQ 573
Cdd:PRK09700 172 PTSSLtNKEVDYLflIMNQLRKEGTA--IVYISHKLAEIRRiCDRYTVMKDGSSVCSGMVSDVSND 235
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
311-525 |
1.58e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.48 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 311 ARLQGISAAADMLIILNAP-----LPENDDSHTANInidanntISIHDLNFSYPNSNEGINNINLTLPSTGLVAIVGASG 385
Cdd:PLN03073 473 SRIKALDRLGHVDAVVNDPdykfeFPTPDDRPGPPI-------ISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNG 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 386 SGKSTLLdcmlgfhpeviQHISIDQQPLTTANISQLQQSIAWIPQKPTLFYDtLAANIKL-------GNPSASHEALEHA 458
Cdd:PLN03073 546 IGKSTIL-----------KLISGELQPSSGTVFRSAKVRMAVFSQHHVDGLD-LSSNPLLymmrcfpGVPEQKLRAHLGS 613
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1590405536 459 AKQAGALEFinelpdgfntligEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLD-SQTEQLIQ 525
Cdd:PLN03073 614 FGVTGNLAL-------------QPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDlDAVEALIQ 668
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
19-321 |
1.87e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 52.90 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 19 LKQQSKPAAMWLKLSIALGTVNAILMIAGAYLlaqtihevmfegrnlaqvtqylwplaGIILLRALFLALSERLSAFATL 98
Cdd:cd18564 30 LGDKPLPGLLGLAPLLGPDPLALLLLAAAALV--------------------------GIALLRGLASYAGTYLTALVGQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 99 KIKSAIRQTLLDKLTQLGPSYIEKNGQGATLNTLHNGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLT 178
Cdd:cd18564 84 RVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIALAV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 179 APLIPFFMILVGHK-AEALNQKRWQQLAVLGnyffdRVQ-GLTQLKL---FNATRKELKQIARISDDFRHATLNVLKIAF 253
Cdd:cd18564 164 APLLLLAARRFSRRiKEASREQRRREGALAS-----VAQeSLSAIRVvqaFGREEHEERRFARENRKSLRAGLRAARLQA 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590405536 254 LSSFALEFLATISVALVaviigfrLFFGTLDFATG---------FVVLLLApeFYLPLRQLgSHYHARLQGISAAAD 321
Cdd:cd18564 239 LLSPVVDVLVAVGTALV-------LWFGAWLVLAGrltpgdllvFLAYLKN--LYKPVRDL-AKLTGRIAKASASAE 305
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
486-561 |
2.03e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 54.21 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 486 LSGGQKQRIALARAF----LKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIAHRLNTVKNAKQLIVM---EN 558
Cdd:pfam02463 1078 LSGGEKTLVALALIFaiqkYKPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVGVtmvEN 1157
|
...
gi 1590405536 559 GCI 561
Cdd:pfam02463 1158 GVS 1160
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
99-305 |
2.05e-07 |
|
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: 52.81 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 99 KIKSAIRQTLLDKLTQLGPSYIEKNGQGATLNTLHNGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLt 178
Cdd:cd18554 76 KILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLV- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 179 apLIPFFMILVGH---KAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATRKELKQIARISDDFRHATLNVLKIAFLS 255
Cdd:cd18554 155 --IFPFYILAVKYffgRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKT 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1590405536 256 SFALEFLATISVALVAVIIGFRLFFGTLDFATGFVVLLLAPEFYLPLRQL 305
Cdd:cd18554 233 FSAVNTITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRL 282
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
378-562 |
2.25e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 53.48 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 378 VAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQ-LQQSIAWIP---QKPTLFYD-TLAANIKLGNPS--A 450
Cdd:COG1129 281 LGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYVPedrKGEGLVLDlSIRENITLASLDrlS 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 451 SHEALEHAAKQAGALEFINEL---PDGFNTLIGEqgegLSGGQKQRIALARAFLKHAPILVLDEPTAHLD--SQTEqlIQ 525
Cdd:COG1129 361 RGGLLDRRRERALAEEYIKRLrikTPSPEQPVGN----LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDvgAKAE--IY 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1590405536 526 NAIAEYAKNHL-----------VITIAHRlntvknakqLIVMENGCIV 562
Cdd:COG1129 435 RLIRELAAEGKavivisselpeLLGLSDR---------ILVMREGRIV 473
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
486-544 |
2.55e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.66 E-value: 2.55e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1590405536 486 LSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVITIAHRL 544
Cdd:PRK13409 213 LSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
343-543 |
2.69e-07 |
|
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: 53.60 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 343 IDANNTISIHDLNFSYPNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQplttanisqlq 422
Cdd:TIGR00954 446 EYQDNGIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAK----------- 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 423 QSIAWIPQKPTLFYDTLAANIKLgnPSASHEALEHAAKQAgALEFINELPDGFNTLIGEQG--------EGLSGGQKQRI 494
Cdd:TIGR00954 515 GKLFYVPQRPYMTLGTLRDQIIY--PDSSEDMKRRGLSDK-DLEQILDNVQLTHILEREGGwsavqdwmDVLSGGEKQRI 591
