|
Name |
Accession |
Description |
Interval |
E-value |
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1-544 |
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: 663.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1 MKPIDPRLLRYARATRFFLAAVVALGVVGAALVIAQAMLVADVVVGGFEDGLTVSGLRTPLILLAAVALGRALVSWLTEL 80
Cdd:COG4988 1 QKPLDKRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPLSALLPLLGLLLAVLLLRALLAWLRER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 81 AAYRASAAVKSELRGRLLDRAAELGPGLLSDRRTGSLVTLATRGVDALDDYFARYLPQLGLAVVVPVAVLARIVTEDWVS 160
Cdd:COG4988 81 AAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 161 AAIIVVTLPLIPLFMILIGWATQSRMDRQWRLLSRLSGHFLDVVAGLPTLKVFGRAKAQAESIRAITSQYRRATLRTLRI 240
Cdd:COG4988 161 GLILLVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKVLRV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 241 AFLSSFALELLATLSVALVAVTIGMRLVHGELDLYTGLVVLILAPEAYLPIRQVGAQYHAAAEGLSAAEEIFSVLETEPR 320
Cdd:COG4988 241 AFLSSAVLEFFASLSIALVAVYIGFRLLGGSLTLFAALFVLLLAPEFFLPLRDLGSFYHARANGIAAAEKIFALLDAPEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 321 RGGTADVP----ESLRLELEGVTVRHEGrGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGV 396
Cdd:COG4988 321 AAPAGTAPlpaaGPPSIELEDVSFSYPG-GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 397 DLATLAPERWRERIAWVPQRPYLFAGTIAENVRLARPDADDGAVAAALRDAGAYDFVAELPDGAQTLLGEDGAGLSAGQR 476
Cdd:COG4988 400 DLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQA 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2351811981 477 QRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQGRTVLLVVHRPALLPLADRVVRLEPG 544
Cdd:COG4988 480 QRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDG 547
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
618-1156 |
0e+00 |
|
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: 607.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 618 VGLMAVSGWLISRASEQPPVLYLMVAVTATRAFGLGRAVFRYAERLVSHDAVLKMLAELRVAVYRGLERIAPAGLRRSRR 697
Cdd:COG4987 32 IGLLALSGWLIAAAALAPPILNLFVPIVGVRAFAIGRTVFRYLERLVSHDATLRLLADLRVRLYRRLEPLAPAGLARLRS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 698 GDLLSRLVADVDALQDYWLRWLLPAGTAVVVGAATAGFIGWLLPAAGIVLATGLLLAGAGVPLVSGACSRHAERQLAPAR 777
Cdd:COG4987 112 GDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALALVLALGLLLAGLLLPLLAARLGRRAGRRLAAAR 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 778 ADLATRITDLLGGTAELTVAGALPARKARTREADGVLTRIAARAATATALGGGLIALIGGLTVVATALVALPAVHDGRLA 857
Cdd:COG4987 192 AALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALS 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 858 GVELAVVVLTPLAAFEAVTGLPLAVQYRQRVKRSAERVYEVLDAPPPVREPDSPAGTPASPfPLEVRGLSARYAGAERDA 937
Cdd:COG4987 272 GPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDAPPAVTEPAEPAPAPGGP-SLELEDVSFRYPGAGRPV 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 938 LDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGLCAQDAHIFDSSIRENLR 1017
Cdd:COG4987 351 LDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLR 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1018 LARTGATDEELRAALDRARLLDWAEALPAGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADAL 1097
Cdd:COG4987 431 LARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQAL 510
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 1098 TADLLAATRGRTTVLITHRLQGLEAVDEVVVLEAGRVVQRGPYADLTAEEGPLRRMLER 1156
Cdd:COG4987 511 LADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQR 569
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
15-541 |
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: 601.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 15 TRFFLAAVVALGVVGAALVIAQAMLVADVVVGGFEDGLTVSGLRTPLILLAAVALGRALVSWLTELAAYRASAAVKSELR 94
Cdd:TIGR02857 1 ARRALALLALLGVLGALLIIAQAWLLARVVDGLISAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 95 GRLLDRAAELGPGLLSDRRTGSLVTLATRGVDALDDYFARYLPQLGLAVVVPVAVLARIVTEDWVSAAIIVVTLPLIPLF 174
Cdd:TIGR02857 81 ERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIPIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 175 MILIGWATQSRMDRQWRLLSRLSGHFLDVVAGLPTLKVFGRAKAQAESIRAITSQYRRATLRTLRIAFLSSFALELLATL 254
Cdd:TIGR02857 161 MILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLELFATL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 255 SVALVAVTIGMRLVHGELDLYTGLVVLILAPEAYLPIRQVGAQYHAAAEGLSAAEEIFSVLETEPR-RGGTADVPE--SL 331
Cdd:TIGR02857 241 SVALVAVYIGFRLLAGDLDLATGLFVLLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAAPRpLAGKAPVTAapAS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 332 RLELEGVTVRHEGRgEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERIA 411
Cdd:TIGR02857 321 SLEFSGVSVAYPGR-RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 412 WVPQRPYLFAGTIAENVRLARPDADDGAVAAALRDAGAYDFVAELPDGAQTLLGEDGAGLSAGQRQRLALARAFLADRPL 491
Cdd:TIGR02857 400 WVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPL 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2351811981 492 LLLDEPTASLDGETEAGIVEAVRRLAQGRTVLLVVHRPALLPLADRVVRL 541
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
589-1117 |
1.02e-170 |
|
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: 514.22 E-value: 1.02e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 589 LARVREAAGAQRGQLALALLLGSLALGSAVGLMAVSGWLISRASEQPPVLYLMVAVTATRAFGLGRAVFRYAERLVSHDA 668
Cdd:TIGR02868 1 LLRILPLLKPRRRRLALAVLLGALALGSAVALLGVSAWLISRAAEMPPVLYLSVAAVAVRAFGIGRAVFRYLERLVGHDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 669 VLKMLAELRVAVYRGLERIAPAGLRRSRRGDLLSRLVADVDALQDYWLRWLLPAGTAVVVGAATAGFIGWLLPAAGIVLA 748
Cdd:TIGR02868 81 ALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 749 TGLLLAGAGVPLVSGACSRHAERQLAPARADLATRITDLLGGTAELTVAGALPARKARTREADGVLTRIAARAATATALG 828
Cdd:TIGR02868 161 AGLLLAGFVAPLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 829 GGLIALIGGLTVVATALVALPAVHDGRLAGVELAVVVLTPLAAFEAVTGLPLAVQYRQRVKRSAERVYEVLDAPPPVREP 908
Cdd:TIGR02868 241 AALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAGPVAEG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 909 DSPAGTPASP--FPLEVRGLSARYAGAERdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDA 986
Cdd:TIGR02868 321 SAPAAGAVGLgkPTLELRDLSAGYPGAPP-VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 987 CVLEGDTVRGFVGLCAQDAHIFDSSIRENLRLARTGATDEELRAALDRARLLDWAEALPAGLDTLVGEHGARLSGGQRQR 1066
Cdd:TIGR02868 400 SSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQR 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 1067 LALARAILADFPVLVLDEPAEHLDLATADALTADLLAATRGRTTVLITHRL 1117
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-544 |
1.44e-136 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 427.34 E-value: 1.44e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 16 RFFLAAVVALGVVGAALVIAQAMLVADVVVGGFEDGLTVSGLRTPLILLAAVALGRALVSWLTELAAYRASAAVKSELRG 95
Cdd:PRK11174 21 KRWLNLSILLGFLSGLLLIAQAWLLATILQALIIENIPREALLPPFILLILLFVLRALLAWLRERVGFKAGQHIRQQIRQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 96 RLLDRAAELGPGLLSDRRTGSLVTLATRGVDALDDYFARYLPQLGLAVVVPVAVLARIVTEDWVSAAIIVVTLPLIPLFM 175
Cdd:PRK11174 101 QVLDKLQQLGPAWIQGKPAGSWATLVLEQVEDMHDFYARYLPQMALAVLVPLLILIAVFPINWAAGLILLGTAPLIPLFM 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 176 ILIGWATQSRMDRQWRLLSRLSGHFLDVVAGLPTLKVFGRAKAQAESIRAITSQYRRATLRTLRIAFLSSFALELLATLS 255
Cdd:PRK11174 181 ALVGMGAADANRRNFLALARLSGHFLDRLRGLETLRLFNRGEAETESIRSASEDFRQRTMEVLRMAFLSSAVLEFFASIS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 256 VALVAVTIGMRLVhGELD---------LYTGLVVLILAPEAYLPIRQVGAQYHAAAEGLSAAEEIFSVLETE--PRRGGT 324
Cdd:PRK11174 261 IALVAVYFGFSYL-GELNfghygtgvtLFAGFFVLILAPEFYQPLRDLGTFYHAKAQAVGAAESLVTFLETPlaHPQQGE 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 325 ADVPESLRLELEG---VTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFtAPDEGRVRVGGVDLATL 401
Cdd:PRK11174 340 KELASNDPVTIEAedlEILSPDGK--TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELREL 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 402 APERWRERIAWVPQRPYLFAGTIAENVRLARPDADDGAVAAALRDAGAYDFVAELPDGAQTLLGEDGAGLSAGQRQRLAL 481
Cdd:PRK11174 417 DPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLAL 496
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2351811981 482 ARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQGRTVLLVVHRPALLPLADRVVRLEPG 544
Cdd:PRK11174 497 ARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDG 559
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
7-544 |
1.13e-124 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 395.30 E-value: 1.13e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 7 RLLRYARATRFFLAAVVALGVVGAALVIAQAMLVADVVVGGFEDGlTVSGLRTPLILLAAVALGRALVSWLTELAAYRAS 86
Cdd:COG1132 11 RLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGG-DLSALLLLLLLLLGLALLRALLSYLQRYLLARLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 87 AAVKSELRGRLLDRAAELGPGLLSDRRTGSLVTLATRGVDALDDYFARYLPQLGLAVVVPVAVLARIVTEDWVSAAIIVV 166
Cdd:COG1132 90 QRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 167 TLPLIPLFMILIGWATQSRMDRQWRLLSRLSGHFLDVVAGLPTLKVFGRAKAQAESIRAITSQYRRATLRTLRIAFLSSF 246
Cdd:COG1132 170 VLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 247 ALELLATLSVALVAVTIGMRLVHGELDLYTGLVVLILAPEAYLPIRQVGAQYHAAAEGLSAAEEIFSVLETEP----RRG 322
Cdd:COG1132 250 LMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPeipdPPG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 323 GTADVPESLRLELEGVTVRHEGrGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLA 402
Cdd:COG1132 330 AVPLPPVRGEIEFENVSFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 403 PERWRERIAWVPQRPYLFAGTIAENVRLARPDADDGAVAAALRDAGAYDFVAELPDGAQTLLGEDGAGLSAGQRQRLALA 482
Cdd:COG1132 409 LESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIA 488
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2351811981 483 RAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQGRTVLLVVHRPALLPLADRVVRLEPG 544
Cdd:COG1132 489 RALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDG 550
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
22-311 |
8.19e-114 |
|
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: 355.56 E-value: 8.19e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 22 VVALGVVGAALVIAQAMLVADVVVGGFEDGLTVSGLRTPLILLAAVALGRALVSWLTELAAYRASAAVKSELRGRLLDRA 101
Cdd:cd18584 1 AVLLGLLAALLIIAQAWLLARIIAGVFLEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 102 AELGPGLLSDRRTGSLVTLATRGVDALDDYFARYLPQLGLAVVVPVAVLARIVTEDWVSAAIIVVTLPLIPLFMILIGWA 181
Cdd:cd18584 81 LALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSALILLVTAPLIPLFMILIGKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 182 TQSRMDRQWRLLSRLSGHFLDVVAGLPTLKVFGRAKAQAESIRAITSQYRRATLRTLRIAFLSSFALELLATLSVALVAV 261
Cdd:cd18584 161 AQAASRRQWAALSRLSGHFLDRLRGLPTLKLFGRARAQAARIARASEDYRRRTMKVLRVAFLSSAVLEFFATLSIALVAV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2351811981 262 TIGMRLVHGELDLYTGLVVLILAPEAYLPIRQVGAQYHAAAEGLSAAEEI 311
Cdd:cd18584 241 YIGFRLLGGSLTLFTALFVLLLAPEFYLPLRQLGAAYHARADGLAAAERL 290
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
582-1161 |
5.39e-103 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 337.14 E-value: 5.39e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 582 AARPGQVLARVREAAGAQRGQLALALLLGSLALGSAVGLMAVSGWLISRASEQPPVLYLMVAVTATRAFGLGRAVFRYAE 661
Cdd:COG1132 2 SKSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 662 RLVSHDAVLKMLAELRVAVYRGLERIAPAGLRRSRRGDLLSRLVADVDALQDYWLRWLLPAGTAVVVGAATAGFIGWLLP 741
Cdd:COG1132 82 RYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 742 AAGIVLATGLLLAGAGVPLVSGAcSRHAERQLAPARADLATRITDLLGGTAELTVAGALPARKARTREADGVLTRIAARA 821
Cdd:COG1132 162 RLALIVLLVLPLLLLVLRLFGRR-LRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 822 ATATALGGGLIALIGGLTVVATALVALPAVHDGRLAGVELAVVVLTPLAAFEAVTGLPLAVQYRQRVKRSAERVYEVLDA 901
Cdd:COG1132 241 ARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 902 PPPVREPDSPAGTPASPFPLEVRGLSARYAGaERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRI 981
Cdd:COG1132 321 PPEIPDPPGAVPLPPVRGEIEFENVSFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 982 GGVDACVLEGDTVRGFVGLCAQDAHIFDSSIRENLRLARTGATDEELRAALDRARLLDWAEALPAGLDTLVGEHGARLSG 1061
Cdd:COG1132 400 DGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1062 GQRQRLALARAILADFPVLVLDEPAEHLDLATADALTADLLAATRGRTTVLITHRLQGLEAVDEVVVLEAGRVVQRGPYA 1141
Cdd:COG1132 480 GQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHE 559
|
570 580
....*....|....*....|
gi 2351811981 1142 DLTAEEGPLRRMLERERETE 1161
Cdd:COG1132 560 ELLARGGLYARLYRLQFGEE 579
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
618-1156 |
4.49e-96 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 318.31 E-value: 4.49e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 618 VGLMAVSGWLISRASeqppVLYLMVAVT--------ATRAFGLGRAVFRYAERLVSHDAVLKMLAELRVAVYRGLERIAP 689
Cdd:PRK11160 33 IGLLTLSGWFLSASA----VAGLAGLYSfnymlpaaGVRGAAIGRTAGRYGERLVSHDATFRVLTHLRVFTFSKLLPLSP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 690 AGLRRSRRGDLLSRLVADVDALQDYWLRWLLPAGTAVVVGAATAGFIGWLLPAAGIVLATGLLLAGAGVPLVSGACSRHA 769
Cdd:PRK11160 109 AGLARYRQGDLLNRLVADVDTLDHLYLRLISPLVAALVVILVLTIGLSFFDLTLALTLGGILLLLLLLLPLLFYRLGKKP 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 770 ERQLAPARADLATRITDLLGGTAELTVAGALPARKARTREADGVLTRIAARAATATALGGGLIALIGGLTVVATALVALP 849
Cdd:PRK11160 189 GQDLTHLRAQYRVQLTEWLQGQAELTLFGAEDRYRQQLEQTEQQWLAAQRRQANLTGLSQALMILANGLTVVLMLWLAAG 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 850 AVHDGRLAGVELAVVVLTPLAAFEAVTGLPLAVQYRQRVKRSAERVYEVLDAPPPVREPDSpAGTPASPFPLEVRGLSAR 929
Cdd:PRK11160 269 GVGGNAQPGALIALFVFAALAAFEALMPVAGAFQHLGQVIASARRINEITEQKPEVTFPTT-STAAADQVSLTLNNVSFT 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 930 YAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGLCAQDAHIFD 1009
Cdd:PRK11160 348 YPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFS 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1010 SSIRENLRLARTGATDEELRAALDRARLLDWAEAlPAGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHL 1089
Cdd:PRK11160 428 ATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGL 506
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2351811981 1090 DLATADALTADLLAATRGRTTVLITHRLQGLEAVDEVVVLEAGRVVQRGPYADLTAEEGPLRRMLER 1156
Cdd:PRK11160 507 DAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQR 573
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
7-544 |
2.80e-94 |
|
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: 313.24 E-value: 2.80e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 7 RLLRYARATRFFLAAVVALGVVGAALVIAqamLVAdvVVGGFedgLTVSGLRTPL--ILLAAV-----ALGRALVSWLTE 79
Cdd:COG4987 5 RLLRLLRPHRGRLLLGVLLGLLTLLAGIG---LLA--LSGWL---IAAAALAPPIlnLFVPIVgvrafAIGRTVFRYLER 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 80 LAAYRASAAVKSELRGRLLDRAAELGPGLLSDRRTGSLVTLATRGVDALDDYFARYLPQLGLAVVVPVAVLARIVTEDWV 159
Cdd:COG4987 77 LVSHDATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 160 SAAIIVVTLPLIPLFMILIGWATQSRMDRQW-RLLSRLSGHFLDVVAGLPTLKVFGRAKAQAESIRAITSQYRRATLRTL 238
Cdd:COG4987 157 LALVLALGLLLAGLLLPLLAARLGRRAGRRLaAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 239 RIAFLSSFALELLATLSVALVAVTIGMRLVHGELDLyTGLVVLILAP----EAYLPIRQVGAQYHAAaegLSAAEEIFSV 314
Cdd:COG4987 237 RLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSG-PLLALLVLAAlalfEALAPLPAAAQHLGRV---RAAARRLNEL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 315 LETEPRR---GGTADVPESLRLELEGVTVRHEGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRV 391
Cdd:COG4987 313 LDAPPAVtepAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 392 RVGGVDLATLAPERWRERIAWVPQRPYLFAGTIAENVRLARPDADDGAVAAALRDAGAYDFVAELPDGAQTLLGEDGAGL 471
Cdd:COG4987 393 TLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRL 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2351811981 472 SAGQRQRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQGRTVLLVVHRPALLPLADRVVRLEPG 544
Cdd:COG4987 473 SGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDG 545
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
622-1148 |
4.74e-92 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 307.07 E-value: 4.74e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 622 AVSGWLISRASEQPPVLYLMVAVtatrAFGLGRAVFRYAERLVSHDAVLKMLAELRVAVYRGLERIAPAGLRRSRRGDLL 701
Cdd:COG4988 43 LLAGLIIGGAPLSALLPLLGLLL----AVLLLRALLAWLRERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 702 SRLVADVDALQDYWLRWLLPAGTAVVVGAATAGFIGWLLPAAGIVLATGLLLAGAGVPLVSGACSRHAERQLApARADLA 781
Cdd:COG4988 119 TLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLILLVTAPLIPLFMILVGKGAAKASRRQWR-ALARLS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 782 TRITDLLGGTAELTVAGALPARKARTREAD------------------GVLTRIaaraatatalggglialigglTVVAT 843
Cdd:COG4988 198 GHFLDRLRGLTTLKLFGRAKAEAERIAEASedfrkrtmkvlrvaflssAVLEFF---------------------ASLSI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 844 ALVALPAVH---DGRLA-GVELAVVVLTPLAaFeavtgLPL---AVQY--RQRVKRSAERVYEVLDAPPPVREPDSPAGT 914
Cdd:COG4988 257 ALVAVYIGFrllGGSLTlFAALFVLLLAPEF-F-----LPLrdlGSFYhaRANGIAAAEKIFALLDAPEPAAPAGTAPLP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 915 PASPFPLEVRGLSARYAGaERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTV 994
Cdd:COG4988 331 AAGPPSIELEDVSFSYPG-GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 995 RGFVGLCAQDAHIFDSSIRENLRLARTGATDEELRAALDRARLLDWAEALPAGLDTLVGEHGARLSGGQRQRLALARAIL 1074
Cdd:COG4988 410 RRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALL 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 1075 ADFPVLVLDEPAEHLDLATADALTADLLAATRGRTTVLITHRLQGLEAVDEVVVLEAGRVVQRGPYADLTAEEG 1148
Cdd:COG4988 490 RDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
7-544 |
6.61e-89 |
|
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: 302.52 E-value: 6.61e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 7 RLLRYARATRFFLAAVVALGVVGAALVIAQA---MLVAD-VVVGGFEDGLTV--SGLrtpLILLAAVALGRALVSWLTEL 80
Cdd:COG2274 146 WFLRLLRRYRRLLLQVLLASLLINLLALATPlftQVVIDrVLPNQDLSTLWVlaIGL---LLALLFEGLLRLLRSYLLLR 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 81 AAYRASAAVKSELRGRLLDraaeLGPGLLSDRRTGSLV-----------TLATRGVDALDDyfaryLPQLGLAVVVpvav 149
Cdd:COG2274 223 LGQRIDLRLSSRFFRHLLR----LPLSFFESRSVGDLAsrfrdvesireFLTGSLLTALLD-----LLFVLIFLIV---- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 150 larIVTEDWVSAAIIVVTLPLIPLFMILIGWATQSRMDRQWRLLSRLSGHFLDVVAGLPTLKVFGRAKAQAESIRAITSQ 229
Cdd:COG2274 290 ---LFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAK 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 230 YRRATLRTLRIAFLSSFALELLATLSVALVAVTIGMRLVHGELDL-----YTGLVVLILAPeaylpIRQVGAQYHAAAEG 304
Cdd:COG2274 367 YLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLgqliaFNILSGRFLAP-----VAQLIGLLQRFQDA 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 305 LSAAEEIFSVL--ETEPRRGGTADVPESLR--LELEGVTVRHEGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVV 380
Cdd:COG2274 442 KIALERLDDILdlPPEREEGRSKLSLPRLKgdIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLL 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 381 LGFTAPDEGRVRVGGVDLATLAPERWRERIAWVPQRPYLFAGTIAENVRLARPDADDGAVAAALRDAGAYDFVAELPDGA 460
Cdd:COG2274 522 LGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGY 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 461 QTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQGRTVLLVVHRPALLPLADRVVR 540
Cdd:COG2274 602 DTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIV 681
|
....