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1590405536 495 ALARAFLkHAPIL-VLDEPTAHLDSQTEQLIQNAIAEYAKNhlVITIAHR 543
Cdd:TIGR00954 592 AMARLFY-HKPQFaILDECTSAVSVDVEGYMYRLCREFGIT--LFSVSHR 638
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
365-565 |
2.98e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 52.44 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGF--HPEVI--QHISIDQQPLTTANISQLQQ----SIAWIPQKP---- 432
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidYPGRVmaEKLEFNGQDLQRISEKERRNlvgaEVAMIFQDPmtsl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 433 ----TLFYDTLAAnIKLgnpsasHEALEHAAKQAGALEFINE--LPDGFNTL--IGEQgegLSGGQKQRIALARAFLKHA 504
Cdd:PRK11022 103 npcyTVGFQIMEA-IKV------HQGGNKKTRRQRAIDLLNQvgIPDPASRLdvYPHQ---LSGGMSQRVMIAMAIACRP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1590405536 505 PILVLDEPTAHLDSQTEQLIQNAIAEYAK--NHLVITIAHRLNTV-KNAKQLIVMENGCIVQQG 565
Cdd:PRK11022 173 KLLIADEPTTALDVTIQAQIIELLLELQQkeNMALVLITHDLALVaEAAHKIIVMYAGQVVETG 236
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
377-543 |
4.65e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 52.96 E-value: 4.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 377 LVAIVGASGSGKSTLLDCMLGfhpeVIQHISIDQQPLTTAN--ISQLQQSIAWIPQKPTLF-----YDTLAANIKLGNPs 449
Cdd:PLN03211 96 ILAVLGPSGSGKSTLLNALAG----RIQGNNFTGTILANNRkpTKQILKRTGFVTQDDILYphltvRETLVFCSLLRLP- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 450 ashEALEHAAKQAGALEFINELpdGF----NTLIGEQG-EGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTE-QL 523
Cdd:PLN03211 171 ---KSLTKQEKILVAESVISEL--GLtkceNTIIGNSFiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAyRL 245
|
170 180
....*....|....*....|
gi 1590405536 524 IQNAIAEYAKNHLVITIAHR 543
Cdd:PLN03211 246 VLTLGSLAQKGKTIVTSMHQ 265
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
365-528 |
5.14e-07 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 50.32 E-value: 5.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGF-HPEVIQ-HISIDQQPLTTAnisqLQQSIAWIPQKPTLFydtlaan 442
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRkTAGVITgEILINGRPLDKN----FQRSTGYVEQQDVHS------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 443 iklgnPSAS-HEALEHAAKQagalefinelpdgfntligeqgEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTE 521
Cdd:cd03232 92 -----PNLTvREALRFSALL----------------------RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAA 144
|
....*..
gi 1590405536 522 QLIQNAI 528
Cdd:cd03232 145 YNIVRFL 151
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
486-538 |
5.27e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.50 E-value: 5.27e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1590405536 486 LSGGQKQRIALARAFLKHAPILVLDEPTAHLDSqtEQLIQ--NAIAEYAKNH----LVI 538
Cdd:PRK13409 454 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDV--EQRLAvaKAIRRIAEEReataLVV 510
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
365-539 |
1.27e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.27 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGfhpeviqhisiDQQPLT-------TANISQLQQSIAWIPQKPTLF-- 435
Cdd:PRK11819 340 IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITG-----------QEQPDSgtikigeTVKLAYVDQSRDALDPNKTVWee 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 436 ----YDTlaanIKLGN---PSASHealehaakqAGAlefinelpdgFNTLIGEQ----GEgLSGGQKQRIALARAFLKHA 504
Cdd:PRK11819 409 isggLDI----IKVGNreiPSRAY---------VGR----------FNFKGGDQqkkvGV-LSGGERNRLHLAKTLKQGG 464
|
170 180 190
....*....|....*....|....*....|....*
gi 1590405536 505 PILVLDEPTAHLDSQTEQLIQNAIAEYAKNHLVIT 539
Cdd:PRK11819 465 NVLLLDEPTNDLDVETLRALEEALLEFPGCAVVIS 499
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
360-566 |
1.35e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.03 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 360 NSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGfHP--EVI------QHISIDQqpLTTANISQLQQSIAW---- 427
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-HPayKILegdilfKGESILD--LEPEERAHLGIFLAFqypi 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 428 -IPQKPTLFYDTLAANIK---LGNPSAshEALEHaakqagaLEFINELPDgfntLIGEQ--------GEGLSGGQKQRIA 495
Cdd:CHL00131 95 eIPGVSNADFLRLAYNSKrkfQGLPEL--DPLEF-------LEIINEKLK----LVGMDpsflsrnvNEGFSGGEKKRNE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1590405536 496 LARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYA-KNHLVITIAH--RLNTVKNAKQLIVMENGCIVQQGD 566
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
378-546 |
1.56e-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: 48.14 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 378 VAIVGASGSGKSTLLDCMLGFhpeviqhisidqqplttanisqlqqsiawipqkptlfYDTLAANIKLGNPSASHEALEH 457
Cdd:smart00382 5 ILIVGPPGSGKTTLARALARE-------------------------------------LGPPGGGVIYIDGEDILEEVLD 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 458 AAKqagalefinelpdgfNTLIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQ-------NAIAE 530
Cdd:smart00382 48 QLL---------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelrlLLLLK 112
|
170
....*....|....*.