gi 2351811981 541 LEPG 544
Cdd:COG2274 682 LDKG 685
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
649-1157 |
3.62e-79 |
|
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: 275.56 E-value: 3.62e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 649 AFGLGRAVFRYAERLVSHDAVLKMLAELRVAVYRGLERIaPAGLRRSRR-GDLLSRlVADVDALQDYWLRWLLPAGTA-- 725
Cdd:COG2274 204 LALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRL-PLSFFESRSvGDLASR-FRDVESIREFLTGSLLTALLDll 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 726 -VVVGAATAGFIGWLLpaAGIVLATGLLLAGAGvpLVSGACSRHAERQLAPARADLATRITDLLGGTAELTVAGALPARK 804
Cdd:COG2274 282 fVLIFLIVLFFYSPPL--ALVVLLLIPLYVLLG--LLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFR 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 805 ARTREADGVLTRIAARAATATALGGGLIALIGGLTVVATALVALPAVHDGRL-AGVELAVVVLTpLAAFEAVTGLPLAVQ 883
Cdd:COG2274 358 RRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLtLGQLIAFNILS-GRFLAPVAQLIGLLQ 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 884 YRQRVKRSAERVYEVLDAPPPVREPDSPAGTPASPFPLEVRGLSARYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTT 963
Cdd:COG2274 437 RFQDAKIALERLDDILDLPPEREEGRSKLSLPRLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKST 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 964 LAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGLCAQDAHIFDSSIRENLRLARTGATDEELRAALDRARLLDWAEA 1043
Cdd:COG2274 517 LLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEA 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1044 LPAGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTADLLAATRGRTTVLITHRLQGLEAV 1123
Cdd:COG2274 597 LPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLA 676
|
490 500 510
....*....|....*....|....*....|....
gi 2351811981 1124 DEVVVLEAGRVVQRGPYADLTAEEGPLRRMLERE 1157
Cdd:COG2274 677 DRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQ 710
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
618-1129 |
1.52e-67 |
|
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: 237.18 E-value: 1.52e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 618 VGLMAVSGWLISRA-----SEQPPVLYLMVAVTATRAFGLGRAVFRYAERLVSHDAVLKMLAELRVAVYRGLERIAPAGL 692
Cdd:TIGR02857 16 ALLIIAQAWLLARVvdgliSAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRERLLEAVAALGPRWL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 693 RRSRRGDLLSRLVADVDALQDYWLRWLLPAGTAVVVGAATAGFIGWLLPAAGIVLATGLLLAGAGVPLVSGACSRHAERQ 772
Cdd:TIGR02857 96 QGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIPIFMILIGWAAQAAARKQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 773 LApARADLATRITDLLGGTAELTVAGAlparkaRTREADGVLTRIAARAATATALGGGLIALIGGLTVVATALVALPAVH 852
Cdd:TIGR02857 176 WA-ALSRLSGHFLDRLRGLPTLKLFGR------AKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLELFATLSVALVAVY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 853 DG-RLAG--VELAVVVLTPLAAFEAVtgLPL---AVQY--RQRVKRSAERVYEVLDAPPPVREPDSPAGTPASPfPLEVR 924
Cdd:TIGR02857 249 IGfRLLAgdLDLATGLFVLLLAPEFY--LPLrqlGAQYhaRADGVAAAEALFAVLDAAPRPLAGKAPVTAAPAS-SLEFS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 925 GLSARYAGAeRDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGLCAQD 1004
Cdd:TIGR02857 326 GVSVAYPGR-RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQH 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1005 AHIFDSSIRENLRLARTGATDEELRAALDRARLLDWAEALPAGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDE 1084
Cdd:TIGR02857 405 PFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDE 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2351811981 1085 PAEHLDLATADALTADLLAATRGRTTVLITHRLQGLEAVDEVVVL 1129
Cdd:TIGR02857 485 PTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
333-544 |
2.49e-67 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 223.80 E-value: 2.49e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERIAW 412
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 413 VPQRPYLFAGTIAENVrlarpdaddgavaaalrdagaydfvaelpdgaqtllgedgagLSAGQRQRLALARAFLADRPLL 492
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2351811981 493 LLDEPTASLDGETEAGIVEAVRRLAQGRTVLLVVHRPALLPLADRVVRLEPG 544
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
7-544 |
4.03e-66 |
|
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: 234.23 E-value: 4.03e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 7 RLLRYARATRF-FLAAVVALGVVGAALVIAqAMLVADVVVGGFEDGLTVSGLRTPLILLAAVALgRALVSWLTELAAYRA 85
Cdd:TIGR02203 4 RLWSYVRPYKAgLVLAGVAMILVAATESTL-AALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVL-RGICSFVSTYLLSWV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 86 SAAVKSELRGRLLDRAAELgPGLLSDRR-TGSLVTLATRGVDALDDYFARYLPQLGLAVVVPVAVLARIVTEDWVSAAII 164
Cdd:TIGR02203 82 SNKVVRDIRVRMFEKLLGL-PVSFFDRQpTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 165 VVTLPLIPLFMiligwatqSRMDRQWRLLSR----LSGHFLDVVA----GLPTLKVFGRAKAQAESIRAITSQYRRATLR 236
Cdd:TIGR02203 161 VVMLPVLSILM--------RRVSKRLRRISKeiqnSMGQVTTVAEetlqGYRVVKLFGGQAYETRRFDAVSNRNRRLAMK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 237 TLRIAFLSSFALELLATLSVALVAVTIGMRLVHGELDLYTGLVVLILAPEAYLPIRQVGAQYHAAAEGLSAAEEIFSVLE 316
Cdd:TIGR02203 233 MTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 317 TEPRRGGTADVPESLR--LELEGVTVRHEGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVG 394
Cdd:TIGR02203 313 SPPEKDTGTRAIERARgdVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 395 GVDLATLAPERWRERIAWVPQRPYLFAGTIAENVRLARPDADDGAV-AAALRDAGAYDFVAELPDGAQTLLGEDGAGLSA 473
Cdd:TIGR02203 393 GHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQADRAEiERALAAAYAQDFVDKLPLGLDTPIGENGVLLSG 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 474 GQRQRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQGRTVLLVVHRPALLPLADRVVRLEPG 544
Cdd:TIGR02203 473 GQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDG 543
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
618-895 |
2.89e-64 |
|
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: 219.66 E-value: 2.89e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 618 VGLMAVSGWLISRASEQPPVLY---LMVAVTATRAFGLGRAVFRYAERLVSHDAVLKMLAELRVAVYRGLERIAPAGLRR 694
Cdd:cd18585 9 IGLLALSGWFISAAALAGLAAPtfnYFTPAAGVRGFAITRTAGRYGERLVSHDATFRLLSNLRVWFYRKLEPLAPARLQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 695 SRRGDLLSRLVADVDALQDYWLRWLLPAGTAVVVGAATAGFIGWLLPAAGIVLATGLLLAGAGVPLVSGACSRHAERQLA 774
Cdd:cd18585 89 YRSGDLLNRIVADIDTLDNLYLRVLSPPVVALLVILATILFLAFFSPALALILLAGLLLAGVVIPLLFYRLGKKIGQQLV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 775 PARADLATRITDLLGGTAELTVAGALPARKARTREADGVLTRIAARAATATALGGGLIALIGGLTVVATALVALPAVHDG 854
Cdd:cd18585 169 QLRAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGLSQALMILLSGLTVWLVLWLGAPLVQNG 248
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2351811981 855 RLAGVELAVVVLTPLAAFEAVTGLPLAVQYRQRVKRSAERV 895
Cdd:cd18585 249 ALDGALLAMLVFAVLASFEAVAPLPLAFQYLGETRAAARRL 289
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
7-529 |
5.13e-64 |
|
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: 227.24 E-value: 5.13e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 7 RLLRYARATRFFLAAVVALGVVGAALVIAQAMLVADVVVGGFEDGlTVSGLRTPLILLAAVALGRALVSWLTELAAYRAS 86
Cdd:TIGR02868 3 RILPLLKPRRRRLALAVLLGALALGSAVALLGVSAWLISRAAEMP-PVLYLSVAAVAVRAFGIGRAVFRYLERLVGHDAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 87 AAVKSELRGRLLDRAAELGPGLLSDRRTGSLVTLATRGVDALDDYFARYLPQLGLAVVVPVAVLARIVTEDWVSAAIIVV 166
Cdd:TIGR02868 82 LRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 167 TLPLIPLFMILI-GWATQSRMDRQWRLLSRLSGHFLDVVAGLPTLKVFGRAKAQAESIRAITSQYRRATLRTLRIAFLSS 245
Cdd:TIGR02868 162 GLLLAGFVAPLVsLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALGA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 246 FALELLATLSVALVAVTIGMRLVHGELDLYTgLVVLILAP----EAYLPIRQVGAQYHAAAEglsAAEEIFSVLETEPRR 321
Cdd:TIGR02868 242 ALTLLAAGLAVLGALWAGGPAVADGRLAPVT-LAVLVLLPlaafEAFAALPAAAQQLTRVRA---AAERIVEVLDAAGPV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 322 GGTAD------VPESLRLELEGVTVRHEGrGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGG 395
Cdd:TIGR02868 318 AEGSApaagavGLGKPTLELRDLSAGYPG-APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 396 VDLATLAPERWRERIAWVPQRPYLFAGTIAENVRLARPDADDGAVAAALRDAGAYDFVAELPDGAQTLLGEDGAGLSAGQ 475
Cdd:TIGR02868 397 VPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGE 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 476 RQRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQGRTVLLVVHRP 529
Cdd:TIGR02868 477 RQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
921-1153 |
8.74e-64 |
|
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: 216.33 E-value: 8.74e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGL 1000
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDAHIFDSSIRENLRLARTGATDEELRAALDRARLLDWAEALPAGLDTLVGEHGARLSGGQRQRLALARAILADFPVL 1080
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2351811981 1081 VLDEPAEHLDLATADALTADLLAATRGRTTVLITHRLQGLEAVDEVVVLEAGRVVQRGPYADLTAEEGPLRRM 1153
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
651-1157 |
1.60e-63 |
|
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: 226.91 E-value: 1.60e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 651 GLGRAVFRYAERLVShdavLKMLAELRVAVYRGLERIAPAGLRRSRRGDLLSRLVADVDAlqdywlrwllpagtavVVGA 730
Cdd:TIGR02203 68 GICSFVSTYLLSWVS----NKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQ----------------VASA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 731 ATAGFIGWLLPAAGIVLATGLLL---------AGAGVPLVSGACS------RHAERQLAPARADLATRITDLLGGTAELT 795
Cdd:TIGR02203 128 ATDAFIVLVRETLTVIGLFIVLLyyswqltliVVVMLPVLSILMRrvskrlRRISKEIQNSMGQVTTVAEETLQGYRVVK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 796 VAGALPARKARTREADGVLTRIAARAATATALGGGLIALIGGLTVVATALVALPAVHDGRLAGVELAVVVLTPLAAFEAV 875
Cdd:TIGR02203 208 LFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 876 TGLPLAVQYRQRVKRSAERVYEVLDAPPpvrEPDspAGTPASPFP---LEVRGLSARYAGAERDALDSVDLRLTAGRRIA 952
Cdd:TIGR02203 288 KSLTNVNAPMQRGLAAAESLFTLLDSPP---EKD--TGTRAIERArgdVEFRNVTFRYPGRDRPALDSISLVIEPGETVA 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 953 VVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGLCAQDAHIFDSSIRENLRLARTG-ATDEELRAA 1031
Cdd:TIGR02203 363 LVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEqADRAEIERA 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1032 LDRARLLDWAEALPAGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTADLLAATRGRTTV 1111
Cdd:TIGR02203 443 LAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTL 522
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2351811981 1112 LITHRLQGLEAVDEVVVLEAGRVVQRGPYADLTAEEG---PLRRMLERE 1157
Cdd:TIGR02203 523 VIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGlyaQLHNMQFRE 571
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
22-311 |
2.73e-63 |
|
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: 217.15 E-value: 2.73e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 22 VVALGVVGAALVIAQAMLVADVVVGGFEdGLTVSGLRTPLILLAAVALGRALVSWLTELAAYRASAAVKSELRGRLLDRA 101
Cdd:cd18561 1 SVLLGLLITALYIAQAWLLARALARIFA-GGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 102 AELGPGLLSDRRTGSLVTLATRGVDALDDYFARYLPQLGLAVVVPVAVLARIVTEDWVSAAIIVVTLPLIPLFMILIGWA 181
Cdd:cd18561 80 LKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 182 TQSRMDRQWRLLSRLSGHFLDVVAGLPTLKVFGRAKAQAESIRAITSQYRRATLRTLRIAFLSSFALELLATLSVALVAV 261
Cdd:cd18561 160 AKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALG 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2351811981 262 TIGMRLVHGELDLYTGLVVLILAPEAYLPIRQVGAQYHAAAEGLSAAEEI 311
Cdd:cd18561 240 VGALRVLGGQLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQGISAADSI 289
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
333-544 |
1.88e-62 |
|
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: 212.48 E-value: 1.88e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERIAW 412
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 413 VPQRPYLFAGTIAENVRLARPDADDGAVAAALRDAGAYDFVAELPDGAQTLLGEDGAGLSAGQRQRLALARAFLADRPLL 492
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2351811981 493 LLDEPTASLDGETEAGIVEAVRRLAQGRTVLLVVHRPALLPLADRVVRLEPG 544
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDG 212
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
158-544 |
3.05e-62 |
|
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: 226.29 E-value: 3.05e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 158 WVSAAIIVVTLPLIPLfMILIGWATQSRMDRQWRLLSRLS----GHFLDVVAGLPTLKVF---GRAKAQAESIRAITSqy 230
Cdd:TIGR03375 282 IIGGPLVWVPLVAIPL-ILLPGLLLQRPLSRLAEESMRESaqrnAVLVESLSGLETIKALnaeGRFQRRWEQTVAALA-- 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 231 rRATLRTLRIA-FLSSFALELLATLSVALVAVtiGMRLVhGELDLYTGLVV--LILAPEAYLPIRQVGA---QYHAAAEG 304
Cdd:TIGR03375 359 -RSGLKSRFLSnLATNFAQFIQQLVSVAIVVV--GVYLI-SDGELTMGGLIacVMLSGRALAPLGQLAGlltRYQQAKTA 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 305 LSAAEEIFSvLETEpRRGGTADV-PESLR--LELEGVTVRHEGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVL 381
Cdd:TIGR03375 435 LQSLDELMQ-LPVE-RPEGTRFLhRPRLQgeIEFRNVSFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLL 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 382 GFTAPDEGRVRVGGVDLATLAPERWRERIAWVPQRPYLFAGTIAENVRLARPDADDGAVAAALRDAGAYDFVAELPDGAQ 461
Cdd:TIGR03375 513 GLYQPTEGSVLLDGVDIRQIDPADLRRNIGYVPQDPRLFYGTLRDNIALGAPYADDEEILRAAELAGVTEFVRRHPDGLD 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 462 TLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQGRTVLLVVHRPALLPLADRVVRL 541
Cdd:TIGR03375 593 MQIGERGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVTHRTSLLDLVDRIIVM 672
|
...
gi 2351811981 542 EPG 544
Cdd:TIGR03375 673 DNG 675
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
344-544 |
2.54e-59 |
|
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: 203.23 E-value: 2.54e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 344 GRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERIAWVPQRPYLFAGT 423
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFSGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 424 IAENVRLARPDADDGAVAAALRDAGAYDFVAELPDGAQTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTASLDG 503
Cdd:cd03254 93 IMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2351811981 504 ETEAGIVEAVRRLAQGRTVLLVVHRPALLPLADRVVRLEPG 544
Cdd:cd03254 173 ETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDG 213
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
934-1157 |
4.18e-59 |
|
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: 203.23 E-value: 4.18e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 934 ERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGLCAQDAHIFDSSIR 1013
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDTVLFNDTIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1014 ENLRLARTGATDEELRAALDRARLLDWAEALPAGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLAT 1093
Cdd:cd03253 93 YNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 1094 ADALTADLLAATRGRTTVLITHRLQGLEAVDEVVVLEAGRVVQRGPYADLTAEEGPLRRMLERE 1157
Cdd:cd03253 173 EREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
332-544 |
2.53e-58 |
|
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: 200.12 E-value: 2.53e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 332 RLELEGVTVRHEGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERIA 411
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 412 WVPQRPYLFAGTIAENVRLARPDADDGAVAAALRDAGAYDFVAELPDGAQTLLGEDGAGLSAGQRQRLALARAFLADRPL 491
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2351811981 492 LLLDEPTASLDGETEAGIVEAVRRLAQGRTVLLVVHRPALLPLADRVVRLEPG 544
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSG 214
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
334-544 |
3.29e-58 |
|
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: 200.46 E-value: 3.29e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 334 ELEGVTVRHEGRGE-PSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERIAW 412
Cdd:cd03249 2 EFKNVSFRYPSRPDvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 413 VPQRPYLFAGTIAENVRLARPDADDGAVAAALRDAGAYDFVAELPDGAQTLLGEDGAGLSAGQRQRLALARAFLADRPLL 492
Cdd:cd03249 82 VSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2351811981 493 LLDEPTASLDGETEAGIVEAVRRLAQGRTVLLVVHRPALLPLADRVVRLEPG 544
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNG 213
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
922-1156 |
2.67e-57 |
|
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: 198.15 E-value: 2.67e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 922 EVRGLSARY-AGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGL 1000
Cdd:cd03249 2 EFKNVSFRYpSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDAHIFDSSIRENLRLARTGATDEELRAALDRARLLDWAEALPAGLDTLVGEHGARLSGGQRQRLALARAILADFPVL 1080
Cdd:cd03249 82 VSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2351811981 1081 VLDEPAEHLDLATADALTADLLAATRGRTTVLITHRLQGLEAVDEVVVLEAGRVVQRGPYADLTAEEGPLRRMLER 1156
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKA 237
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
921-1133 |
3.85e-57 |
|
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: 194.91 E-value: 3.85e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGL 1000
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDAHIFDSSIRENLrlartgatdeelraaldrarlldwaealpagldtlvgehgarLSGGQRQRLALARAILADFPVL 1080
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2351811981 1081 VLDEPAEHLDLATADALTADLLAATRGRTTVLITHRLQGLEAVDEVVVLEAGR 1133
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
921-1138 |
5.32e-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: 196.27 E-value: 5.32e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGL 1000
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDAHIFDSSIRENLRLARTGATDEELRAALDRARLLDWAEALPAGLDTLVGEHGARLSGGQRQRLALARAILADFPVL 1080
Cdd:cd03245 83 VPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2351811981 1081 VLDEPAEHLDLATADALTADLLAATRGRTTVLITHRLQGLEAVDEVVVLEAGRVVQRG 1138
Cdd:cd03245 163 LLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
938-1159 |
1.10e-55 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 204.31 E-value: 1.10e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 938 LDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLdAREGTYRIGGVDACVLEGDTVRGFVGLCAQDAHIFDSSIRENLR 1017
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVL 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1018 LARTGATDEELRAALDRARLLDWAEALPAGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADAL 1097
Cdd:PRK11174 445 LGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLV 524
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2351811981 1098 TADLLAATRGRTTVLITHRLQGLEAVDEVVVLEAGRVVQRGPYADLTAEEGPLRRMLERERE 1159
Cdd:PRK11174 525 MQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQE 586
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
880-1167 |
1.83e-55 |
|
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: 204.28 E-value: 1.83e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 880 LAVQYRQrVKRSA---ERVYEVLDAPPPVREPDSPAGTPASPFPLEVRGLSARYaGAERDALDSVDLRLTAGRRIAVVGP 956
Cdd:COG5265 315 LGFVYRE-IRQALadmERMFDLLDQPPEVADAPDAPPLVVGGGEVRFENVSFGY-DPERPILKGVSFEVPAGKTVAIVGP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 957 SGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGLCAQDAHIFDSSIRENLRLARTGATDEELRAALDRAR 1036
Cdd:COG5265 393 SGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQ 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1037 LLDWAEALPAGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTADLLAATRGRTTVLITHR 1116
Cdd:COG5265 473 IHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHR 552
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 1117 LQGLEAVDEVVVLEAGRVVQRGPYADLTAEEGPLRRMLERERETEGVAEEA 1167
Cdd:COG5265 553 LSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEEAEEAL 603
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
896-1148 |
4.04e-55 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 202.88 E-value: 4.04e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 896 YEVLDAPPPVREPDSPAGTPASPFPLEVRGLSARYAGAeRDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAR 975
Cdd:PRK13657 310 FEVEDAVPDVRDPPGAIDLGRVKGAVEFDDVSFSYDNS-RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQ 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 976 EGTYRIGGVDACVLEGDTVRGFVGLCAQDAHIFDSSIRENLRLARTGATDEELRAALDRARLLDWAEALPAGLDTLVGEH 1055
Cdd:PRK13657 389 SGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGER 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1056 GARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTADLLAATRGRTTVLITHRLQGLEAVDEVVVLEAGRVV 1135
Cdd:PRK13657 469 GRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVV 548
|
250
....*....|...
gi 2351811981 1136 QRGPYADLTAEEG 1148
Cdd:PRK13657 549 ESGSFDELVARGG 561
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
937-1148 |
1.01e-53 |
|
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: 187.43 E-value: 1.01e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 937 ALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGLCAQDAHIFDSSIRENL 1016
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFSGTIMENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1017 RLARTGATDEELRAALDRARLLDWAEALPAGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADA 1096
Cdd:cd03254 98 RLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2351811981 1097 LTADLLAATRGRTTVLITHRLQGLEAVDEVVVLEAGRVVQRGPYADLTAEEG 1148
Cdd:cd03254 178 IQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
921-1139 |
2.04e-52 |
|
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: 197.01 E-value: 2.04e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGL 1000
Cdd:TIGR03375 464 IEFRNVSFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGY 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDAHIFDSSIRENLRLARTGATDEELRAALDRARLLDWAEALPAGLDTLVGEHGARLSGGQRQRLALARAILADFPVL 1080
Cdd:TIGR03375 544 VPQDPRLFYGTLRDNIALGAPYADDEEILRAAELAGVTEFVRRHPDGLDMQIGERGRSLSGGQRQAVALARALLRDPPIL 623
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 1081 VLDEPAEHLDLATADALTADLLAATRGRTTVLITHRLQGLEAVDEVVVLEAGRVVQRGP 1139
Cdd:TIGR03375 624 LLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVTHRTSLLDLVDRIIVMDNGRIVADGP 682
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
3-528 |
2.83e-52 |
|
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: 194.65 E-value: 2.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 3 PIDPRLLRYARATRFFLAAVVALGVVGAALVIAQAMLVADVVVGGFEDGLTVsglrTPLILLAAVALGRALVSWLTEL-- 80
Cdd:COG5265 24 LLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAALLV----VPVGLLLAYGLLRLLSVLFGELrd 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 81 -----AAYRASAAVKSELRGRLLDraaelgpglLS-----DRRTGSLVTLATRGVDALDD--YFARY--LPQLGLAVVVP 146
Cdd:COG5265 100 alfarVTQRAVRRLALEVFRHLHA---------LSlrfhlERQTGGLSRDIERGTKGIEFllRFLLFniLPTLLEIALVA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 147 VAVLARIvteDWVSAAIIVVTlplIPLFMILIGWATQSRMD--RQW-RLLSRLSGHFLDVVAGLPTLKVFGRAKAQAESI 223
Cdd:COG5265 171 GILLVKY---DWWFALITLVT---VVLYIAFTVVVTEWRTKfrREMnEADSEANTRAVDSLLNYETVKYFGNEAREARRY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 224 RAITSQYRRATLRTLRIAFLSSFALELLATLSVALVAVTIGMRLVHGELDLytGLVVLI--LAPEAYLPIRQVGAQYHAA 301
Cdd:COG5265 245 DEALARYERAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTV--GDFVLVnaYLIQLYIPLNFLGFVYREI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 302 AEGLSAAEEIFSVLETEPRrggTADVPESLRLELEGVTVRHEG------RGEPSLDHASLVVDEGETVALVGPSGVGKST 375
Cdd:COG5265 323 RQALADMERMFDLLDQPPE---VADAPDAPPLVVGGGEVRFENvsfgydPERPILKGVSFEVPAGKTVAIVGPSGAGKST 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 376 LLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERIAWVPQRPYLFAGTIAENVRLARPDADDGAVAAALRDAGAYDFVAE 455
Cdd:COG5265 400 LARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIES 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2351811981 456 LPDGAQTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQGRTVLLVVHR 528
Cdd:COG5265 480 LPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHR 552
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
333-545 |
6.53e-52 |
|
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: 182.69 E-value: 6.53e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERIAW 412
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 413 VPQRPYLFAGTIAENVRLARPDADDGAVAAALRDAGAYDFVAELPDGAQTLLGEDGAGLSAGQRQRLALARAFLADRPLL 492
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2351811981 493 LLDEPTASLDGETEAGIVEAVRRLAQGRTVLLVVHRPALLPLADRVVRLEPGA 545
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGR 213
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
921-1139 |
2.05e-51 |
|
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: 180.38 E-value: 2.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGL 1000
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDAHIFDSSIRENLRlARTGATDEELRAALDRARLLDWAEALPAGLDTLVGEHGARLSGGQRQRLALARAILADFPVL 1080
Cdd:cd03244 83 IPQDPVLFSGTIRSNLD-PFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 1081 VLDEPAEHLDLATADALTADLLAATRGRTTVLITHRLQGLEAVDEVVVLEAGRVVQRGP 1139
Cdd:cd03244 162 VLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
282-545 |
4.45e-51 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 189.96 E-value: 4.45e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 282 ILAPEAYLPIRQVGAQYHAAAEGLSAAEEIFSVLETEPRRGGTADVPESL-RLELEGVTVRHEGRGEPSLDHASLVVDEG 360
Cdd:COG4618 279 ILMGRALAPIEQAIGGWKQFVSARQAYRRLNELLAAVPAEPERMPLPRPKgRLSVENLTVVPPGSKRPILRGVSFSLEPG 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 361 ETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERIAWVPQRPYLFAGTIAENV-RLARPDADDGA 439
Cdd:COG4618 359 EVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIaRFGDADPEKVV 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 440 VAAALrdAGAYDFVAELPDGAQTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRL-AQ 518
Cdd:COG4618 439 AAAKL--AGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkAR 516
|
250 260
....*....|....*....|....*..
gi 2351811981 519 GRTVLLVVHRPALLPLADRVVRLEPGA 545
Cdd:COG4618 517 GATVVVITHRPSLLAAVDKLLVLRDGR 543
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
921-1148 |
1.12e-50 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 189.46 E-value: 1.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGL 1000
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDAHIFDSSIRENLRLARTGA-TDEELRAALDRARLLDWAEALPAGLDTLVGEHGARLSGGQRQRLALARAILADFPV 1079
Cdd:PRK11176 422 VSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPI 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 1080 LVLDEPAEHLDLATADALTADLLAATRGRTTVLITHRLQGLEAVDEVVVLEAGRVVQRGPYADLTAEEG 1148
Cdd:PRK11176 502 LILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNG 570
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
333-545 |
7.22e-50 |
|
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: 174.33 E-value: 7.22e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERIAW 412
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 413 VPQRPYLFAGTIAENVrlarpdaddgavaaalrdagaydfvaelpdgaqtllgedgagLSAGQRQRLALARAFLADRPLL 492
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 493 LLDEPTASLDGETEAGIVEAVRRL-AQGRTVLLVVHRPALLPLADRVVRLEPGA 545
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGR 172
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
346-544 |
2.21e-48 |
|
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: 172.41 E-value: 2.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 346 GEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERIAWVPQRPYLFAGTIA 425
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDTVLFNDTIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 426 ENVRLARPDADDGAVAAALRDAGAYDFVAELPDGAQTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGET 505
Cdd:cd03253 93 YNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHT 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 2351811981 506 EAGIVEAVRRLAQGRTVLLVVHRPALLPLADRVVRLEPG 544
Cdd:cd03253 173 EREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDG 211
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
215-548 |
7.53e-48 |
|
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: 180.24 E-value: 7.53e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 215 RAKAQAESIRAITSQyRRATLRTLRIAFLSSFALELLATLSVALVAVTIgmrlVHGELDlyTGLVVL--ILAPEAYLPIR 292
Cdd:TIGR01842 203 TKRWGRFHSKYLSAQ-SAASDRAGMLSNLSKYFRIVLQSLVLGLGAYLA----IDGEIT--PGMMIAgsILVGRALAPID 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 293 QVGAQYHAAAEGLSAAEEIFSVLETEPRRGGTADVPE-SLRLELEGVTVRHEGRGEPSLDHASLVVDEGETVALVGPSGV 371
Cdd:TIGR01842 276 GAIGGWKQFSGARQAYKRLNELLANYPSRDPAMPLPEpEGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGS 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 372 GKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERIAWVPQRPYLFAGTIAENVRLARPDADDGAVAAALRDAGAYD 451
Cdd:TIGR01842 356 GKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHE 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 452 FVAELPDGAQTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRL-AQGRTVLLVVHRPA 530
Cdd:TIGR01842 436 LILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPS 515
|
330
....*....|....*...
gi 2351811981 531 LLPLADRVVRLEPGATLR 548
Cdd:TIGR01842 516 LLGCVDKILVLQDGRIAR 533
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
333-544 |
9.76e-48 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 169.61 E-value: 9.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERIAW 412
Cdd:COG4619 1 LELEGLSFRVGGK--PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 413 VPQRPYLFAGTIAENVRLARPDADDGAVAAALRDAGAYdfvAELPDgaqTLLGEDGAGLSAGQRQRLALARAFLADRPLL 492
Cdd:COG4619 79 VPQEPALWGGTVRDNLPFPFQLRERKFDRERALELLER---LGLPP---DILDKPVERLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2351811981 493 LLDEPTASLDGETEAGIVEAVRRLAQ--GRTVLLVVHRPALLP-LADRVVRLEPG 544
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYLAeeGRAVLWVSHDPEQIErVADRVLTLEAG 207
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
886-1159 |
5.39e-47 |
|
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: 180.32 E-value: 5.39e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 886 QRVKRSAERVYEVLDAPPPVRePDSPAGTPASPFPLEVRGLSARYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLA 965
Cdd:TIGR01846 422 QQTGIALERLGDILNSPTEPR-SAGLAALPELRGAITFENIRFRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLT 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 966 QVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGLCAQDAHIFDSSIRENLRLARTGATDEELRAALDRARLLDWAEALP 1045
Cdd:TIGR01846 501 KLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELP 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1046 AGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTADLLAATRGRTTVLITHRLQGLEAVDE 1125
Cdd:TIGR01846 581 QGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDR 660
|
250 260 270
....*....|....*....|....*....|....
gi 2351811981 1126 VVVLEAGRVVQRGPYADLTAEEGPLRRMLERERE 1159
Cdd:TIGR01846 661 IIVLEKGQIAESGRHEELLALQGLYARLWQQQSG 694
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
7-544 |
1.50e-46 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 177.08 E-value: 1.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 7 RLLR-YARATRFFLA-AVVALGVVGAALVIAQAMLVADVVVGGFEDGLtvSGLRTPLILLAA-VALG------RALVSWL 77
Cdd:PRK13657 2 SLFRlYARVLQYLGAeKRLGILLAVANVLLAAATFAEPILFGRIIDAI--SGKGDIFPLLAAwAGFGlfniiaGVLVARH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 78 TELAAYRASAAVKSELRGRLLDraaeLGPGLLSDRRTGSLVTLATRGVDALDDYFARYLPQLGLAVVVPVAVLARIVTED 157
Cdd:PRK13657 80 ADRLAHRRRLAVLTEYFERIIQ----LPLAWHSQRGSGRALHTLLRGTDALFGLWLEFMREHLATLVALVVLLPLALFMN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 158 WVSAAIIVVtlpLIPLFMILIGWATQSRMDRQWRL---LSRLSGHFLDVVAGLPTLKVFGRAKAQAESIRAITSQYRRAT 234
Cdd:PRK13657 156 WRLSLVLVV---LGIVYTLITTLVMRKTKDGQAAVeehYHDLFAHVSDAIGNVSVVQSYNRIEAETQALRDIADNLLAAQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 235 LRTLRIAFLSSFALELLATLSVaLVAVTIGMRLV-HGELDLytGLVVLILAPEAYLPIR--QVGAQYHAAAEGLSAAEEI 311
Cdd:PRK13657 233 MPVLSWWALASVLNRAASTITM-LAILVLGAALVqKGQLRV--GEVVAFVGFATLLIGRldQVVAFINQVFMAAPKLEEF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 312 FSVLETEPRRGGTADVPESLRL----ELEGVTVRHEGRGePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPD 387
Cdd:PRK13657 310 FEVEDAVPDVRDPPGAIDLGRVkgavEFDDVSFSYDNSR-QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 388 EGRVRVGGVDLATLAPERWRERIAWVPQRPYLFAGTIAENVRLARPDADDGAVAAALRDAGAYDFVAELPDGAQTLLGED 467
Cdd:PRK13657 389 SGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGER 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2351811981 468 GAGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQGRTVLLVVHRPALLPLADRVVRLEPG 544
Cdd:PRK13657 469 GRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNG 545
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
886-1148 |
2.37e-46 |
|
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: 178.78 E-value: 2.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 886 QRVKRSAERVYEVLDAPPPVREPDSPAGTPASPFPLEVRGLSARYaGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLA 965
Cdd:TIGR01193 439 QAARVANNRLNEVYLVDSEFINKKKRTELNNLNGDIVINDVSYSY-GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLA 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 966 QVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGLCAQDAHIFDSSIRENLRL-ARTGATDEELRAALDRARLLDWAEAL 1044
Cdd:TIGR01193 518 KLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLgAKENVSQDEIWAACEIAEIKDDIENM 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1045 PAGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTADLLAATRgRTTVLITHRLQGLEAVD 1124
Cdd:TIGR01193 598 PLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSD 676
|
250 260
....*....|....*....|....
gi 2351811981 1125 EVVVLEAGRVVQRGPYADLTAEEG 1148
Cdd:TIGR01193 677 KIIVLDHGKIIEQGSHDELLDRNG 700
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
921-1153 |
3.48e-46 |
|
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: 166.12 E-value: 3.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGL 1000
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDAHIFDSSIRENLRLARTGATDEELRAALDRARLLDWAEALPAGLDTLVGEHGARLSGGQRQRLALARAILADFPVL 1080
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2351811981 1081 VLDEPAEHLDLATADALTADLLAATRGRTTVLITHRLQGLEAVDEVVVLEAGRVVQRGPYADLTAEEGPLRRM 1153
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
886-1139 |
4.91e-46 |
|
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: 175.32 E-value: 4.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 886 QRVKRSAERVYEVLDAPPPVREPDSpagTPASPFPLEVRGLSARYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLA 965
Cdd:COG4618 299 VSARQAYRRLNELLAAVPAEPERMP---LPRPKGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 966 QVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGLCAQDAHIFDSSIRENLrlAR-TGATDEELRAALDRARLLDWAEAL 1044
Cdd:COG4618 376 RLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENI--ARfGDADPEKVVAAAKLAGVHEMILRL 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1045 PAGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTADLLAA-TRGRTTVLITHRLQGLEAV 1123
Cdd:COG4618 454 PDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAV 533
|
250
....*....|....*.