gi 1590405536 531 YAKNHLVITIAHRLNT 546
Cdd:smart00382 113 SEKNLTVILTTNDEKD 128
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
486-538 |
1.58e-06 |
|
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: 50.94 E-value: 1.58e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1590405536 486 LSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNH----LVI 538
Cdd:COG1245 456 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRgktaMVV 512
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
349-553 |
2.30e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 48.33 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLNFSYPNSNegINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFhpeviqhisidQQPlTTANISQLQQSIAWI 428
Cdd:PRK13541 2 LSLHQLQFNIEQKN--LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGI-----------MQP-SSGNIYYKNCNINNI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 429 pQKPTLFYdtLAANIKLGNPSASHEALEHAAKQAGALEFINELPDGF--NTLIGEQGEGLSGGQKQRIALARAFLKHAPI 506
Cdd:PRK13541 68 -AKPYCTY--IGHNLGLKLEMTVFENLKFWSEIYNSAETLYAAIHYFklHDLLDEKCYSLSSGMQKIVAIARLIACQSDL 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1590405536 507 LVLDEPTAHLDSQTEQLIQNAIAEYAKN-HLVITIAHRLNTVKNAKQL 553
Cdd:PRK13541 145 WLLDEVETNLSKENRDLLNNLIVMKANSgGIVLLSSHLESSIKSAQIL 192
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
367-565 |
4.71e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 48.02 E-value: 4.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 367 NINLTLPSTGLVAIVGASGSGKSTL-LDC---------MLGFHPEVIQHISIDQQPLTTaNISQLQQSIAwIPQKP---- 432
Cdd:cd03270 13 NVDVDIPRNKLVVITGVSGSGKSSLaFDTiyaegqrryVESLSAYARQFLGQMDKPDVD-SIEGLSPAIA-IDQKTtsrn 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 433 --------TLFYDTLA---ANIKLGNpsashealehaakqagALEFINELPDGFNTLiGEQGEGLSGGQKQRIALAR--- 498
Cdd:cd03270 91 prstvgtvTEIYDYLRllfARVGIRE----------------RLGFLVDVGLGYLTL-SRSAPTLSGGEAQRIRLATqig 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1590405536 499 AFLKHApILVLDEPTAHL-DSQTEQLIQNAIAEYAKNHLVITIAHRLNTVKNAKQLIVM------ENGCIVQQG 565
Cdd:cd03270 154 SGLTGV-LYVLDEPSIGLhPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDIgpgagvHGGEIVAQG 226
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
365-554 |
4.89e-06 |
|
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: 49.63 E-value: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCML---------------GFHPEVI--QHIS----IDQQ---------PLT 414
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINDTLypalanrlngaktvpGRYTSIEglEHLDkvihIDQSpigrtprsnPAT 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 415 -TANISQLQQSIAWIPQKPTLFYDT--LAANIKLG---------------------------------NPSA-------- 450
Cdd:TIGR00630 704 yTGVFDEIRELFAETPEAKVRGYTPgrFSFNVKGGrceacqgdgvikiemhflpdvyvpcevckgkryNRETlevkykgk 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 451 -SHEALEHAAKQAgaLEFINELPD-------------GFNTLiGEQGEGLSGGQKQRIALARAFLK---HAPILVLDEPT 513
Cdd:TIGR00630 784 nIADVLDMTVEEA--YEFFEAVPSisrklqtlcdvglGYIRL-GQPATTLSGGEAQRIKLAKELSKrstGRTLYILDEPT 860
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1590405536 514 A--HLD--SQTEQLIQNAIaeyAKNHLVITIAHRLNTVKNAKQLI 554
Cdd:TIGR00630 861 TglHFDdiKKLLEVLQRLV---DKGNTVVVIEHNLDVIKTADYII 902
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
60-288 |
8.54e-06 |
|
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: 47.86 E-value: 8.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 60 FEGRNLAQVTQYLWPLAGIILLRALFLA--------LSERLSAfatlkiksAIRQTLLDKLTQLGPSYIEKNGQGATLNT 131
Cdd:cd18575 27 FAAGNTALLNRAFLLLLAVALVLALASAlrfylvswLGERVVA--------DLRKAVFAHLLRLSPSFFETTRTGEVLSR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 132 LHNGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMILVGHKAEALNQKRWQQLAVLGNYF 211
Cdd:cd18575 99 LTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1590405536 212 FDRVQGLTQLKLFNatrKELKQIARisddFRHATLNVLKIAFLSSFALEFLATISVALVAVIIGFRLFFGTLDFATG 288
Cdd:cd18575 179 EETLSAIKTVQAFT---REDAERQR----FATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGAHDVLAG 248
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
344-576 |
8.74e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 49.24 E-value: 8.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 344 DANNTISIHDLNFSYP-NSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTaNISQLQ 422
Cdd:TIGR01257 1933 NKTDILRLNELTKVYSgTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVH 2011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 423 QSIAWIPQKPTLfYDTLAANIKL-------GNPSASHEALEHAAKQAGALefinelpdgfnTLIGEQGEG-LSGGQKQRI 494
Cdd:TIGR01257 2012 QNMGYCPQFDAI-DDLLTGREHLylyarlrGVPAEEIEKVANWSIQSLGL-----------SLYADRLAGtYSGGNKRKL 2079
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 495 ALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKN-HLVITIAHRLNTVKN-AKQLIVMENGCIVQQGDFKALSQ 572
Cdd:TIGR01257 2080 STAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREgRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKS 2159
|
....