gi 2351811981 1124 DEVVVLEAGRVVQRGP 1139
Cdd:COG4618 534 DKLLVLRDGRVQAFGP 549
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
212-544 |
1.39e-45 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 174.05 E-value: 1.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 212 VFGRAKAQAESIRAITSQYRRATLRTLRIAFLSSFALELLATLSVALVAVTIGMRLVHGELDLYTGLVVL-----ILAPE 286
Cdd:PRK11176 219 IFGGQEVETKRFDKVSNRMRQQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFssmiaLMRPL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 287 AYLPirQVGAQYHaaaEGLSAAEEIFSVLETEPRRGGTADVPESLR--LELEGVTVRHEGRGEPSLDHASLVVDEGETVA 364
Cdd:PRK11176 299 KSLT--NVNAQFQ---RGMAACQTLFAILDLEQEKDEGKRVIERAKgdIEFRNVTFTYPGKEVPALRNINFKIPAGKTVA 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 365 LVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERIAWVPQRPYLFAGTIAENVRLARPDA-DDGAVAAA 443
Cdd:PRK11176 374 LVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEA 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 444 LRDAGAYDFVAELPDGAQTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQGRTVL 523
Cdd:PRK11176 454 ARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSL 533
|
330 340
....*....|....*....|.
gi 2351811981 524 LVVHRPALLPLADRVVRLEPG 544
Cdd:PRK11176 534 VIAHRLSTIEKADEILVVEDG 554
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
332-544 |
1.58e-45 |
|
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: 163.43 E-value: 1.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 332 RLELEGVTVRHEGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERIA 411
Cdd:cd03244 2 DIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 412 WVPQRPYLFAGTIAENV---------RLARpdaddgavaaALRDAGAYDFVAELPDGAQTLLGEDGAGLSAGQRQRLALA 482
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLdpfgeysdeELWQ----------ALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2351811981 483 RAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQGRTVLLVVHRPALLPLADRVVRLEPG 544
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKG 213
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
162-544 |
2.57e-44 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 170.39 E-value: 2.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 162 AIIVVTLPLIPLFMILIGWA-----TQSRmdRQWRLLsrlsghFLDVVAGLPTLKVFG-----RAKAQAESIRAITSQYR 231
Cdd:PRK11160 168 GILLLLLLLLPLLFYRLGKKpgqdlTHLR--AQYRVQ------LTEWLQGQAELTLFGaedryRQQLEQTEQQWLAAQRR 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 232 RATLRTLRIAFLSsFALELLATLSVALVAVTIGMRLVHGELdlyTGLVVL-------ILAP--EAYLPIRQVgaqyhaaa 302
Cdd:PRK11160 240 QANLTGLSQALMI-LANGLTVVLMLWLAAGGVGGNAQPGAL---IALFVFaalaafeALMPvaGAFQHLGQV-------- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 303 egLSAAEEIFSVLETEPR---RGGTADVPESLRLELEGVTVRHEGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDV 379
Cdd:PRK11160 308 --IASARRINEITEQKPEvtfPTTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQL 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 380 VLGFTAPDEGRVRVGGVDLATLAPERWRERIAWVPQRPYLFAGTIAENVRLARPDADDGAVAAALRDAGaYDFVAELPDG 459
Cdd:PRK11160 386 LTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVG-LEKLLEDDKG 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 460 AQTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQGRTVLLVVHRPALLPLADRVV 539
Cdd:PRK11160 465 LNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRIC 544
|
....*
gi 2351811981 540 RLEPG 544
Cdd:PRK11160 545 VMDNG 549
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
921-1138 |
1.34e-43 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 156.32 E-value: 1.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEgDTVRGFVGL 1000
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDAHIFDSSIRENLrlartgatdeelraaldrarlldwaealpagldtlvgehGARLSGGQRQRLALARAILADFPVL 1080
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2351811981 1081 VLDEPAEHLDLATADALTADLLAATRGRTTVLITHRLQGLEAVDEVVVLEAGRVVQRG 1138
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
202-1153 |
9.67e-43 |
|
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: 170.90 E-value: 9.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 202 DVVAGLPTLKVFGRAKAQAESIRAItsqyRRATLRTLRI-AFLSSFAL------ELLATLSVALVAVTIGMRLVhgeLDL 274
Cdd:TIGR00957 501 EILNGIKVLKLYAWELAFLDKVEGI----RQEELKVLKKsAYLHAVGTftwvctPFLVALITFAVYVTVDENNI---LDA 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 275 YTGLVVLILAPEAYLPIR---QVGAQYHAAAEGLSAAEEIFSVLETEPRRGGTADVPESlrlELEGVTVRHE----GRGE 347
Cdd:TIGR00957 574 EKAFVSLALFNILRFPLNilpMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPG---EGNSITVHNAtftwARDL 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 348 P-SLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGvdlatlaperwreRIAWVPQRPYLFAGTIAE 426
Cdd:TIGR00957 651 PpTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRE 717
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 427 NVRLARPDADDGAVAAALRDAGAYDfVAELPDGAQTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETE 506
Cdd:TIGR00957 718 NILFGKALNEKYYQQVLEACALLPD-LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVG 796
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 507 AGIVEAV---RRLAQGRTVLLVVHRPALLPLADRVVRLEPGA----------------------TLRPEKPEGSVAVPRP 561
Cdd:TIGR00957 797 KHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKisemgsyqellqrdgafaeflrTYAPDEQQGHLEDSWT 876
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 562 ADASAAGRAAVPEPETLRDTAARPGQVL-------------------------ARVREAAG----AQRGQLALALLLGSL 612
Cdd:TIGR00957 877 ALVSGEGKEAKLIENGMLVTDVVGKQLQrqlsasssdsgdqsrhhgssaelqkAEAKEETWklmeADKAQTGQVELSVYW 956
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 613 ALGSAVGL-----------------MAVSGWLiSRASEQPPV------LYLMVAVTATRAFGLGRAVFRYAERLvshdAV 669
Cdd:TIGR00957 957 DYMKAIGLfitflsiflfvcnhvsaLASNYWL-SLWTDDPMVngtqnnTSLRLSVYGALGILQGFAVFGYSMAV----SI 1031
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 670 LKMLAE--LRVAVYRGLERIAPAGLRRSRRGDLLSRLVADVDALQD-------YWLRWLLPA-GTAVVVGAATAgfigwl 739
Cdd:TIGR00957 1032 GGIQASrvLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSmippvikMFMGSLFNViGALIVILLATP------ 1105
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 740 lPAAGIVLATGLLLAGagVPLVSGACSRHAERQLAPARADLATRITDLLGGtaeLTVAGALPARKARTREADgvltriaa 819
Cdd:TIGR00957 1106 -IAAVIIPPLGLLYFF--VQRFYVASSRQLKRLESVSRSPVYSHFNETLLG---VSVIRAFEEQERFIHQSD-------- 1171
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 820 raatatalggglialiggLTVVATALVALPAVHDGRLAGVELAVV--VLTPLAAFEAVTG--------LPLAVQYRQRVK 889
Cdd:TIGR00957 1172 ------------------LKVDENQKAYYPSIVANRWLAVRLECVgnCIVLFAALFAVISrhslsaglVGLSVSYSLQVT 1233
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 890 R-----------------SAERVYEV----LDAPPPVREPDSPAGTPASPfPLEVRGLSARYagaeRDALDSV--DLRLT 946
Cdd:TIGR00957 1234 FylnwlvrmssemetnivAVERLKEYseteKEAPWQIQETAPPSGWPPRG-RVEFRNYCLRY----REDLDLVlrHINVT 1308
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 947 --AGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGLCAQDAHIFDSSIRENLRlARTGAT 1024
Cdd:TIGR00957 1309 ihGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLD-PFSQYS 1387
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1025 DEELRAALDRARLLDWAEALPAGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTADLLAA 1104
Cdd:TIGR00957 1388 DEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQ 1467
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*....
gi 2351811981 1105 TRGRTTVLITHRLQGLEAVDEVVVLEAGRVVQRGPYADLTAEEGPLRRM 1153
Cdd:TIGR00957 1468 FEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
333-544 |
7.56e-42 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 153.28 E-value: 7.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHeGRGEPS---LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERW--- 406
Cdd:COG1136 5 LELRNLTKSY-GTGEGEvtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 407 -RERIAWVPQRPYLFAG-TIAENVRLArpdaddgavaaaLRDAGAYdfVAELPDGAQTLLGEDGAG---------LSAGQ 475
Cdd:COG1136 84 rRRHIGFVFQFFNLLPElTALENVALP------------LLLAGVS--RKERRERARELLERVGLGdrldhrpsqLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 476 RQRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQ--GRTVLLVVHRPALLPLADRVVRLEPG 544
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDG 220
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
851-1155 |
9.80e-42 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 164.73 E-value: 9.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 851 VHDGRLAGVELaVVVLTPLAAF-EAVTGLPLAVQYRQRVKRSAERVYEVLDAP--PPVREPDSPAGTPASPFPL----EV 923
Cdd:TIGR03796 402 VMEGQLTIGML-VAFQSLMSSFlEPVNNLVGFGGTLQELEGDLNRLDDVLRNPvdPLLEEPEGSAATSEPPRRLsgyvEL 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 924 RGLSARYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGLCAQ 1003
Cdd:TIGR03796 481 RNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQ 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1004 DAHIFDSSIRENLRLARTGATDEELRAALDRARLLDWAEALPAGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLD 1083
Cdd:TIGR03796 561 DIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILD 640
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2351811981 1084 EPAEHLDLATADALTADLlaATRGRTTVLITHRLQGLEAVDEVVVLEAGRVVQRGPYADLTAEEGPLRRMLE 1155
Cdd:TIGR03796 641 EATSALDPETEKIIDDNL--RRRGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARLIR 710
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
334-544 |
6.83e-41 |
|
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: 147.78 E-value: 6.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 334 ELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERIAWV 413
Cdd:cd00267 1 EIENLSFRYGGR--TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 414 PQrpylfagtiaenvrlarpdaddgavaaalrdagaydfvaelpdgaqtllgedgagLSAGQRQRLALARAFLADRPLLL 493
Cdd:cd00267 79 PQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2351811981 494 LDEPTASLDGETEAGIVEAVRRLAQ-GRTVLLVVHRPALL-PLADRVVRLEPG 544
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAeLAADRVIVLKDG 156
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
333-544 |
2.86e-40 |
|
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: 148.41 E-value: 2.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRGEPS--LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERW---- 406
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 407 RERIAWVPQRPYLFAG-TIAENVRLArpdaddgavaaaLRDAGayDFVAELPDGAQTLLGEDGAG---------LSAGQR 476
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELP------------LLLAG--VPKKERRERAEELLERVGLGdrlnhypseLSGGQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 477 QRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQ--GRTVLLVVHRPALLPLADRVVRLEPG 544
Cdd:cd03255 147 QRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
333-544 |
3.86e-39 |
|
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: 144.53 E-value: 3.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRGEPS---LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGvdlatlaperwreR 409
Cdd:cd03250 1 ISVEDASFTWDSGEQETsftLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 410 IAWVPQRPYLFAGTIAENVRLARPdaddgavaaalRDAGAYDFV----------AELPDGAQTLLGEDGAGLSAGQRQRL 479
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKP-----------FDEERYEKVikacalepdlEILPDGDLTEIGEKGINLSGGQKQRI 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2351811981 480 ALARAFLADRPLLLLDEPTASLDGETEAGIVEAV--RRLAQGRTVLLVVHRPALLPLADRVVRLEPG 544
Cdd:cd03250 137 SLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCilGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
333-539 |
1.29e-38 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 144.05 E-value: 1.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATlAPERWRERIAW 412
Cdd:COG1131 1 IEVRGLTKRYGDK--TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 413 VPQRPYLFAG-TIAENVRLARPDADDGAVAAALRDAGAYDFVaELPDGAQTLLGEdgagLSAGQRQRLALARAFLADRPL 491
Cdd:COG1131 78 VPQEPALYPDlTVRENLRFFARLYGLPRKEARERIDELLELF-GLTDAADRKVGT----LSGGMKQRLGLALALLHDPEL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2351811981 492 LLLDEPTASLDGETEAGIVEAVRRLA-QGRTVLLVVHrpaLLP----LADRVV 539
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLRELAaEGKTVLLSTH---YLEeaerLCDRVA 202
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
334-541 |
1.53e-38 |
|
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: 143.06 E-value: 1.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 334 ELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDlatlaPERWRERIAWV 413
Cdd:cd03235 1 EVEDLTVSYGGH--PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKP-----LEKERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 414 PQRPYL---FAGTIAENVRLARpdADDGAVAAALRDAG------AYDFVaELPDGAQTLLGEdgagLSAGQRQRLALARA 484
Cdd:cd03235 74 PQRRSIdrdFPISVRDVVLMGL--YGHKGLFRRLSKADkakvdeALERV-GLSELADRQIGE----LSGGQQQRVLLARA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 485 FLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQ-GRTVLLVVH-RPALLPLADRVVRL 541
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRReGMTILVVTHdLGLVLEYFDRVLLL 205
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
334-544 |
1.62e-38 |
|
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: 142.99 E-value: 1.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 334 ELEGVTVRHEGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERIAWV 413
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 414 PQRP--YLFAGTIAENVRLARPDADDGAVAAALRDAGAYDFVaelpdGAQTLLGEDGAGLSAGQRQRLALARAfLADRP- 490
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELV-----GLEGLRDRSPFTLSGGQKQRVAIAGV-LAMDPd 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2351811981 491 LLLLDEPTASLDGETEAGIVEAVRRL-AQGRTVLLVVHRPALL-PLADRVVRLEPG 544
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLkAEGKTIIIVTHDLDLLlELADRVIVLEDG 210
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
332-545 |
1.65e-38 |
|
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: 143.77 E-value: 1.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 332 RLELEGVTVRHEGRGE-PSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERI 410
Cdd:cd03248 11 IVKFQNVTFAYPTRPDtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 411 AWVPQRPYLFAGTIAENVRLARPDADDGAVAAALRDAGAYDFVAELPDGAQTLLGEDGAGLSAGQRQRLALARAFLADRP 490
Cdd:cd03248 91 SLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2351811981 491 LLLLDEPTASLDGETEAGIVEAVRRLAQGRTVLLVVHRPALLPLADRVVRLEPGA 545
Cdd:cd03248 171 VLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGR 225
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
333-541 |
1.67e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 144.08 E-value: 1.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDlatlaPERWRERIAW 412
Cdd:COG1121 7 IELENLTVSYGGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP-----PRRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 413 VPQRPYL---FAGTIAENVRLAR----------PDADDGAVAAALRDAGAYDFvaelpdgAQTLLGEdgagLSAGQRQRL 479
Cdd:COG1121 80 VPQRAEVdwdFPITVRDVVLMGRygrrglfrrpSRADREAVDEALERVGLEDL-------ADRPIGE----LSGGQQQRV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 480 ALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRL-AQGRTVLLVVHRP-ALLPLADRVVRL 541
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLgAVREYFDRVLLL 212
|
|
| ABC_6TM_AarD_CydDC_like |
cd18781 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine ... |
23-311 |
2.44e-38 |
|
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: 145.37 E-value: 2.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 23 VALGVVGAALVIAQAMLVADVVVGGFEDGLTVSGLRTPLILLAAVALGRALVSWLTELAAYRASAAVKSELRGRLLDRAA 102
Cdd:cd18781 2 VLLQWISLLANIAFVFSIANLLQKLLEGKLTTASLLIVLGILAIAIIVRFICTRLASRASYRASADVKKTLREKIYDKLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 103 ELGPGLLSDRRTGSLVTLATRGVDALDDYFARYLPQLGLAVVVPVAVLARIVTEDWVSAAIIVVTLPLIPLFMILIGWAT 182
Cdd:cd18781 82 RLGPSYQEKVSTAEVVQLSVEGVEQLEIYFGRYLPQFFYSMLAPLTLFVVLAPINWKAALVLLICVPLIPISIIAVQKIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 183 QSRMDRQWRLLSRLSGHFLDVVAGLPTLKVFGRAKAQAESIRAITSQYRRATLRTLRIAFLSSFALELLATLSVALVAVT 262
Cdd:cd18781 162 KKLLSKYWGSYTDLGDSFLENLQGLTTLKIYQADERRHEEMNEEAEDFRKITMKVLTMQLNSITVMDLVAYGGAALGIIL 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2351811981 263 IGMRLVHGELDLYTGLVVLILAPEAYLPIRQVGAQYHAAAEGLSAAEEI 311
Cdd:cd18781 242 ALLQFANGSISLAGALFIILLSAEFFLPLRLLGSFFHIAMNGMAASDKI 290
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
921-1152 |
3.44e-38 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 142.86 E-value: 3.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGaERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGL 1000
Cdd:COG1122 1 IELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQ--DAHIFDSSIRENLR--LARTGATDEELraaldRARLLDWAEALpaGLDTLVGEHGARLSGGQRQRLALARAILAD 1076
Cdd:COG1122 80 VFQnpDDQLFAPTVEEDVAfgPENLGLPREEI-----RERVEEALELV--GLEHLADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 1077 FPVLVLDEPAEHLDLATADALtADLLAA--TRGRTTVLITHRLQGLEAV-DEVVVLEAGRVVQRGPYADLTAEEGPLRR 1152
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRREL-LELLKRlnKEGKTVIIVTHDLDLVAELaDRVIVLDDGRIVADGTPREVFSDYELLEE 230
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
333-544 |
1.14e-37 |
|
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: 139.07 E-value: 1.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATlAPERWRERIAW 412
Cdd:cd03230 1 IEVRNLSKRYGKK--TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 413 VPQRPYLFAG-TIAENVRlarpdaddgavaaalrdagaydfvaelpdgaqtllgedgagLSAGQRQRLALARAFLADRPL 491
Cdd:cd03230 78 LPEEPSLYENlTVRENLK-----------------------------------------LSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2351811981 492 LLLDEPTASLDGETEAGIVEAVRRLA-QGRTVLLVVHRPALLP-LADRVVRLEPG 544
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKkEGKTILLSSHILEEAErLCDRVAILNNG 171
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
921-1134 |
1.65e-37 |
|
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: 138.89 E-value: 1.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGL 1000
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDAHIFDSSIRENLrlartgatdeelraaldrarlldwaealpagldtlvgehgarLSGGQRQRLALARAILADFPVL 1080
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2351811981 1081 VLDEPAEHLDLATADALTADLLAA-TRGRTTVLITHRLQGLEAVDEVVVLEAGRV 1134
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
921-1133 |
2.91e-37 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 139.14 E-value: 2.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAERDA---LDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVdacvlegdtvrgf 997
Cdd:cd03250 1 ISVEDASFTWDSGEQETsftLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 998 VGLCAQDAHIFDSSIRENLRLartGAT-DEE-LRAALDRARLLDWAEALPAGLDTLVGEHGARLSGGQRQRLALARAILA 1075
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILF---GKPfDEErYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1076 DFPVLVLDEPAEHLDLATADALTADLL--AATRGRTTVLITHRLQGLEAVDEVVVLEAGR 1133
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVGRHIFENCIlgLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
333-544 |
3.88e-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: 137.83 E-value: 3.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERwRERIAW 412
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKAL-SSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 413 VPQRPYLFAGTIAENVrlarpdaddgavaaalrdagaydfvaelpdgaqtllgedGAGLSAGQRQRLALARAFLADRPLL 492
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2351811981 493 LLDEPTASLDGETEAGIVEAVRRLAQGRTVLLVVHRPALLPLADRVVRLEPG 544
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENG 172
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
889-1146 |
7.03e-37 |
|
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: 147.49 E-value: 7.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 889 KRSAERVYEVLDAPPPvrePDSPAGTPASPFPLEVRGLSARYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVL 968
Cdd:TIGR01842 288 RQAYKRLNELLANYPS---RDPAMPLPEPEGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLI 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 969 LRFLDAREGTYRIGGVDACVLEGDTVRGFVGLCAQDAHIFDSSIRENLRLARTGATDEELRAALDRARLLDWAEALPAGL 1048
Cdd:TIGR01842 365 VGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGY 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1049 DTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTADLLAA-TRGRTTVLITHRLQGLEAVDEVV 1127
Cdd:TIGR01842 445 DTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCVDKIL 524
|
250
....*....|....*....