gi 1590405536 573 QSGE 576
Cdd:TIGR01257 2160 KFGD 2163
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
345-547 |
1.12e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 47.80 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 345 ANNTISIHDLN--FSYPNSN-EGINNINLTLPSTGLVAIVGASGSGKS-TLLDCM--LGFHPEVIQHISIDQQPLTTANI 418
Cdd:PRK09473 9 ADALLDVKDLRvtFSTPDGDvTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMglLAANGRIGGSATFNGREILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 419 SQLQ----QSIAWIPQKPTLF---Y----DTLAANIKLGNPSASHEALEH------AAKQAGALEFINELPDGFntlige 481
Cdd:PRK09473 89 KELNklraEQISMIFQDPMTSlnpYmrvgEQLMEVLMLHKGMSKAEAFEEsvrmldAVKMPEARKRMKMYPHEF------ 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1590405536 482 qgeglSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAK--NHLVITIAHRLNTV 547
Cdd:PRK09473 163 -----SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVV 225
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
365-570 |
1.19e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 48.31 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQLQ---QSIAWIPQKPtlfYDTLAA 441
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQalrRDIQFIFQDP---YASLDP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 442 NIKLG----NPSASHEAL--EHAAKQ-AGALEFINELPDGFNTLIGEqgegLSGGQKQRIALARAFLKHAPILVLDEPTA 514
Cdd:PRK10261 417 RQTVGdsimEPLRVHGLLpgKAAAARvAWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEAVS 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1590405536 515 HLDSQTEQLIQNAIAEYAKNHLV--ITIAHRLNTVKN-AKQLIVMENGCIVQQGDFKAL 570
Cdd:PRK10261 493 ALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAV 551
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
473-538 |
1.32e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.03 E-value: 1.32e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 473 DGFNTLIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQ----TEQLIQNAIAEYAKNHLVI 538
Cdd:cd03222 59 DGITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnAARAIRRLSEEGKKTALVV 128
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
75-276 |
1.50e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 47.19 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 75 LAGIILLRALFLALSERLSAFATLKIKSAIRQTLLDKLTQLGPSYIEKNGQGATLNTLhNGVEALHDYYAkylpGVAYSA 154
Cdd:cd18566 48 VVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERL-NSLEQIREFLT----GQALLA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 155 LI--PLAI--LVVIFPTDYKAGLIFLLTAPLIPFFMILVGHKAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATRKE 230
Cdd:cd18566 123 LLdlPFVLifLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQM 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1590405536 231 LKQIARISddfRHATLNVLKIAFLSSFALEFLATISVALVAVIIGF 276
Cdd:cd18566 203 LRRYERLQ---ANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAF 245
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
345-512 |
1.64e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 46.68 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 345 ANNTISIHDLNFSYPNsNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQL--- 421
Cdd:PRK11831 4 VANLVDMRGVSFTRGN-RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 422 QQSIAWIPQKPTLFYD-TLAANIKLgnPSASHEALEHAAKQAGA---LEFINeLPDGFNTLIGEqgegLSGGQKQRIALA 497
Cdd:PRK11831 83 RKRMSMLFQSGALFTDmNVFDNVAY--PLREHTQLPAPLLHSTVmmkLEAVG-LRGAAKLMPSE----LSGGMARRAALA 155
|
170
....*....|....*
gi 1590405536 498 RAFLKHAPILVLDEP 512
Cdd:PRK11831 156 RAIALEPDLIMFDEP 170
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
486-544 |
3.78e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 46.70 E-value: 3.78e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1590405536 486 LSGGQKQRIALARAFLKHAPILVLDEPTAHLDSqTEQL-IQNAIAEYAK-NHLVITIAHRL 544
Cdd:COG1245 213 LSGGELQRVAIAAALLRDADFYFFDEPSSYLDI-YQRLnVARLIRELAEeGKYVLVVEHDL 272
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
480-554 |
4.62e-05 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 44.22 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 480 GEQGEGLSGGQKQRIALARAF----LKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKNHL-VITIAHRLNTVKNAKQLI 554
Cdd:cd03239 89 GKVEQILSGGEKSLSALALIFalqeIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHTSqFIVITLKKEMFENADKLI 168