gi 2351811981 1128 VLEAGRVVQRGPYADLTAE 1146
Cdd:TIGR01842 525 VLQDGRIARFGERDEVLAK 543
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
640-1157 |
1.15e-36 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 148.57 E-value: 1.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 640 LMVAVTATRAFGLGRAVFRYAERLvshdAVLKML----AELRVAVYRGLERIAPAGLRRSRRGDLLSRLVAdVDALqdyw 715
Cdd:TIGR03797 175 LVQIALALLAAAVGAAAFQLAQSL----AVLRLEtrmdASLQAAVWDRLLRLPVSFFRQYSTGDLASRAMG-ISQI---- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 716 lRWLLpagTAVVVGAATAGFIG----WLLPAAGIVLA---TGLLLAGAGVPLVSGACSRHAERQLAPARADLATRITDLL 788
Cdd:TIGR03797 246 -RRIL---SGSTLTTLLSGIFAllnlGLMFYYSWKLAlvaVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLI 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 789 GGTAELTVAGA----------LPARKART-READGVltriaaraatatalggglialiggLTVVATALVALPAVHDGRL- 856
Cdd:TIGR03797 322 NGISKLRVAGAenrafarwakLFSRQRKLeLSAQRI------------------------ENLLTVFNAVLPVLTSAALf 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 857 --AGVELAVVVLTP------LAAF----EAVTGLPLAVQYRQRVKRSAERVYEVLDAPPPVREPDSPAGTPASPfpLEVR 924
Cdd:TIGR03797 378 aaAISLLGGAGLSLgsflafNTAFgsfsGAVTQLSNTLISILAVIPLWERAKPILEALPEVDEAKTDPGKLSGA--IEVD 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 925 GLSARYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGLCAQD 1004
Cdd:TIGR03797 456 RVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQN 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1005 AHIFDSSIRENLrLARTGATDEELRAALDRARLLDWAEALPAGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDE 1084
Cdd:TIGR03797 536 GRLMSGSIFENI-AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDE 614
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2351811981 1085 PAEHLDLATADALTADL--LAATRgrttVLITHRLQGLEAVDEVVVLEAGRVVQRGPYADLTAEEGPLRRMLERE 1157
Cdd:TIGR03797 615 ATSALDNRTQAIVSESLerLKVTR----IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLARRQ 685
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
344-544 |
1.40e-36 |
|
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: 148.73 E-value: 1.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 344 GRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERIAWVPQRPYLFAGT 423
Cdd:TIGR01193 484 GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGS 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 424 IAENVRL-ARPDADDGAVAAALRDAGAYDFVAELPDGAQTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTASLD 502
Cdd:TIGR01193 564 ILENLLLgAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2351811981 503 GETEAGIVEAVRRLaQGRTVLLVVHRPALLPLADRVVRLEPG 544
Cdd:TIGR01193 644 TITEKKIVNNLLNL-QDKTIIFVAHRLSVAKQSDKIIVLDHG 684
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
32-546 |
2.92e-36 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 146.01 E-value: 2.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 32 LVIAQAMLVADVVVGGFEDGLTVSGLRTPLIL-----LAAVALGRALVSWLTELAAYRASAAVKSELRGRLLDRAAELGP 106
Cdd:PRK10789 5 IIIAMLQLIPPKVVGIIVDGVTEQHMTTGQILmwigtMVLIAVVVYLLRYVWRVLLFGASYQLAVELREDFYRQLSRQHP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 107 GLLSDRRTGSLVTLATRGVDALddYFARYLPQLGLAVVVPVAVLARIVTEDWVSAAIIVVTLPLIPLFMILI---GWATQ 183
Cdd:PRK10789 85 EFYLRHRTGDLMARATNDVDRV--VFAAGEGVLTLVDSLVMGCAVLIVMSTQISWQLTLLALLPMPVMAIMIkryGDQLH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 184 SRMDRQWRLLSRLSGHFLDVVAGLPTLKVFGRAKAQAESIRAITSQYRRATLRTLRIAflSSFALELLATLSVA-LVAVT 262
Cdd:PRK10789 163 ERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARID--ARFDPTIYIAIGMAnLLAIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 263 IGMRLV-HGELDL--------YTGLVVLilapeaylPIRQVGAQYHAAAEGLSAAEEIFSVLETEPR-RGGTADVPESlR 332
Cdd:PRK10789 241 GGSWMVvNGSLTLgqltsfvmYLGLMIW--------PMLALAWMFNIVERGSAAYSRIRAMLAEAPVvKDGSEPVPEG-R 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEgVTVRH---EGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRER 409
Cdd:PRK10789 312 GELD-VNIRQftyPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 410 IAWVPQRPYLFAGTIAENVRLARPDADDGAVAAALRDAGAYDFVAELPDGAQTLLGEDGAGLSAGQRQRLALARAFLADR 489
Cdd:PRK10789 391 LAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNA 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2351811981 490 PLLLLDEPTASLDGETEAGIVEAVRRLAQGRTVLLVVHRPALLPLADRVVRLEPGAT 546
Cdd:PRK10789 471 EILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHI 527
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
333-544 |
5.16e-36 |
|
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: 136.54 E-value: 5.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVV-----LGFTAPDEGRVRVGGVDLATLA--PER 405
Cdd:cd03260 1 IELRDLNVYYGDK--HALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDIYDLDvdVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 406 WRERIAWVPQRPYLFAGTIAENVRLA-------RPDADDGAVAAALRDAGAYDFVAelpDGAqtllgeDGAGLSAGQRQR 478
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKAALWDEVK---DRL------HALGLSGGQQQR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2351811981 479 LALARAfLADRP-LLLLDEPTASLDGETEAGIVEAVRRLAQGRTVLLVVHRPA-LLPLADRVVRLEPG 544
Cdd:cd03260 150 LCLARA-LANEPeVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQqAARVADRTAFLLNG 216
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
891-1154 |
7.27e-36 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 146.41 E-value: 7.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 891 SAERVYEVLDAPPPVrepdSPAGTPASPF---PLEVRGLSARYAG-AERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQ 966
Cdd:TIGR00958 450 ASEKVFEYLDRKPNI----PLTGTLAPLNlegLIEFQDVSFSYPNrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAA 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 967 VLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGLCAQDAHIFDSSIRENLRLARTGATDEELRAALDRARLLDWAEALPA 1046
Cdd:TIGR00958 526 LLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPN 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1047 GLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTADLLAAtrGRTTVLITHRLQGLEAVDEV 1126
Cdd:TIGR00958 606 GYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRA--SRTVLLIAHRLSTVERADQI 683
|
250 260
....*....|....*....|....*...
gi 2351811981 1127 VVLEAGRVVQRGPYADLTAEEGPLRRML 1154
Cdd:TIGR00958 684 LVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
332-545 |
7.69e-36 |
|
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: 135.30 E-value: 7.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 332 RLELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATlAPERWRERIA 411
Cdd:COG4133 2 MLEAENLSCRRGER--LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 412 WVPQRPYLFAG-TIAENVRLARPDADDGAVAAALRDAgaydfVAELpdGAQTLLGEDGAGLSAGQRQRLALARAFLADRP 490
Cdd:COG4133 79 YLGHADGLKPElTVRENLRFWAALYGLRADREAIDEA-----LEAV--GLAGLADLPVRQLSAGQKRRVALARLLLSPAP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2351811981 491 LLLLDEPTASLDGETEAGIVEAVRR-LAQGRTVLLVVHRPALLPlADRVVRLEPGA 545
Cdd:COG4133 152 LWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTHQPLELA-AARVLDLGDFK 206
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
921-1148 |
7.72e-36 |
|
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: 136.53 E-value: 7.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDAcVLEGDTVRGFVGL 1000
Cdd:COG4555 2 IEVENLSKKYGKVP--ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDV-RKEPREARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDAHIFDS-SIRENLRLART--GATDEELRAALDR-ARLLDwaeaLPAGLDTLVGEhgarLSGGQRQRLALARAILAD 1076
Cdd:COG4555 79 LPDERGLYDRlTVRENIRYFAElyGLFDEELKKRIEElIELLG----LEEFLDRRVGE----LSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 1077 FPVLVLDEPAEHLDLATADALTADLLA-ATRGRTTVLITHRLQGLEAV-DEVVVLEAGRVVQRGPYADLTAEEG 1148
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRAlKKEGKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
332-561 |
9.59e-36 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 136.76 E-value: 9.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 332 RLELEGVTVRHEGRGEPS--LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPerwreR 409
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVtaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP-----D 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 410 IAWVPQRPYLFA-GTIAENVRLArpdaddgavaaaLRDAGAYDfvAELPDGAQTLLGE---DGAG------LSAGQRQRL 479
Cdd:COG1116 82 RGVVFQEPALLPwLTVLDNVALG------------LELRGVPK--AERRERARELLELvglAGFEdayphqLSGGMRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 480 ALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRL--AQGRTVLLVVH--RPALLpLADRVVRLEPG-ATLRPEKPeg 554
Cdd:COG1116 148 AIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHdvDEAVF-LADRVVVLSARpGRIVEEID-- 224
|
....*..
gi 2351811981 555 sVAVPRP 561
Cdd:COG1116 225 -VDLPRP 230
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
894-1153 |
9.81e-36 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 144.08 E-value: 9.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 894 RVYEVLDAPPPVREPDSPagTPASPFPLEVRGLSARYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLD 973
Cdd:PRK10789 289 RIRAMLAEAPVVKDGSEP--VPEGRGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFD 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 974 AREGTYRIGGVDACVLEGDTVRGFVGLCAQDAHIFDSSIRENLRLARTGATDEELRAALDRARLLDWAEALPAGLDTLVG 1053
Cdd:PRK10789 367 VSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVG 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1054 EHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTADLLAATRGRTTVLITHRLQGLEAVDEVVVLEAGR 1133
Cdd:PRK10789 447 ERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGH 526
|
250 260
....*....|....*....|
gi 2351811981 1134 VVQRGPYADLTAEEGPLRRM 1153
Cdd:PRK10789 527 IAQRGNHDQLAQQSGWYRDM 546
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
7-546 |
1.15e-35 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 144.48 E-value: 1.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 7 RLLRYARATRFFLAAVVALGVVGAALVIAQAMLVA---DVVV--GGFEDGLtVSGLRTPLILLAAVAlgrALVSWLTELA 81
Cdd:PRK10790 13 RLLAYGSPWRKPLGLAVLMLWVAAAAEVSGPLLISyfiDNMVakGNLPLGL-VAGLAAAYVGLQLLA---AGLHYAQSLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 82 AYRASAAVKSELRGRLLDRAAELGPGLLSDRRTGSLVTLATRGVDALDDYFARYLPQLGLAVVVPVAVLARIVTEDWVSA 161
Cdd:PRK10790 89 FNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 162 AIIVVTLPLIPLFMILIGWATQSRMDRQWRLLSRLSGHFLDVVAGLPTLKVFGRAKAQAESIRAITSQYRRATLRTLRia 241
Cdd:PRK10790 169 LVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLR-- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 242 fLSSFALELLATLSVALVAVtiGMRLVHGELDLYTGLVVLILAPEAYL-----PIRQVGAQYHAAAEGLSAAEEIFSVLE 316
Cdd:PRK10790 247 -LDGFLLRPLLSLFSALILC--GLLMLFGFSASGTIEVGVLYAFISYLgrlnePLIELTTQQSMLQQAVVAGERVFELMD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 317 TEPRRGGTADVP-ESLRLELEGVTVRHeGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGG 395
Cdd:PRK10790 324 GPRQQYGNDDRPlQSGRIDIDNVSFAY-RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 396 VDLATLAPERWRERIAWVPQRPYLFAGTIAENVRLARPDADDGAVAAaLRDAGAYDFVAELPDGAQTLLGEDGAGLSAGQ 475
Cdd:PRK10790 403 RPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQA-LETVQLAELARSLPDGLYTPLGEQGNNLSVGQ 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 476 RQRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQGRTVLLVVHRPALLPLADRVVRLEPGAT 546
Cdd:PRK10790 482 KQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQA 552
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
158-545 |
1.62e-35 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 145.25 E-value: 1.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 158 WVSAAIIVVTLPLIPLFMILigwatQSRMDRQWRLLS--------RLSGHFLDVVAGLPTLKVFGRAKAQAesiraitSQ 229
Cdd:TIGR00958 298 WLSPRLTMVTLINLPLVFLA-----EKVFGKRYQLLSeelqeavaKANQVAEEALSGMRTVRSFAAEEGEA-------SR 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 230 YRRATLRTLRIAFLSSFAL-------ELLATLSVALVAVTIGMRLVHGELDlyTGLVVLILAPEAYL--PIRQVGAQYHA 300
Cdd:TIGR00958 366 FKEALEETLQLNKRKALAYagylwttSVLGMLIQVLVLYYGGQLVLTGKVS--SGNLVSFLLYQEQLgeAVRVLSYVYSG 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 301 AAEGLSAAEEIFSVLETEPR---RGGTADVPESLRLELEGVTVRHEGRGE-PSLDHASLVVDEGETVALVGPSGVGKSTL 376
Cdd:TIGR00958 444 MMQAVGASEKVFEYLDRKPNiplTGTLAPLNLEGLIEFQDVSFSYPNRPDvPVLKGLTFTLHPGEVVALVGPSGSGKSTV 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 377 LDVVLGFTAPDEGRVRVGGVDLATLAPERWRERIAWVPQRPYLFAGTIAENVRLARPDADDGAVAAALRDAGAYDFVAEL 456
Cdd:TIGR00958 524 AALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEF 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 457 PDGAQTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAvrRLAQGRTVLLVVHRPALLPLAD 536
Cdd:TIGR00958 604 PNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVLLIAHRLSTVERAD 681
|
....*....
gi 2351811981 537 RVVRLEPGA 545
Cdd:TIGR00958 682 QILVLKKGS 690
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
921-1155 |
2.14e-35 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 134.81 E-value: 2.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGaeRDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDAcVLEGDTVRGFVGL 1000
Cdd:COG1131 1 IEVRGLTKRYGD--KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV-ARDPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDAHIFDS-SIRENLRLART--GATDEELRAALDRarLLDWAEaLPAGLDTLVGEhgarLSGGQRQRLALARAILADF 1077
Cdd:COG1131 78 VPQEPALYPDlTVRENLRFFARlyGLPRKEARERIDE--LLELFG-LTDAADRKVGT----LSGGMKQRLGLALALLHDP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1078 PVLVLDEPAEHLDLATADALTADLLA-ATRGRTTVLITHRLQGLEAV-DEVVVLEAGRVVQRGPYADLtaeegpLRRMLE 1155
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWELLRElAAEGKTVLLSTHYLEEAERLcDRVAIIDKGRIVADGTPDEL------KARLLE 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
350-499 |
2.64e-35 |
|
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: 131.62 E-value: 2.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 350 LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERIAWVPQRPYLFAG-TIAENV 428
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2351811981 429 RLARPDADDGAVAaalRDAGAYDFVAEL--PDGAQTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTA 499
Cdd:pfam00005 81 RLGLLLKGLSKRE---KDARAEEALEKLglGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
921-1138 |
3.33e-35 |
|
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: 133.31 E-value: 3.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGL 1000
Cdd:cd03369 7 IEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDAHIFDSSIRENLRLARTgATDEELRAALDrarlldwaealpagldtlVGEHGARLSGGQRQRLALARAILADFPVL 1080
Cdd:cd03369 87 IPQDPTLFSGTIRSNLDPFDE-YSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 1081 VLDEPAEHLDLATaDALTADLLAATRGRTTVL-ITHRLQGLEAVDEVVVLEAGRVVQRG 1138
Cdd:cd03369 148 VLDEATASIDYAT-DALIQKTIREEFTNSTILtIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
332-544 |
9.84e-35 |
|
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: 133.63 E-value: 9.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 332 RLELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERIA 411
Cdd:COG1120 1 MLEAENLSVGYGGR--PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 412 WVPQRPYL-FAGTIAENVRLAR-PDADDGAVAAA---------LRDAGAYDFvaelpdgAQTLLGEdgagLSAGQRQRLA 480
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGRyPHLGLFGRPSAedreaveeaLERTGLEHL-------ADRPVDE----LSGGERQRVL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2351811981 481 LARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLA--QGRTVLLVVHRPAL-LPLADRVVRLEPG 544
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLAreRGRTVVMVLHDLNLaARYADRLVLLKDG 214
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
2-544 |
1.12e-34 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 142.40 E-value: 1.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 2 KPIDPR-LLRYA-RATRFFLAAVVALGVVGAALV----IAQAMLVADVVVGGFEDGLTVSGLrtpliLLAAVALGRALVS 75
Cdd:TIGR03797 119 KALGLRdLLRFAlRGARRDLLAILAMGLLGTLLGmlvpIATGILIGTAIPDADRSLLVQIAL-----ALLAAAVGAAAFQ 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 76 WLTELAAYRASAAVKSELRGRLLDRAAELGPGLLSDRRTGSLVTLATrGVDALDDYFARYLPQLGLAVVVPVAVLARIVT 155
Cdd:TIGR03797 194 LAQSLAVLRLETRMDASLQAAVWDRLLRLPVSFFRQYSTGDLASRAM-GISQIRRILSGSTLTTLLSGIFALLNLGLMFY 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 156 EDWVSAAIIVVTLPLIPLFMILIGWATQSRMDRQWRLLSRLSGHFLDVVAGLPTLKVfgrakAQAESiRAIT------SQ 229
Cdd:TIGR03797 273 YSWKLALVAVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGISKLRV-----AGAEN-RAFArwaklfSR 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 230 YRRATLRTLRIA-FLSSFALELLATLSVALVAVTIGMrLVHGELDLYTGLVVLILAPEAYLPIRQVGAQYHAAAEGLSAA 308
Cdd:TIGR03797 347 QRKLELSAQRIEnLLTVFNAVLPVLTSAALFAAAISL-LGGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLISILAVIPLW 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 309 EEIFSVLETEPRRGGTADVPESL--RLELEGVTVRHEGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAP 386
Cdd:TIGR03797 426 ERAKPILEALPEVDEAKTDPGKLsgAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETP 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 387 DEGRVRVGGVDLATLAPERWRERIAWVPQRPYLFAGTIAENVRLARPDADDGAVAAaLRDAGAYDFVAELPDGAQTLLGE 466
Cdd:TIGR03797 506 ESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEA-ARMAGLAEDIRAMPMGMHTVISE 584
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 467 DGAGLSAGQRQRLALARAfLADRP-LLLLDEPTASLDGETEAGIVEAVRRLAQGRTVllVVHRPALLPLADRVVRLEPG 544
Cdd:TIGR03797 585 GGGTLSGGQRQRLLIARA-LVRKPrILLFDEATSALDNRTQAIVSESLERLKVTRIV--IAHRLSTIRNADRIYVLDAG 660
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
333-547 |
1.29e-34 |
|
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: 133.06 E-value: 1.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLaPERWRERIAW 412
Cdd:COG4555 2 IEVENLSKKYGKV--PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKE-PREARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 413 VPQRPYLFAG-TIAENVRLARPDADDGAVAAALRdagAYDFV--AELPDGAQTLLGEdgagLSAGQRQRLALARAFLADR 489
Cdd:COG4555 79 LPDERGLYDRlTVRENIRYFAELYGLFDEELKKR---IEELIelLGLEEFLDRRVGE----LSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 490 PLLLLDEPTASLDGETEAGIVEAVRRLA-QGRTVLLVVHRPALLP-LADRVVRLEPGATL 547
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEaLCDRVVILHKGKVV 211
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
938-1134 |
1.75e-34 |
|
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: 131.82 E-value: 1.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 938 LDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGLCAQDAHIFDSSIRENLR 1017
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFARSLQDNIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1018 LARTGATDEELRAALDRARLLDWAEALPAGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADAL 1097
Cdd:cd03248 110 YGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQV 189
|
170 180 190
....*....|....*....|....*....|....*..