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
349-559 |
4.64e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 46.20 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHDLnfsypnSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQHISIDQQPLTTANISQ-LQQSIAW 427
Cdd:PRK15439 269 LTVEDL------TGEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVY 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 428 IP---QKPTLFYDT-LAANIKlgnpSASHEAL---EHAAKQAGALE-FINELPDGFNTLigEQG-EGLSGGQKQRIALAR 498
Cdd:PRK15439 343 LPedrQSSGLYLDApLAWNVC----ALTHNRRgfwIKPARENAVLErYRRALNIKFNHA--EQAaRTLSGGNQQKVLIAK 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1590405536 499 AFLKHAPILVLDEPTAHLD----SQTEQLIQNaIAeyAKNHLVITIAHRLNTV-KNAKQLIVMENG 559
Cdd:PRK15439 417 CLEASPQLLIVDEPTRGVDvsarNDIYQLIRS-IA--AQNVAVLFISSDLEEIeQMADRVLVMHQG 479
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
349-520 |
5.02e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.10 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 349 ISIHD--LNFSYpnsNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGfhpEVIQ---HISIDQQplttANISQLQQ 423
Cdd:PRK11147 4 ISIHGawLSFSD---APLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNG---EVLLddgRIIYEQD----LIVARLQQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 424 SiawiPQK--PTLFYDTLAANIK----------------LGNPSASH--------EALEHAakqaGALEFINELPDGFnT 477
Cdd:PRK11147 74 D----PPRnvEGTVYDFVAEGIEeqaeylkryhdishlvETDPSEKNlnelaklqEQLDHH----NLWQLENRINEVL-A 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1590405536 478 LIGEQGEG----LSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQT 520
Cdd:PRK11147 145 QLGLDPDAalssLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
377-566 |
5.71e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.26 E-value: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 377 LVAIVGASGSGKSTLLDCML----GFHPEVIQHISIDQqpLTTANI-SQLQQSIAWIPQKPTLF-----YDTLAANIKLG 446
Cdd:TIGR00956 89 LTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDG--ITPEEIkKHYRGDVVYNAETDVHFphltvGETLDFAARCK 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 447 NPSASHEAL---EHAAKQAGALEFINELPDGFNTLIG-EQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQ 522
Cdd:TIGR00956 167 TPQNRPDGVsreEYAKHIADVYMATYGLSHTRNTKVGnDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATAL 246
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1590405536 523 LIQNAI---AEYAKNHLVITIahrLNTVKNAKQL----IVMENGCIVQQGD 566
Cdd:TIGR00956 247 EFIRALktsANILDTTPLVAI---YQCSQDAYELfdkvIVLYEGYQIYFGP 294
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
355-525 |
6.69e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 44.23 E-value: 6.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 355 NFsypNSNEGINNINLTLpstGLVAIVGASGSGKSTLLDCM-LGF--------------------HPEVIQHISIDQQP- 412
Cdd:COG0419 9 NF---RSYRDTETIDFDD---GLNLIVGPNGAGKSTILEAIrYALygkarsrsklrsdlinvgseEASVELEFEHGGKRy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 413 -----------LTTANISQLQQSIAwipqkpTLF----YDTLAANIKlgnpsASHEALEHAAKQAGALEFINElpDGFNT 477
Cdd:COG0419 83 rierrqgefaeFLEAKPSERKEALK------RLLgleiYEELKERLK-----ELEEALESALEELAELQKLKQ--EILAQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1590405536 478 LIG-EQGEGLSGGQKQRIALARAFLkhapiLVLDepTAHLDSQT-EQLIQ 525
Cdd:COG0419 150 LSGlDPIETLSGGERLRLALADLLS-----LILD--FGSLDEERlERLLD 192
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
346-531 |
1.24e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.88 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 346 NNTISIHDLNFSYPNsNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGfhpeviqhisidqqplttaNISQLQQSI 425
Cdd:PRK15064 317 RNALEVENLTKGFDN-GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVG-------------------ELEPDSGTV 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 426 AWipqkptlfydtlAANIKLGnpsasHEALEHAAkqagalEFINELpdgfnTL--------------------------- 478
Cdd:PRK15064 377 KW------------SENANIG-----YYAQDHAY------DFENDL-----TLfdwmsqwrqegddeqavrgtlgrllfs 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1590405536 479 ---IGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEY 531
Cdd:PRK15064 429 qddIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKY 484
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
365-565 |