gi 2351811981 1098 TADLLAATRGRTTVLITHRLQGLEAVDEVVVLEAGRV 1134
Cdd:cd03248 190 QQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
922-1133 |
2.17e-34 |
|
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: 131.05 E-value: 2.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 922 EVRGLSARYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGLC 1001
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1002 AQDAH--IFDSSIRE-------NLRLARtgatdEElraalDRARLLDWAEALpaGLDTLVGEHGARLSGGQRQRLALARA 1072
Cdd:cd03225 81 FQNPDdqFFGPTVEEevafgleNLGLPE-----EE-----IEERVEEALELV--GLEGLRDRSPFTLSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 1073 ILADFPVLVLDEPAEHLDLATADALTAdLLA--ATRGRTTVLITHRLQGLEAV-DEVVVLEAGR 1133
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLE-LLKklKAEGKTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
333-559 |
2.34e-34 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 131.44 E-value: 2.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRGEP--SLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPerwreRI 410
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP-----DR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 411 AWVPQRPYLFA-GTIAENVRLArpdaddgAVAAALRDAGAYDFVAELPDgaqtLLGEDGAG------LSAGQRQRLALAR 483
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALG-------LELQGVPKAEARERAEELLE----LVGLSGFEnayphqLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 484 AFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQ--GRTVLLVVH--RPALLpLADRVVRLEPgatlRPEKPEGSVAVP 559
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHdiDEAVF-LADRVVVLSA----RPGRIVAEVEVD 219
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
170-1148 |
2.74e-34 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 143.58 E-value: 2.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 170 LIPLFMILIgwatqSRMDR------QWRllSRLSGHFLDVVAGLPTLKVFGRAKAQAESIRAIT----SQYRRATLrtlr 239
Cdd:PLN03232 453 LIPLQTLIV-----RKMRKltkeglQWT--DKRVGIINEILASMDTVKCYAWEKSFESRIQGIRneelSWFRKAQL---- 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 240 iafLSSFALELLATLSVALVAVTIGM-RLVHGELD---LYTGLVV--LILAPEAYLPirQVGAQYHAAAEGLSAAEEIFS 313
Cdd:PLN03232 522 ---LSAFNSFILNSIPVVVTLVSFGVfVLLGGDLTparAFTSLSLfaVLRSPLNMLP--NLLSQVVNANVSLQRIEELLL 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 314 VLE-----TEPRRGGTADVpeSLRlelEGVTVRHEGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDE 388
Cdd:PLN03232 597 SEErilaqNPPLQPGAPAI--SIK---NGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE 671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 389 grvrVGGVDLatlaperwRERIAWVPQRPYLFAGTIAENVRLARPDADDGAVAAALRDAGAYDfVAELPDGAQTLLGEDG 468
Cdd:PLN03232 672 ----TSSVVI--------RGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHD-LDLLPGRDLTEIGERG 738
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 469 AGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEAGIVEA-VRRLAQGRTVLLVVHRPALLPLADRVVRLEPGATl 547
Cdd:PLN03232 739 VNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDScMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMI- 817
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 548 rpeKPEGSVA--------VPRPADASAAGRAAVPEPETLRDTAARPGQVLARV--REAAGAQRGQLALALLLGSLALGSA 617
Cdd:PLN03232 818 ---KEEGTFAelsksgslFKKLMENAGKMDATQEVNTNDENILKLGPTVTIDVseRNLGSTKQGKRGRSVLVKQEERETG 894
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 618 V--------------GLMAV-----------------SGWLI-----SRASEQPPVLYLMV---------AVTATRAFGL 652
Cdd:PLN03232 895 IiswnvlmrynkavgGLWVVmillvcylttevlrvssSTWLSiwtdqSTPKSYSPGFYIVVyallgfgqvAVTFTNSFWL 974
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 653 GRAVFRYAERLvsHDAVLKMLaeLRVAVYrgLERIAPAGLRRSRrgdlLSRLVADVDA----LQDYWLR--WLLPAgTAV 726
Cdd:PLN03232 975 ISSSLHAAKRL--HDAMLNSI--LRAPML--FFHTNPTGRVINR----FSKDIGDIDRnvanLMNMFMNqlWQLLS-TFA 1043
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 727 VVGAATAGFIGWLLPaagivlatgLLLAGAGVPLVSGACSRHAERQLAPARADLATRITDLLGGTAeltvagALPARKAR 806
Cdd:PLN03232 1044 LIGTVSTISLWAIMP---------LLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLS------SIRAYKAY 1108
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 807 TREAdgvltriaaraatatALGGGLIALIGGLTVVATALVALPAVHDGRLAGVELAVVVLTPL---------AAFEAVTG 877
Cdd:PLN03232 1109 DRMA---------------KINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVlrngnaenqAGFASTMG 1173
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 878 LPLAVQ----------YRQRVK-----RSAERVYEVLDAP---PPVREPDSPAGTPASPFPLEVRGLSARYAGAERDALD 939
Cdd:PLN03232 1174 LLLSYTlnittllsgvLRQASKaenslNSVERVGNYIDLPseaTAIIENNRPVSGWPSRGSIKFEDVHLRYRPGLPPVLH 1253
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 940 SVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGLCAQDAHIFDSSIRENLRlA 1019
Cdd:PLN03232 1254 GLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNID-P 1332
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1020 RTGATDEELRAALDRARLLDWAEALPAGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTA 1099
Cdd:PLN03232 1333 FSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQR 1412
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*....
gi 2351811981 1100 DLLAATRGRTTVLITHRLQGLEAVDEVVVLEAGRVVQRGPYADLTAEEG 1148
Cdd:PLN03232 1413 TIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDT 1461
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
333-544 |
5.13e-34 |
|
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: 131.46 E-value: 5.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHE--GRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERI 410
Cdd:COG1124 2 LEVRNLSVSYGqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 411 AWVPQRPYL-------FAGTIAENVRLARPDADDGAVAAALRDAGaydfvaeLPDGaqtLLGEDGAGLSAGQRQRLALAR 483
Cdd:COG1124 82 QMVFQDPYAslhprhtVDRILAEPLRIHGLPDREERIAELLEQVG-------LPPS---FLDRYPHQLSGGQRQRVAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 484 AFLADRPLLLLDEPTASLDGETEAGIVEAVRRL--AQGRTVLLVVHRPALLP-LADRVVRLEPG 544
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSVQAEILNLLKDLreERGLTYLFVSHDLAVVAhLCDRVAVMQNG 215
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
328-544 |
1.09e-33 |
|
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: 129.07 E-value: 1.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 328 PESLRLELEGVTVRHEGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWR 407
Cdd:cd03369 2 PEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 408 ERIAWVPQRPYLFAGTIAENVrlarpdaddgavaaalrdaGAYDFVAELPDGAQTLLGEDGAGLSAGQRQRLALARAFLA 487
Cdd:cd03369 82 SSLTIIPQDPTLFSGTIRSNL-------------------DPFDEYSDEEIYGALRVSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2351811981 488 DRPLLLLDEPTASLDGETEAGIVEAVRRLAQGRTVLLVVHRPALLPLADRVVRLEPG 544
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAG 199
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
910-1147 |
1.53e-33 |
|
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: 130.41 E-value: 1.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 910 SPAGTPASPFPLEVRGLSARYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVL 989
Cdd:cd03288 9 SNSGLVGLGGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 990 EGDTVRGFVGLCAQDAHIFDSSIRENLRLARTgATDEELRAALDRARLLDWAEALPAGLDTLVGEHGARLSGGQRQRLAL 1069
Cdd:cd03288 89 PLHTLRSRLSIILQDPILFSGSIRFNLDPECK-CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2351811981 1070 ARAILADFPVLVLDEPAEHLDLATADALTADLLAATRGRTTVLITHRLQGLEAVDEVVVLEAGRVVQRGPYADLTAEE 1147
Cdd:cd03288 168 ARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQE 245
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
333-544 |
1.75e-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: 129.37 E-value: 1.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGrGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERIAW 412
Cdd:COG1122 1 IELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 413 VPQRP--YLFAGTIAENV-----RLARPDADdgavaaalRDAGAYDFVAELpdGAQTLLGEDGAGLSAGQRQRLALARAf 485
Cdd:COG1122 80 VFQNPddQLFAPTVEEDVafgpeNLGLPREE--------IRERVEEALELV--GLEHLADRPPHELSGGQKQRVAIAGV- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2351811981 486 LADRP-LLLLDEPTASLDGETEAGIVEAVRRL-AQGRTVLLVVHRPALL-PLADRVVRLEPG 544
Cdd:COG1122 149 LAMEPeVLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVaELADRVIVLDDG 210
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
921-1143 |
1.40e-32 |
|
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: 127.23 E-value: 1.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAERD--ALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFV 998
Cdd:COG1124 2 LEVRNLSVSYGQGGRRvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 999 GLCAQDA-------HIFDSSIRENLRLARTGATDEELRAALDRArlldwaeALPAG-LDTLVGEhgarLSGGQRQRLALA 1070
Cdd:COG1124 82 QMVFQDPyaslhprHTVDRILAEPLRIHGLPDREERIAELLEQV-------GLPPSfLDRYPHQ----LSGGQRQRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2351811981 1071 RAILADFPVLVLDEPAEHLDLATAdALTADLLA---ATRGRTTVLITHRLQGLEAV-DEVVVLEAGRVVQRGPYADL 1143
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQ-AEILNLLKdlrEERGLTYLFVSHDLAVVAHLcDRVAVMQNGRIVEELTVADL 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
333-544 |
1.67e-32 |
|
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: 124.61 E-value: 1.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPER--WRERI 410
Cdd:cd03229 1 LELKNVSKRYGQK--TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 411 AWVPQRPYLFAG-TIAENVRLarpdaddgavaaalrdagaydfvaelpdgaqtllgedgaGLSAGQRQRLALARAFLADR 489
Cdd:cd03229 79 GMVFQDFALFPHlTVLENIAL---------------------------------------GLSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2351811981 490 PLLLLDEPTASLDGETEAGIVEAVRRLAQ--GRTVLLVVHRPA-LLPLADRVVRLEPG 544
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLQAqlGITVVLVTHDLDeAARLADRVVVLRDG 177
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
333-544 |
1.68e-32 |
|
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: 126.65 E-value: 1.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGrGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERIAW 412
Cdd:cd03295 1 IEFENVTKRYGG-GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 413 VPQRPYLFAG-TIAENVRLArPDADDGAVAAalRDAGAYDFVAELPDGAQTLLGEDGAGLSAGQRQRLALARAFLADRPL 491
Cdd:cd03295 80 VIQQIGLFPHmTVEENIALV-PKLLKWPKEK--IRERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2351811981 492 LLLDEPTASLDGETEAGIVEAVRRLAQ--GRTVLLVVH--RPALLpLADRVVRLEPG 544
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHdiDEAFR-LADRIAIMKNG 212
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
891-1153 |
2.34e-32 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 134.08 E-value: 2.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 891 SAERVYEVLDAPppvREPDSPAGTPASPFPLEVRGLSARYaGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLR 970
Cdd:PRK10790 314 AGERVFELMDGP---RQQYGNDDRPLQSGRIDIDNVSFAY-RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMG 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 971 FLDAREGTYRIGGVDACVLEGDTVRGFVGLCAQDAHIFDSSIRENLRLARTgATDEELRAALDRARLLDWAEALPAGLDT 1050
Cdd:PRK10790 390 YYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRD-ISEEQVWQALETVQLAELARSLPDGLYT 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1051 LVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALtADLLAATRGRTT-VLITHRLQGLEAVDEVVVL 1129
Cdd:PRK10790 469 PLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAI-QQALAAVREHTTlVVIAHRLSTIVEADTILVL 547
|
250 260
....*....|....*....|....
gi 2351811981 1130 EAGRVVQRGPYADLTAEEGPLRRM 1153
Cdd:PRK10790 548 HRGQAVEQGTHQQLLAAQGRYWQM 571
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
921-1135 |
2.82e-32 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 125.54 E-value: 2.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYA--GAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGD---TVR 995
Cdd:COG1136 5 LELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERelaRLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 996 ----GFVGlcaQDAHIFDS-SIREN----LRLARTGATDEELRA--ALDRARLLDWAEALPagldtlvgehgARLSGGQR 1064
Cdd:COG1136 85 rrhiGFVF---QFFNLLPElTALENvalpLLLAGVSRKERRERAreLLERVGLGDRLDHRP-----------SQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2351811981 1065 QRLALARAILADFPVLVLDEPAEHLDLATADALTADL--LAATRGRTTVLITHRLQGLEAVDEVVVLEAGRVV 1135
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLreLNRELGTTIVMVTHDPELAARADRVIRLRDGRIV 223
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
333-547 |
3.28e-32 |
|
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: 125.63 E-value: 3.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHegRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAP-ERWRERIA 411
Cdd:cd03219 1 LEVRGLTKRF--GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPhEIARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 412 WVPQRPYLFAG-TIAENVRLARpdadDGAVAAALRDAGAYDFVAELPDGAQTLLGEDG---------AGLSAGQRQRLAL 481
Cdd:cd03219 79 RTFQIPRLFPElTVLENVMVAA----QARTGSGLLLARARREEREARERAEELLERVGladladrpaGELSYGQQRRLEI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 482 ARAFLADRPLLLLDEPTASL-DGETEAgIVEAVRRLAQ-GRTVLLVVHR-PALLPLADRVVRLEPGATL 547
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGLnPEETEE-LAELIRELRErGITVLLVEHDmDVVMSLADRVTVLDQGRVI 222
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
333-544 |
3.80e-32 |
|
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: 124.94 E-value: 3.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHegRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPErwRERIAW 412
Cdd:cd03259 1 LELKGLSKTY--GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 413 VPQRPYLFAG-TIAENVRLARPDADDGAVAAALRdAGAYDFVAELPDgaqtLLGEDGAGLSAGQRQRLALARAFLADRPL 491
Cdd:cd03259 77 VFQDYALFPHlTVAENIAFGLKLRGVPKAEIRAR-VRELLELVGLEG----LLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2351811981 492 LLLDEPTASLDGETEAGIVEAVRRL--AQGRTVLLVVHRPA-LLPLADRVVRLEPG 544
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELqrELGITTIYVTHDQEeALALADRIAVMNEG 207
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
333-544 |
4.34e-32 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 125.25 E-value: 4.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRgepsLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPErwreriaw 412
Cdd:COG3840 2 LRLDDLTYRYGDF----PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 413 vpQRPY--------LFAG-TIAENVRLA-RP-----DADDGAVAAALRDAGAYDFVAELPdgaqtllgedgAGLSAGQRQ 477
Cdd:COG3840 70 --ERPVsmlfqennLFPHlTVAQNIGLGlRPglkltAEQRAQVEQALERVGLAGLLDRLP-----------GQLSGGQRQ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 478 RLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLA--QGRTVLLVVHRPA-LLPLADRVVRLEPG 544
Cdd:COG3840 137 RVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCreRGLTVLMVTHDPEdAARIADRVLLVADG 206
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
921-1139 |
4.44e-32 |
|
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: 124.99 E-value: 4.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAgaERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDA-----REGTYRIGGVDACVLEGD--T 993
Cdd:cd03260 1 IELRDLNVYYG--DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDvlE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 994 VRGFVGLCAQDAHIFDSSIRENLRLA-------RTGATDEELRAALDRARLldWAEALpaglDTLvgeHGARLSGGQRQR 1066
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKAAL--WDEVK----DRL---HALGLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2351811981 1067 LALARAILADFPVLVLDEPAEHLD-LATADalTADLLAATRGRTTVLI-THRL-QGLEAVDEVVVLEAGRVVQRGP 1139
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDpISTAK--IEELIAELKKEYTIVIvTHNMqQAARVADRTAFLLNGRLVEFGP 223
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
333-541 |
5.24e-32 |
|
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: 124.93 E-value: 5.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRGEPS--LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPER---WR 407
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkiRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 408 ERIAWVPQRPYL-------FAGTIAENVRLARPdaddGAVAAALRDAGAYDFVaELPDGAQtLLGEDGAGLSAGQRQRLA 480
Cdd:cd03257 82 KEIQMVFQDPMSslnprmtIGEQIAEPLRIHGK----LSKKEARKEAVLLLLV-GVGLPEE-VLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 481 LARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQ--GRTVLLVVHRPALL-PLADRVVRL 541
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVaKIADRVAVM 219
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
921-1134 |
6.59e-32 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 123.77 E-value: 6.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGaeRDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGL 1000
Cdd:COG4619 1 LELEGLSFRVGG--KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDAHIFDSSIRENLRLARTGATDEelraaLDRARLLDWAEAL---PAGLDTLVgehgARLSGGQRQRLALARAILADF 1077
Cdd:COG4619 79 VPQEPALWGGTVRDNLPFPFQLRERK-----FDRERALELLERLglpPDILDKPV----ERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 1078 PVLVLDEPAEHLDLATADA---LTADLLAAtRGRTTVLITHRLQGLEAV-DEVVVLEAGRV 1134
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRveeLLREYLAE-EGRAVLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
334-544 |
1.21e-31 |
|
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: 122.16 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 334 ELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERIAWV 413
Cdd:cd03214 1 EVENLSVGYGGR--TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 414 PQrpylfagtiaenvrlarpdaddgavaaALRDAGAYDFvaelpdgAQTLLGEdgagLSAGQRQRLALARAFLADRPLLL 493
Cdd:cd03214 79 PQ---------------------------ALELLGLAHL-------ADRPFNE----LSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 494 LDEPTASLDGETEAGIVEAVRRLAQ--GRTVLLVVHRPAL-LPLADRVVRLEPG 544
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARerGKTVVMVLHDLNLaARYADRVILLKDG 174
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
333-578 |
1.29e-31 |
|
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: 130.79 E-value: 1.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPD---EGRVRVGGVDLATLAPERWRER 409
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 410 IAWVPQRPY--LFAGTIAENVRLARPDADDGAVAAALRDAGAYDFVaelpdGAQTLLGEDGAGLSAGQRQRLALARAFLA 487
Cdd:COG1123 85 IGMVFQDPMtqLNPVTVGDQIAEALENLGLSRAEARARVLELLEAV-----GLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 488 DRPLLLLDEPTASLDGETEAGIVEAVRRLAQ--GRTVLLVVHRPAL-LPLADRVVRLEPGATLR-------PEKPEGSVA 557
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVvAEIADRVVVMDDGRIVEdgppeeiLAAPQALAA 239
|
250 260
....*....|....*....|.
gi 2351811981 558 VPRPADASAAGRAAVPEPETL 578
Cdd:COG1123 240 VPRLGAARGRAAPAAAAAEPL 260
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
921-1146 |
2.15e-31 |
|
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: 124.00 E-value: 2.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGaeRDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGL 1000
Cdd:COG1120 2 LEAENLSVGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDAHI-FDSSIRENLRLART---------GATDEEL-RAALDRARLLDWAealpaglDTLVGEhgarLSGGQRQRLAL 1069
Cdd:COG1120 80 VPQEPPApFGLTVRELVALGRYphlglfgrpSAEDREAvEEALERTGLEHLA-------DRPVDE----LSGGERQRVLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1070 ARAILADFPVLVLDEPAEHLDLA----TADALTAdlLAATRGRTTVLITHRL-QGLEAVDEVVVLEAGRVVQRGPYAD-L 1143
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAhqleVLELLRR--LARERGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGPPEEvL 226
|
...
gi 2351811981 1144 TAE 1146
Cdd:COG1120 227 TPE 229
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
921-1137 |
2.56e-31 |
|
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: 122.58 E-value: 2.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARY--AGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDtvRGFV 998
Cdd:cd03293 1 LEVRNVSKTYggGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD--RGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 999 glcAQDAHIFD-SSIREN----LRLARTGATD--EELRAALDRARLLDWAEALPAgldtlvgehgaRLSGGQRQRLALAR 1071
Cdd:cd03293 79 ---FQQDALLPwLTVLDNvalgLELQGVPKAEarERAEELLELVGLSGFENAYPH-----------QLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2351811981 1072 AILADFPVLVLDEPAEHLDLATADALTADLLA--ATRGRTTVLITHRLQglEAV---DEVVVLEA--GRVVQR 1137
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDID--EAVflaDRVVVLSArpGRIVAE 215
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
921-1135 |
2.56e-31 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 124.05 E-value: 2.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARY--AGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGvdACVLEGDTVRGFV 998
Cdd:COG1116 8 LELRGVSKRFptGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG--KPVTGPGPDRGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 999 glcAQDAHIFD-SSIRENLRLA------RTGATDEELRAALDRARLLDWAEALPagldtlvgehgARLSGGQRQRLALAR 1071
Cdd:COG1116 86 ---FQEPALLPwLTVLDNVALGlelrgvPKAERRERARELLELVGLAGFEDAYP-----------HQLSGGMRQRVAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 1072 AILADFPVLVLDEPAEHLDLATADALTADLLA--ATRGRTTVLITHRLQglEAV---DEVVVLEA--GRVV 1135
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHDVD--EAVflaDRVVVLSArpGRIV 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
899-1154 |
2.80e-31 |
|
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: 130.02 E-value: 2.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 899 LDAPPPVREPDSPAGTPAspfpLEVRGLSARYAGAERD---ALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAR 975
Cdd:COG1123 243 LGAARGRAAPAAAAAEPL----LEVRNLSKRYPVRGKGgvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPT 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 976 EGTYRIGGVDACVLEGDTVRGF---VGLCAQDAH--------IFDsSIRENLRLARTG---ATDEELRAALDRARL-LDW 1040
Cdd:COG1123 319 SGSILFDGKDLTKLSRRSLRELrrrVQMVFQDPYsslnprmtVGD-IIAEPLRLHGLLsraERRERVAELLERVGLpPDL 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1041 AEALPagldtlvgehgARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALtADLLA---ATRGRTTVLITHRL 1117
Cdd:COG1123 398 ADRYP-----------HELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQI-LNLLRdlqRELGLTYLFISHDL 465
|
250 260 270
....*....|....*....|....*....|....*....
gi 2351811981 1118 QGLEAV-DEVVVLEAGRVVQRGPYAD-LTAEEGPLRRML 1154
Cdd:COG1123 466 AVVRYIaDRVAVMYDGRIVEDGPTEEvFANPQHPYTRAL 504
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
921-1138 |
6.02e-31 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 121.84 E-value: 6.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYA--GAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDacVLEGDTV---- 994
Cdd:cd03257 2 LEVKNLSVSFPtgGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKD--LLKLSRRlrki 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 995 -RGFVGLCAQDAH--------IFDsSIRENLRLARTGATDEELRAALDRARLL-----DWAEALPagldtlvgehgARLS 1060
Cdd:cd03257 80 rRKEIQMVFQDPMsslnprmtIGE-QIAEPLRIHGKLSKKEARKEAVLLLLVGvglpeEVLNRYP-----------HELS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1061 GGQRQRLALARAILADFPVLVLDEPAEHLDLATAdALTADLL---AATRGRTTVLITHRLQGLEAV-DEVVVLEAGRVVQ 1136
Cdd:cd03257 148 GGQRQRVAIARALALNPKLLIADEPTSALDVSVQ-AQILDLLkklQEELGLTLLFITHDLGVVAKIaDRVAVMYAGKIVE 226
|
..
gi 2351811981 1137 RG 1138
Cdd:cd03257 227 EG 228
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
921-1138 |
6.08e-31 |
|
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: 121.47 E-value: 6.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAerDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDacVLEGDTVRGFVGL 1000
Cdd:cd03259 1 LELKGLSKTYGSV--RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRD--VTGVPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDAHIFDS-SIREN----LRLARTGATDEELRA--ALDRARLLDWAEALPAGLdtlvgehgarlSGGQRQRLALARAI 1073
Cdd:cd03259 77 VFQDYALFPHlTVAENiafgLKLRGVPKAEIRARVreLLELVGLEGLLNRYPHEL-----------SGGQQQRVALARAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1074 LADFPVLVLDEPAEHLDLATADALTADL--LAATRGRTTVLITHRLQglEAV---DEVVVLEAGRVVQRG 1138
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELkeLQRELGITTIYVTHDQE--EALalaDRIAVMNEGRIVQVG 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
333-544 |
8.07e-31 |
|
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: 121.39 E-value: 8.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHegRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAP-ERWRERIA 411
Cdd:cd03224 1 LEVENLNAGY--GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPhERARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 412 WVPQRPYLFAG-TIAENVRLARPDADDGAVAAALrdAGAYDFVAELpdgaQTLLGEDGAGLSAGQRQRLALARAFLADRP 490
Cdd:cd03224 79 YVPEGRRIFPElTVEENLLLGAYARRRAKRKARL--ERVYELFPRL----KERRKQLAGTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2351811981 491 LLLLDEPTASLDGETEAGIVEAVRRL-AQGRTVLLVVHR-PALLPLADRVVRLEPG 544
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEAIRELrDEGVTILLVEQNaRFALEIADRAYVLERG 208
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
350-1143 |
1.28e-30 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 131.44 E-value: 1.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 350 LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVrvggvdlatlaperWRER-IAWVPQRPYLFAGTIAENV 428
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV--------------WAERsIAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 429 rLARPDADDGAVAAALRDAGAYDFVAELPDGAQTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEAG 508
Cdd:PTZ00243 742 -LFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGER 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 509 IVEAV--RRLAqGRTVLLVVHRPALLPLADRVVRLEPG-----------------ATLR------PEKPEGSV-----AV 558
Cdd:PTZ00243 821 VVEECflGALA-GKTRVLATHQVHVVPRADYVVALGDGrvefsgssadfmrtslyATLAaelkenKDSKEGDAdaevaEV 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 559 PRPADASAAGRAAVPEPETL--------RDTAArpGQVLARVREAAGAQRGQLALALLLGSLALGSAVGLMAVSGW--LI 628
Cdd:PTZ00243 900 DAAPGGAVDHEPPVAKQEGNaeggdgaaLDAAA--GRLMTREEKASGSVPWSTYVAYLRFCGGLHAAGFVLATFAVteLV 977
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 629 SRASEqppvlyLMVAVTATRAFGLGRAVFRYAERLV--------------SHDAVLKMLAELRVAVYRGLERIAPAGLRR 694
Cdd:PTZ00243 978 TVSSG------VWLSMWSTRSFKLSAATYLYVYLGIvllgtfsvplrfflSYEAMRRGSRNMHRDLLRSVSRGTMSFFDT 1051
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 695 SRRGDLLSRLVADVDALQD-------YWLRWLLPAGTAVVVGAATAGFIGWLLPAAGIVLATglllagagVPLVSGACSR 767
Cdd:PTZ00243 1052 TPLGRILNRFSRDIDILDNtlpmsylYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYR--------LMQFYNSANR 1123
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 768 HAERQLAPARADLATRITDLLGGTAELTVAGalparKART--READGVLTRIAARAATATALGGGLIALIGGLTVVATAL 845
Cdd:PTZ00243 1124 EIRRIKSVAKSPVFTLLEEALQGSATITAYG-----KAHLvmQEALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTV 1198
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 846 VALPAVHDG--RLAGVELAVVVLTPLAAFEAVTGLPLAVQYRQRVK---RSAERVYEVLDAPPP---------------- 904
Cdd:PTZ00243 1199 IALIGVIGTmlRATSQEIGLVSLSLTMAMQTTATLNWLVRQVATVEadmNSVERLLYYTDEVPHedmpeldeevdalerr 1278
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 905 -----------VREPDSPAGT---PASPFPLEVRGLSARYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLR 970
Cdd:PTZ00243 1279 tgmaadvtgtvVIEPASPTSAaphPVQAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMR 1358
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 971 FLDAREGTYRIGGVDACVLEGDTVRGFVGLCAQDAHIFDSSIRENLRlARTGATDEELRAALDRARLLDWAEALPAGLDT 1050
Cdd:PTZ00243 1359 MVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVD-PFLEASSAEVWAALELVGLRERVASESEGIDS 1437
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1051 LVGEHGARLSGGQRQRLALARAILA-DFPVLVLDEPAEHLDLATADALTADLLAATRGRTTVLITHRLQGLEAVDEVVVL 1129
Cdd:PTZ00243 1438 RVLEGGSNYSVGQRQLMCMARALLKkGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVM 1517
|
890
....*....|....
gi 2351811981 1130 EAGRVVQRGPYADL 1143
Cdd:PTZ00243 1518 DHGAVAEMGSPREL 1531
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
334-546 |
1.34e-30 |
|
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: 120.05 E-value: 1.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 334 ELEGVTVRHEGRGEpSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLAtlAPERwRERIAWV 413
Cdd:cd03226 1 RIENISFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK--AKER-RKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 414 PQRP--YLFAGTIAENVRLARPDADDGAVAAA--LRDAGAYDFVAELPdgaqtllgedgAGLSAGQRQRLALARAFLADR 489
Cdd:cd03226 77 MQDVdyQLFTDSVREELLLGLKELDAGNEQAEtvLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGK 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 490 PLLLLDEPTASLDGETEAGIVEAVRRLA-QGRTVLLVVHRPALLPL-ADRVVRLEPGAT 546
Cdd:cd03226 146 DLLIFDEPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLAKvCDRVLLLANGAI 204
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
921-1171 |
1.77e-30 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 127.33 E-value: 1.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAR---EGTYRIGGVDACVLEGDTVRGF 997
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 998 VGLCAQD--AHIFDSSIRENLR--LARTGATDEELraaldRARLLDWAEALpaGLDTLVGEHGARLSGGQRQRLALARAI 1073
Cdd:COG1123 85 IGMVFQDpmTQLNPVTVGDQIAeaLENLGLSRAEA-----RARVLELLEAV--GLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1074 LADFPVLVLDEPAEHLDLATADALTADL--LAATRGRTTVLITHRLQG-LEAVDEVVVLEAGRVVQRGPYADL------T 1144
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLreLQRERGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEIlaapqaL 237
|
250 260
....*....|....*....|....*..
gi 2351811981 1145 AEEGPLRRMLERERETEGVAEEALGVR 1171
Cdd:COG1123 238 AAVPRLGAARGRAAPAAAAAEPLLEVR 264
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
938-1085 |
2.54e-30 |
|
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: 117.36 E-value: 2.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 938 LDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGLCAQDAHIF-DSSIRENL 1016
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 1017 RLartGATDEELRAALDRARLLDWAEALPAG--LDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEP 1085
Cdd:pfam00005 81 RL---GLLLKGLSKREKDARAEEALEKLGLGdlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
333-539 |
4.43e-30 |
|
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: 120.14 E-value: 4.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAP-ERWRERIA 411
Cdd:COG0411 5 LEVRGLTKRFGGL--VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPhRIARLGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 412 WVPQRPYLFAG-TIAENVRLARPDAD-DGAVAAALRDAGAYDFVAELPDGAQTLL---------GEDGAGLSAGQRQRLA 480
Cdd:COG0411 83 RTFQNPRLFPElTVLENVLVAAHARLgRGLLAALLRLPRARREEREARERAEELLervgladraDEPAGNLSYGQQRRLE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 481 LARAfLADRP-LLLLDEPTASL-DGETEAgIVEAVRRLA--QGRTVLLVVHR-PALLPLADRVV 539
Cdd:COG0411 163 IARA-LATEPkLLLLDEPAAGLnPEETEE-LAELIRRLRdeRGITILLIEHDmDLVMGLADRIV 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
333-539 |
6.90e-30 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 122.51 E-value: 6.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERwReRIAW 412
Cdd:COG3842 6 LELENVSKRYGDV--TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK-R-NVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 413 VPQR----PYLfagTIAENV----RLARpdaddgavaaaLRDAGAYDFVAELPDgaqtLLGEDGAG------LSAGQRQR 478
Cdd:COG3842 82 VFQDyalfPHL---TVAENVafglRMRG-----------VPKAEIRARVAELLE----LVGLEGLAdryphqLSGGQQQR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2351811981 479 LALARAfLADRP-LLLLDEPTASLDGETEAGIVEAVRRL--AQGRTVLLVVHRP--ALLpLADRVV 539
Cdd:COG3842 144 VALARA-LAPEPrVLLLDEPLSALDAKLREEMREELRRLqrELGITFIYVTHDQeeALA-LADRIA 207
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
921-1134 |
7.92e-30 |
|
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: 116.73 E-value: 7.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGaeRDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDAcVLEGDTVRGFVGL 1000
Cdd:cd03230 1 IEVRNLSKRYGK--KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI-KKEPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDAHIFDS-SIRENLRLartgatdeelraaldrarlldwaealpagldtlvgehgarlSGGQRQRLALARAILADFPV 1079
Cdd:cd03230 78 LPEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2351811981 1080 LVLDEPAEHLDLATADALTaDLLA--ATRGRTTVLITHRLQGLEAV-DEVVVLEAGRV 1134
Cdd:cd03230 117 LILDEPTSGLDPESRREFW-ELLRelKKEGKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
296-555 |
7.93e-30 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 126.08 E-value: 7.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 296 AQYHAAAEGLSAAEEIFSVLETEPRRGGTADVPESLRLELEGVTVRHeGRGEPSLDHASLVVDEGETVALVGPSGVGKST 375
Cdd:COG4178 326 AEWRATVDRLAGFEEALEAADALPEAASRIETSEDGALALEDLTLRT-PDGRPLLEDLSLSLKPGERLLITGPSGSGKST 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 376 LLDVVLGFTAPDEGRVRVggvdlatlaPERwrERIAWVPQRPYLFAGTIAENvrLARPDADDGAVAAALRDAGAydfVAE 455
Cdd:COG4178 405 LLRAIAGLWPYGSGRIAR---------PAG--ARVLFLPQRPYLPLGTLREA--LLYPATAEAFSDAELREALE---AVG 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 456 LPDGAQTLLGED--GAGLSAGQRQRLALARAFLAdRP-LLLLDEPTASLDGETEAGIVEAVRRLAQGRTVLLVVHRPALL 532
Cdd:COG4178 469 LGHLAERLDEEAdwDQVLSLGEQQRLAFARLLLH-KPdWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLA 547
|
250 260
....*....|....*....|...
gi 2351811981 533 PLADRVVRLEPGATLRPEKPEGS 555
Cdd:COG4178 548 AFHDRVLELTGDGSWQLLPAEAP 570
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
921-1152 |
3.15e-29 |
|
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: 117.22 E-value: 3.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGaeRDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVL---EGDTVRGF 997
Cdd:cd03261 1 IELRGLTKSFGG--RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLseaELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 998 VGLCAQDAHIFDS-SIREN--LRLARTGATDEELRaaldRARLLDWAEA--LPAGLDTLVGEhgarLSGGQRQRLALARA 1072
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENvaFPLREHTRLSEEEI----REIVLEKLEAvgLRGAEDLYPAE----LSGGMKKRVALARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1073 ILADFPVLVLDEPAEHLDLATADALtADL---LAATRGRTTVLITHRLQ-GLEAVDEVVVLEAGRVVQRGPYADLTAEEG 1148
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIASGVI-DDLirsLKKELGLTSIMVTHDLDtAFAIADRIAVLYDGKIVAEGTPEELRASDD 229
|
....
gi 2351811981 1149 PLRR 1152
Cdd:cd03261 230 PLVR 233
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
333-550 |
3.55e-29 |
|
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: 116.76 E-value: 3.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRGEP--SLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPE---RWR 407
Cdd:COG4181 9 IELRGLTKTVGTGAGEltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDaraRLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 408 -ERIAWVPQRPYLFAG-TIAENVRLArpdaddgavaaaLRDAGAydfvAELPDGAQTLLGEDG---------AGLSAGQR 476
Cdd:COG4181 89 aRHVGFVFQSFQLLPTlTALENVMLP------------LELAGR----RDARARARALLERVGlghrldhypAQLSGGEQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2351811981 477 QRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRL--AQGRTVLLVVHRPALLPLADRVVRLEPGATLRPE 550
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnrERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDT 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
301-539 |
4.55e-29 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 123.09 E-value: 4.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 301 AAEGLSAAEEIFSVLETEPRRGGTADVPESLR--LELEGVTVRHEGRGEPS---LDHASLVVDEGETVALVGPSGVGKST 375
Cdd:COG1123 227 PEEILAAPQALAAVPRLGAARGRAAPAAAAAEplLEVRNLSKRYPVRGKGGvraVDDVSLTLRRGETLGLVGESGSGKST 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 376 LLDVVLGFTAPDEGRVRVGGVDLATLAPERWRE---RIAWVPQRPY--LF-----AGTIAENVRLARpdaddgavaaALR 445
Cdd:COG1123 307 LARLLLGLLRPTSGSILFDGKDLTKLSRRSLRElrrRVQMVFQDPYssLNprmtvGDIIAEPLRLHG----------LLS 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 446 DAGAYDFVAELPDgaQTLLGEDGAG-----LSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQ-- 518
Cdd:COG1123 377 RAERRERVAELLE--RVGLPPDLADrypheLSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRel 454
|
250 260
....*....|....*....|..