1.58e-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: 43.29 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLdcmlgfhpEVIQHISidqqPLTTANISqLQQSIAWIpqkptlfydtLAANIK 444
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLL--------RLLAGIY----PPDSGTVT-VRGRVSSL----------LGLGGG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 445 LgNPSASHE------ALEHAAKQAGALEFIN------ELPDGFNTLIGEqgegLSGGQKQRIALARAFLKHAPILVLDEP 512
Cdd:cd03220 95 F-NPELTGReniylnGRLLGLSRKEIDEKIDeiiefsELGDFIDLPVKT----YSSGMKARLAFAIATALEPDILLIDEV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1590405536 513 TAHLDSQTEQLIQNAIAEYAKNH-LVITIAHRLNTVKN-AKQLIVMENGCIVQQG 565
Cdd:cd03220 170 LAVGDAAFQEKCQRRLRELLKQGkTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
486-554 |
1.69e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 1.69e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1590405536 486 LSGGQKQRIALARAFL---KHAPILVLDEPTAHLDSQ-TEQLIQNAIAEYAKNHLVITIAHRLNTVKNAKQLI 554
Cdd:PRK00635 810 LSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHdIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVL 882
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
486-570 |
1.90e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 43.92 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 486 LSGGQKQRIALARAFLkHAP-ILVLDEPTAHLDSQTEQLIQNAIAEYAKNH--LVITIAHRLNTVKN-AKQLIVMENGCI 561
Cdd:COG4586 155 LSLGQRMRCELAAALL-HRPkILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMDDIEAlCDRVIVIDHGRI 233
|
....*....
gi 1590405536 562 VQQGDFKAL 570
Cdd:COG4586 234 IYDGSLEEL 242
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
365-520 |
2.05e-04 |
|
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: 42.63 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFHPEVIQ---HISIDQQPLTTANiSQLQQSIAWIPQK----PTLfyd 437
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSvegDIHYNGIPYKEFA-EKYPGEIIYVSEEdvhfPTL--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 438 TLAaniklgnpsashEALEHAAKQAGAlEFInelpdgfntligeqgEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLD 517
Cdd:cd03233 99 TVR------------ETLDFALRCKGN-EFV---------------RGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
...
gi 1590405536 518 SQT 520
Cdd:cd03233 151 SST 153
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
379-554 |
2.39e-04 |
|
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213241 [Multi-domain] Cd Length: 212 Bit Score: 42.67 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 379 AIVGASGSGKSTLLDCML---GFHPEVIQHisidqqplttANISQLQQSIAwipQKPTLFYDTLAAN----IKLGNPSAS 451
Cdd:cd03274 29 AIVGPNGSGKSNVIDSMLfvfGFRASKMRQ----------KKLSDLIHNSA---GHPNLDSCSVEVHfqeiIDKPLLKSK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 452 HEALEHaaKQ----AGALEFINELPDGFNTLIGEqgegLSGGQKQRIALARAFLKH----APILVLDEPTAHLDSQTEQL 523
Cdd:cd03274 96 GIDLDH--NRflilQGEVEQIAQMPKKSWKNISN----LSGGEKTLSSLALVFALHhykpTPLYVMDEIDAALDFRNVSI 169
|
170 180 190
....*....|....*....|....*....|.
gi 1590405536 524 IQNAIAEYAKNHLVITIAHRLNTVKNAKQLI 554
Cdd:cd03274 170 VANYIKERTKNAQFIVISLRNNMFELADRLV 200
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
370-517 |
2.85e-04 |
|
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: 42.74 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 370 LTLPSTGLV-AIVGASGSGKSTLLDCMLGfhpEVIQHISIDQQPLTTANI------SQLQQSIAwipqkpTLFYDTLAAN 442
Cdd:cd03236 20 LPVPREGQVlGLVGPNGIGKSTALKILAG---KLKPNLGKFDDPPDWDEIldefrgSELQNYFT------KLLEGDVKVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 443 IKLGN----PSASHEALEHAAKQAGALEFINELPD--GFNTLIGEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHL 516
Cdd:cd03236 91 VKPQYvdliPKAVKGKVGELLKKKDERGKLDELVDqlELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
.
gi 1590405536 517 D 517
Cdd:cd03236 171 D 171
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
365-531 |
3.68e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.62 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGfhpeviqhisidqqplttaNISQLQQSIAwipqkptlfydtLAANIK 444
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG-------------------ELAPVSGEIG------------LAKGIK 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 445 LGNPS--------ASHEALEHAAKQAGAlEFINELPD-----GFN-TLIGEQGEGLSGGQKQRIALARAFLKHAPILVLD 510
Cdd:PRK10636 377 LGYFAqhqleflrADESPLQHLARLAPQ-ELEQKLRDylggfGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLD 455
|
170 180
....*....|....*....|.
gi 1590405536 511 EPTAHLDSQTEQLIQNAIAEY 531
Cdd:PRK10636 456 EPTNHLDLDMRQALTEALIDF 476
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
486-558 |
3.78e-04 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 42.07 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 486 LSGGQKQRIALARAF----LKHAPILVLDEPTAHLD-SQTEQLIqNAIAEYAKNHLVITIAHRLNTVKNAKQLI--VMEN 558
Cdd:cd03278 114 LSGGEKALTALALLFaifrVRPSPFCVLDEVDAALDdANVERFA-RLLKEFSKETQFIVITHRKGTMEAADRLYgvTMQE 192
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
480-575 |
5.14e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 42.41 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 480 GEQGEGLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYAKN--HLVITIAHRLNTVKNAKQLIVME 557
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDgaTVLLTTQYMEEAEQLAHELTVID 218
|
90
....*....|....*...
gi 1590405536 558 NGCIVQQGDFKALSQQSG 575
Cdd:NF000106 219 RGRVIADGKVDELKTKVG 236
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
61-281 |
6.09e-04 |
|
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: 42.16 E-value: 6.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 61 EGRNLAQVTQYLWPLAGIILLRALFLALseRLSAFATL--KIKSAIRQTLLDKLTQLGPSYIEKNGQGATLNTLHNGVEA 138
Cdd:cd18557 28 KGGDLDVLNELALILLAIYLLQSVFTFV--RYYLFNIAgeRIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 139 LHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMILVGHKAEALNQKRWQQLAVLGNYFFDRVQGL 218
Cdd:cd18557 106 LQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNI 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1590405536 219 TQLKLFNATRKELKQiarisddFRHATLNVLKIAFLSSFALEFLATISVALVAVIIGFRLFFG 281
Cdd:cd18557 186 RTVRSFSAEEKEIRR-------YSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYG 241
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
32-327 |
7.94e-04 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 41.70 E-value: 7.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 32 LSIALGTVNAILMIAGAYLLAQTIHEVMfegRNLAQVTQYLWPLAGIILLRALFLALSERLSAFAT----LKIKSAIRQT 107
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLS---SYPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSfrlgMRVRSALSSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 108 LLDKLTQLGPSYIEKNGQGATLNTLHNGVEALHDyyakYLPGVAYSALIPLAILVVIFPTDYKAG-------LIFLLTAP 180
Cdd:cd18579 78 IYRKALRLSSSARQETSTGEIVNLMSVDVQRIED----FFLFLHYLWSAPLQIIVALYLLYRLLGwaalaglGVLLLLIP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 181 LIPFFMILVGHkaealNQKRWQQLA---------VLGN-----------YFFDRVQGLtqlklfnatR-KELKQIARISd 239
Cdd:cd18579 154 LQAFLAKLISK-----LRKKLMKATdervkltneILSGikviklyawekPFLKRIEEL---------RkKELKALRKFG- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 240 dfrhatlnvLKIAFLSSFaleFLATISVALVAVIIGFRLFFGTLDFATGFVVLLLapeFYL---PLRQLGshyharlQGI 316
Cdd:cd18579 219 ---------YLRALNSFL---FFSTPVLVSLATFATYVLLGNPLTAAKVFTALSL---FNLlrfPLLMLP-------QAI 276
|
330
....*....|.
gi 1590405536 317 SAAADMLIILN 327
Cdd:cd18579 277 SSLIEALVSLK 287
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
365-517 |
8.70e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.08 E-value: 8.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 365 INNINLTLPSTGLVAIVGASGSGKSTLLDCMLGfhpeviqHISIDQQPLTTANISQLqqsiAWIPQ------KPTLFY-- 436
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKN-------EISADGGSYTFPGNWQL----AWVNQetpalpQPALEYvi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 437 -----------DTLAANIKL-GNPSAS-H---EALEHAAKQAGALEFINELpdGF-NTLIGEQGEGLSGGQKQRIALARA 499
Cdd:PRK10636 86 dgdreyrqleaQLHDANERNdGHAIATiHgklDAIDAWTIRSRAASLLHGL--GFsNEQLERPVSDFSGGWRMRLNLAQA 163
|
170
....*....|....*...
gi 1590405536 500 FLKHAPILVLDEPTAHLD 517
Cdd:PRK10636 164 LICRSDLLLLDEPTNHLD 181
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
32-285 |
1.35e-03 |
|
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: 40.84 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 32 LSIALGTVNAILMIAGAYLLAQTIhEVMFEGRNLAQVTQYLWPLAGIILLRALFLALSERLSAFATLKIKSAIRQTLLDK 111
Cdd:cd18548 3 LAPLFKLLEVLLELLLPTLMADII-DEGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 112 LTQLGPSYIEKNGQGATLNTLHNGVEALHDYYAKYLPGVAYSALIPLAILVVIFPTDYKAGLIFLLTAPLIPFFMILVGH 191
Cdd:cd18548 82 IQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 192 KAEALNQKRWQQLAVLGNYFFDRVQGLTQLKLFNATRKELKQIARISDDFRHATLNVLKIAFLSSFALEFLATISVALVA 271
Cdd:cd18548 162 KAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAIL 241
|
250
....*....|....
gi 1590405536 272 VIIGFRLFFGTLDF 285
Cdd:cd18548 242 WFGGHLINAGSLQV 255
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
367-391 |
2.02e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.21 E-value: 2.02e-03
|
| DotB_TraJ |
cd19516 |
dot/icm secretion system protein DotB-like; Defect in organelle trafficking (Dot)B is part of ... |
372-398 |
2.87e-03 |
|
dot/icm secretion system protein DotB-like; Defect in organelle trafficking (Dot)B is part of the type IVb secretion (T4bS) system, also known as the dot/icm system, and is the main energy supplier of the secretion system. It is an ATPase, similar to the VirB11 component of the T4aS systems. This family also includes Escherichia coli IncI plasmid-encoded conjugative transfer ATPase TraJ encoded on the tra (transfer) operon.
Pssm-ID: 410924 [Multi-domain] Cd Length: 179 Bit Score: 38.90 E-value: 2.87e-03
10 20
....*....|....*....|....*..
gi 1590405536 372 LPSTGLVAIVGASGSGKSTLLDCMLGF 398
Cdd:cd19516 8 FPREGLVYVAGATGSGKSTLLAAIYRY 34
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
474-559 |
3.26e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.10 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 474 GFNTLIGEqgegLSGGQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYA-KNHLVITIAHRLNTVKN-AK 551
Cdd:PRK10982 384 GHRTQIGS----LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSEMPELLGiTD 459
|
....*...
gi 1590405536 552 QLIVMENG 559
Cdd:PRK10982 460 RILVMSNG 467
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
348-517 |
5.02e-03 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 38.86 E-value: 5.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 348 TISIHDLNFSYpNSNEGINNINLTLPSTGLVAIVGASGSGKSTLLDCMLGFhpevIQ----HISIDQQPLTTANISQ-LQ 422
Cdd:COG1137 3 TLEAENLVKSY-GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGL----VKpdsgRIFLDGEDITHLPMHKrAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1590405536 423 QSIAWIPQKPTLFYD-TLAANIKLgnpsasheALEHAAK-QAGALEFINELPDGFNtlIGE----QGEGLSGGQKQRIAL 496
Cdd:COG1137 78 LGIGYLPQEASIFRKlTVEDNILA--------VLELRKLsKKEREERLEELLEEFG--ITHlrksKAYSLSGGERRRVEI 147
|
170 180
....*....|....*....|...
gi 1590405536 497 ARAfLKHAP--ILvLDEPTAHLD 517
Cdd:COG1137 148 ARA-LATNPkfIL-LDEPFAGVD 168
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
365-395 |
5.69e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 38.25 E-value: 5.69e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1590405536 365 INNI----NLTL-PSTGLVAIVGASGSGKSTLLDCM 395
Cdd:pfam13476 3 IENFrsfrDQTIdFSKGLTLITGPNGSGKTTILDAI 38
|
|
| PilT |
COG2805 |
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular ... |
369-406 |
6.02e-03 |
|
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular structures];
Pssm-ID: 442056 Cd Length: 342 Bit Score: 39.30 E-value: 6.02e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1590405536 369 NLTLPSTGLVAIVGASGSGKSTLLDCMlgfhpevIQHI 406
Cdd:COG2805 119 ELAELPRGLVLVTGPTGSGKSTTLAAM-------IDYI 149
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
489-547 |
6.47e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.49 E-value: 6.47e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1590405536 489 GQKQRIALARAFLKHAPILVLDEPTAHLDSQTEQLIQNAIAEYakNHLVITIAH-R--LNTV 547
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNER--NSTMIIISHdRhfLNSV 218
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
367-392 |
6.86e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.67 E-value: 6.86e-03
10 20
....*....|....*....|....*.
gi 1590405536 367 NINLTLPSTGLVAIVGASGSGKSTLL 392
Cdd:PRK00349 627 NVDVEIPLGKFTCVTGVSGSGKSTLI 652
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
367-391 |
7.46e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.24 E-value: 7.46e-03
10 20
....*....|....*....|....*
gi 1590405536 367 NINLTLPSTGLVAIVGASGSGKSTL 391
Cdd:COG0178 623 NVDVEIPLGVLTCVTGVSGSGKSTL 647
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
367-391 |
8.44e-03 |
|
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: 39.23 E-value: 8.44e-03
|
| |