gi 2351811981 519 GRTVLLVVHRPAL-LPLADRVV 539
Cdd:COG1123 455 GLTYLFISHDLAVvRYIADRVA 476
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
921-1146 |
5.59e-29 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 115.99 E-value: 5.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDT-VRGFVG 999
Cdd:cd03224 1 LEVENLNAGYGKSQ--ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1000 LCAQDAHIFDS-SIRENLRLARTGATDEELRAALDRArlldwAEALPAgLDTLVGEHGARLSGGQRQRLALARAILADFP 1078
Cdd:cd03224 79 YVPEGRRIFPElTVEENLLLGAYARRRAKRKARLERV-----YELFPR-LKERRKQLAGTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1079 VLVLDEPAEHLDLATADALTADLLA-ATRGRTTVLITHRLQG-LEAVDEVVVLEAGRVVQRGPYADLTAE 1146
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEAIRElRDEGVTILLVEQNARFaLEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
881-1142 |
6.85e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 122.48 E-value: 6.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 881 AVQYRQRVKRsAERVyEVLDAPPPVREP--DSPAGTPASPFPLEVRGLSARYAGaeRDALDSVDLRLTAGRRIAVVGPSG 958
Cdd:COG0488 276 AKQAQSRIKA-LEKL-EREEPPRRDKTVeiRFPPPERLGKKVLELEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPNG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 959 SGKTTLAQVLLRFLDAREGTYRIGgvdacvlegDTVRgfVGLCAQDAHIFDS--SIRENLRLARTGATDEELRAALdrAR 1036
Cdd:COG0488 352 AGKSTLLKLLAGELEPDSGTVKLG---------ETVK--IGYFDQHQEELDPdkTVLDELRDGAPGGTEQEVRGYL--GR 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1037 LLDWAEALpaglDTLVGehgaRLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTaDLLAATRGrTTVLITH- 1115
Cdd:COG0488 419 FLFSGDDA----FKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALE-EALDDFPG-TVLLVSHd 488
|
250 260 270
....*....|....*....|....*....|
gi 2351811981 1116 R--LQGLeaVDEVVVLEAGRVVQR-GPYAD 1142
Cdd:COG0488 489 RyfLDRV--ATRILEFEDGGVREYpGGYDD 516
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
921-1146 |
7.19e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 116.34 E-value: 7.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGaeRDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDAcvlegDTVRGFVGL 1000
Cdd:COG1121 7 IELENLTVSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-----RRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDAHI---FDSSIRENLRLARTG---------ATDEEL-RAALDRARLLDWAealpaglDTLVGEhgarLSGGQRQRL 1067
Cdd:COG1121 80 VPQRAEVdwdFPITVRDVVLMGRYGrrglfrrpsRADREAvDEALERVGLEDLA-------DRPIGE----LSGGQQQRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1068 ALARAILADFPVLVLDEPAEHLDLATADALtADLLA--ATRGRTTVLITHRLQGL-EAVDEVVVLeAGRVVQRGPYAD-L 1143
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEAL-YELLRelRREGKTILVVTHDLGAVrEYFDRVLLL-NRGLVAHGPPEEvL 226
|
...
gi 2351811981 1144 TAE 1146
Cdd:COG1121 227 TPE 229
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
352-544 |
8.59e-29 |
|
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: 115.28 E-value: 8.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 352 HASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPErwRERIAWVPQRPYLFAG-TIAENVRL 430
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAHlTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 431 ARP------DADDGAVAAALRDAGAYDFVAELPDgaqtllgedgaGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGE 504
Cdd:cd03298 94 GLSpglkltAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2351811981 505 TEAGIVEAVRRL--AQGRTVLLVVHRPA-LLPLADRVVRLEPG 544
Cdd:cd03298 163 LRAEMLDLVLDLhaETKMTVLMVTHQPEdAKRLAQRVVFLDNG 205
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
333-544 |
9.68e-29 |
|
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: 115.68 E-value: 9.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPE---RWRER 409
Cdd:cd03261 1 IELRGLTKSFGGR--TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 410 IAWVPQRPYLFAG-TIAENVrlARPdaddgavaaaLRDAGAY------DFVAE------LPDGAQTLLGEdgagLSAGQR 476
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENV--AFP----------LREHTRLseeeirEIVLEkleavgLRGAEDLYPAE----LSGGMK 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 477 QRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRL--AQGRTVLLVVHR-PALLPLADRVVRLEPG 544
Cdd:cd03261 143 KRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDlDTAFAIADRIAVLYDG 213
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
346-561 |
1.11e-28 |
|
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: 115.51 E-value: 1.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 346 GEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPErwRERIAWVPQRPYLFAG-TI 424
Cdd:cd03299 11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPHmTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 425 AENVRLArpdaDDGAVAAALRDAGAYDFVAELPdGAQTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGE 504
Cdd:cd03299 89 YKNIAYG----LKKRKVDKKEIERKVLEIAEML-GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 505 TEAGIVEAVRRLAQ--GRTVLLVVHRPA-LLPLADRVVRLEPGATLRPEKPEGSVAVPRP 561
Cdd:cd03299 164 TKEKLREELKKIRKefGVTVLHVTHDFEeAWALADKVAIMLNGKLIQVGKPEEVFKKPKN 223
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
921-1145 |
1.19e-28 |
|
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: 115.46 E-value: 1.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGaeRDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDT---VRGF 997
Cdd:COG1127 6 IEVRNLTKSFGD--RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyeLRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 998 VGLCAQDAHIFDS-SIRENLRLA---RTGATDEELRA----ALDRARLLDWAEALPagldtlvgehgARLSGGQRQRLAL 1069
Cdd:COG1127 84 IGMLFQGGALFDSlTVFENVAFPlreHTDLSEAEIRElvleKLELVGLPGAADKMP-----------SELSGGMRKRVAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1070 ARAILADFPVLVLDEPAEHLDLATADALtADL---LAATRGRTTVLITHRLQGLEAV-DEVVVLEAGRVVQRGPYADLTA 1145
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDPITSAVI-DELireLRDELGLTSVVVTHDLDSAFAIaDRVAVLADGKIIAEGTPEELLA 231
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
348-545 |
1.55e-28 |
|
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: 114.84 E-value: 1.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 348 PSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRV----GGVDLATLAPERW----RERIAWVPQrpyl 419
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDLAQASPREIlalrRRTIGYVSQ---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 420 FAGTI----AENVrLARPdaddgavaaaLRDAGAYDFVAElpDGAQTLLGEDG----------AGLSAGQRQRLALARAF 485
Cdd:COG4778 101 FLRVIprvsALDV-VAEP----------LLERGVDREEAR--ARARELLARLNlperlwdlppATFSGGEQQRVNIARGF 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2351811981 486 LADRPLLLLDEPTASLDGETEAGIVEAVRRL-AQGRTVLLVVHRPALL-PLADRVVRLEPGA 545
Cdd:COG4778 168 IADPPLLLLDEPTASLDAANRAVVVELIEEAkARGTAIIGIFHDEEVReAVADRVVDVTPFS 229
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
907-1166 |
3.86e-28 |
|
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: 123.52 E-value: 3.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 907 EPDSPAGTPASP---FPLEVRGLSARYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYrigg 983
Cdd:TIGR00957 620 EPDSIERRTIKPgegNSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV---- 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 984 vdacvlegdTVRGFVGLCAQDAHIFDSSIRENLRLARTgATDEELRAALDRARLLDWAEALPAGLDTLVGEHGARLSGGQ 1063
Cdd:TIGR00957 696 ---------HMKGSVAYVPQQAWIQNDSLRENILFGKA-LNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQ 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1064 RQRLALARAILADFPVLVLDEPAEHLDLATADALTADLLAAT---RGRTTVLITHRLQGLEAVDEVVVLEAGRVVQRGPY 1140
Cdd:TIGR00957 766 KQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEgvlKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSY 845
|
250 260
....*....|....*....|....*...
gi 2351811981 1141 ADLTAEEGPLRRMLER--ERETEGVAEE 1166
Cdd:TIGR00957 846 QELLQRDGAFAEFLRTyaPDEQQGHLED 873
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
921-1147 |
4.96e-28 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 114.00 E-value: 4.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAERdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGF--- 997
Cdd:COG3638 3 LELRNLSKRYPGGTP-ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 998 VGLCAQDAHIFD-SSIRENL---RLARTGA--------TDEELRAA---LDRARLLDWAEAlPAGldtlvgehgaRLSGG 1062
Cdd:COG3638 82 IGMIFQQFNLVPrLSVLTNVlagRLGRTSTwrsllglfPPEDRERAleaLERVGLADKAYQ-RAD----------QLSGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1063 QRQRLALARAILADfPVLVL-DEPAEHLDLATADALTADL--LAATRGRTTVLITHRLQ-GLEAVDEVVVLEAGRVVQRG 1138
Cdd:COG3638 151 QQQRVAIARALVQE-PKLILaDEPVASLDPKTARQVMDLLrrIAREDGITVVVNLHQVDlARRYADRIIGLRDGRVVFDG 229
|
....*....
gi 2351811981 1139 PYADLTAEE 1147
Cdd:COG3638 230 PPAELTDAV 238
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
921-1128 |
5.09e-28 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 112.57 E-value: 5.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAgaERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDAcVLEGDTVRGFVGL 1000
Cdd:COG4133 3 LEAENLSCRRG--ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI-RDAREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDAHIFDS-SIRENLRLAR----TGATDEELRAALDRARLLDwAEALPAGldtlvgehgaRLSGGQRQRLALARAILA 1075
Cdd:COG4133 80 LGHADGLKPElTVRENLRFWAalygLRADREAIDEALEAVGLAG-LADLPVR----------QLSAGQKRRVALARLLLS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2351811981 1076 DFPVLVLDEPAEHLDLATADALtADLLAA--TRGRTTVLITHRLQGLEAVDEVVV 1128
Cdd:COG4133 149 PAPLWLLDEPFTALDAAGVALL-AELIAAhlARGGAVLLTTHQPLELAAARVLDL 202
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
333-544 |
9.85e-28 |
|
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: 112.77 E-value: 9.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAP-ERWRERIA 411
Cdd:COG0410 4 LEVENLHAGYGGI--HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPhRIARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 412 WVPQRPYLFAG-TIAENVRLARPDADDGAVAAALRDAgAYDFVAELpdgaQTLLGEDGAGLSAGQRQRLALARAFLADRP 490
Cdd:COG0410 82 YVPEGRRIFPSlTVEENLLLGAYARRDRAEVRADLER-VYELFPRL----KERRRQRAGTLSGGEQQMLAIGRALMSRPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2351811981 491 LLLLDEPTASL------DgeteagIVEAVRRL-AQGRTVLLVVHR-PALLPLADRVVRLEPG 544
Cdd:COG0410 157 LLLLDEPSLGLapliveE------IFEIIRRLnREGVTILLVEQNaRFALEIADRAYVLERG 212
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
333-551 |
1.04e-27 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 112.45 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHeGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPER---WRER 409
Cdd:COG2884 2 IRFENVSKRY-PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 410 IAWVPQRPYLFAG-TIAENVRLA------RPDADDGAVAAALRDAGAYDFVAELPDGaqtllgedgagLSAGQRQRLALA 482
Cdd:COG2884 81 IGVVFQDFRLLPDrTVYENVALPlrvtgkSRKEIRRRVREVLDLVGLSDKAKALPHE-----------LSGGEQQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 483 RAFLADRPLLLLDEPTASLDGETEAGIVEAVRRL-AQGRTVLLVVHRPALLPLAD-RVVRLEPGATLRPEK 551
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLELVDRMPkRVLELEDGRLVRDEA 220
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
330-547 |
1.05e-27 |
|
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: 111.49 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 330 SLRLELEGVTVRHEGRGEPS----LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAP--DEGRVRVGGVDLAtlaP 403
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPSKSgkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLD---K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 404 ERWRERIAWVPQRPYLFAG-TIAENVrlarpdaddgavaaalrdagayDFVAELpdgaqtllgedgAGLSAGQRQRLALA 482
Cdd:cd03213 78 RSFRKIIGYVPQDDILHPTlTVRETL----------------------MFAAKL------------RGLSGGERKRVSIA 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2351811981 483 RAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQ-GRTVLLVVHRPA--LLPLADRVVRLEPGATL 547
Cdd:cd03213 124 LELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADtGRTIICSIHQPSseIFELFDKLLLLSQGRVI 191
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
333-539 |
1.12e-27 |
|
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: 112.77 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPE---RWRER 409
Cdd:COG1127 6 IEVRNLTKSFGDR--VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 410 IAWVPQRPYLFAG-TIAENVRLArpdaddgavaaaLR------DAGAYDFVAE------LPDGAQTLLGEdgagLSAGQR 476
Cdd:COG1127 84 IGMLFQGGALFDSlTVFENVAFP------------LRehtdlsEAEIRELVLEklelvgLPGAADKMPSE----LSGGMR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2351811981 477 QRLALARAfLADRP-LLLLDEPTASLDGETEAGIVEAVRRL--AQGRTVLLVVHR-PALLPLADRVV 539
Cdd:COG1127 148 KRVALARA-LALDPeILLYDEPTAGLDPITSAVIDELIRELrdELGLTSVVVTHDlDSAFAIADRVA 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
922-1133 |
1.22e-27 |
|
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: 110.03 E-value: 1.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 922 EVRGLSARYAGaeRDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGLC 1001
Cdd:cd00267 1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1002 AQdahifdssirenlrlartgatdeelraaldrarlldwaealpagldtlvgehgarLSGGQRQRLALARAILADFPVLV 1081
Cdd:cd00267 79 PQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 1082 LDEPAEHLDLATADALTADLLA-ATRGRTTVLITHRLQGLE-AVDEVVVLEAGR 1133
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAElAADRVIVLKDGK 157
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
921-1134 |
1.73e-27 |
|
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: 111.43 E-value: 1.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARY--AGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVD-ACVLEGDTVR-- 995
Cdd:cd03255 1 IELKNLSKTYggGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDiSKLSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 996 ----GFVglcAQDAHIFDS-SIREN----LRLARTGATDEELRA--ALDRARLLDWAEALPagldtlvgehgARLSGGQR 1064
Cdd:cd03255 81 rrhiGFV---FQSFNLLPDlTALENvelpLLLAGVPKKERRERAeeLLERVGLGDRLNHYP-----------SELSGGQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2351811981 1065 QRLALARAILADFPVLVLDEPAEHLDLATADALTADL--LAATRGRTTVLITHRLQGLEAVDEVVVLEAGRV 1134
Cdd:cd03255 147 QRVAIARALANDPKIILADEPTGNLDSETGKEVMELLreLNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
333-544 |
1.98e-27 |
|
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: 112.28 E-value: 1.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHeGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPE---RWRER 409
Cdd:cd03256 1 IEVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalrQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 410 IAWVPQRPYLFAG-TIAENV---RLAR-----------PDADDGAVAAALRDAGaydfvaeLPDGAQTLLGEdgagLSAG 474
Cdd:cd03256 80 IGMIFQQFNLIERlSVLENVlsgRLGRrstwrslfglfPKEEKQRALAALERVG-------LLDKAYQRADQ----LSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2351811981 475 QRQRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQ--GRTVLLVVHRPAL-LPLADRVVRLEPG 544
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDLaREYADRIVGLKDG 221
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
922-1135 |
5.55e-27 |
|
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: 109.65 E-value: 5.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 922 EVRGLSARYaGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEgdtVRGFVGLC 1001
Cdd:cd03226 1 RIENISFSY-KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---RRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1002 AQDA--HIFDSSIRENLRLA--RTGATDEELRAALDRARLLDWAEALPAGLdtlvgehgarlSGGQRQRLALARAILADF 1077
Cdd:cd03226 77 MQDVdyQLFTDSVREELLLGlkELDAGNEQAETVLKDLDLYALKERHPLSL-----------SGGQKQRLAIAAALLSGK 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 1078 PVLVLDEPAEHLDLATADALtADLL--AATRGRTTVLITHRLQGL-EAVDEVVVLEAGRVV 1135
Cdd:cd03226 146 DLLIFDEPTSGLDYKNMERV-GELIreLAAQGKAVIVITHDYEFLaKVCDRVLLLANGAIV 205
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
921-1135 |
6.01e-27 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 110.14 E-value: 6.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGaERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGF--- 997
Cdd:COG2884 2 IRFENVSKRYPG-GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 998 VGLCAQDAH-IFDSSIRENLRLA-R-TGATDEELR----AALDRARLLDWAEALPAgldtlvgehgaRLSGGQRQRLALA 1070
Cdd:COG2884 81 IGVVFQDFRlLPDRTVYENVALPlRvTGKSRKEIRrrvrEVLDLVGLSDKAKALPH-----------ELSGGEQQRVAIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2351811981 1071 RAILADFPVLVLDEPAEHLDLATADALTADLLAATRGRTTVLI-THRLQGLEAVDE-VVVLEAGRVV 1135
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIaTHDLELVDRMPKrVLELEDGRLV 216
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
350-544 |
8.98e-27 |
|
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: 109.16 E-value: 8.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 350 LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLaTLAPERW---RERIAWVPQRPYLFAG-TIA 425
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNInelRQKVGMVFQQFNLFPHlTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 426 ENVRLA------RPDADDgavaaalrDAGAYDFVAE--LPDGAQTLLGEdgagLSAGQRQRLALARAFLADRPLLLLDEP 497
Cdd:cd03262 95 ENITLApikvkgMSKAEA--------EERALELLEKvgLADKADAYPAQ----LSGGQQQRVAIARALAMNPKVMLFDEP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2351811981 498 TASLDGETEAGIVEAVRRLAQ-GRTVLLVVHRPAL-LPLADRVVRLEPG 544
Cdd:cd03262 163 TSALDPELVGEVLDVMKDLAEeGMTMVVVTHEMGFaREVADRVIFMDDG 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
921-1133 |
9.15e-27 |
|
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: 108.04 E-value: 9.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAgaERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTV--RGFV 998
Cdd:cd03229 1 LELKNVSKRYG--QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPplRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 999 GLCAQDAHIFDS-SIRENLRLArtgatdeelraaldrarlldwaealpagldtlvgehgarLSGGQRQRLALARAILADF 1077
Cdd:cd03229 79 GMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 1078 PVLVLDEPAEHLDLATADALTADL--LAATRGRTTVLITHRLQGLEAV-DEVVVLEAGR 1133
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLksLQAQLGITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
333-543 |
1.08e-26 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 109.11 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPD---EGRVRVGGVDLATLAPErwRER 409
Cdd:COG4136 2 LSLENLTITLGGR--PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAE--QRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 410 IAWVPQRPYLFAG-TIAENVRLARPDADDGAVaaalRDAGAYDFVAELpdGAQTLLGEDGAGLSAGQRQRLALARAFLAD 488
Cdd:COG4136 78 IGILFQDDLLFPHlSVGENLAFALPPTIGRAQ----RRARVEQALEEA--GLAGFADRDPATLSGGQRARVALLRALLAE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2351811981 489 RPLLLLDEPTASLDGETEAGIVEAVRRLAQGRT--VLLVVHRPALLPLADRVVRLEP 543
Cdd:COG4136 152 PRALLLDEPFSKLDAALRAQFREFVFEQIRQRGipALLVTHDEEDAPAAGRVLDLGN 208
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
333-545 |
1.65e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 109.03 E-value: 1.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERIAW 412
Cdd:PRK10247 8 LQLQNVGYLAGDA--KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 413 VPQRPYLFAGTIAENVRLARPDADDGAVAAALRDAGAYdFvaELPDgaqTLLGEDGAGLSAGQRQRLALAR--AFLADrp 490
Cdd:PRK10247 86 CAQTPTLFGDTVYDNLIFPWQIRNQQPDPAIFLDDLER-F--ALPD---TILTKNIAELSGGEKQRISLIRnlQFMPK-- 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2351811981 491 LLLLDEPTASLDGETEAGIVEAVRRLA--QGRTVLLVVHRPALLPLADRVVRLEPGA 545
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRYVreQNIAVLWVTHDKDEINHADKVITLQPHA 214
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
921-1154 |
1.74e-26 |
|
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: 109.30 E-value: 1.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDacvLEG----DTVRG 996
Cdd:COG0410 4 LEVENLHAGYGGIH--VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGED---ITGlpphRIARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 997 FVGLCAQDAHIFDS-SIRENLRL-ARTGATDEELRAALDRArlldwAEALPAgLDTLVGEHGARLSGGQRQRLALARAIL 1074
Cdd:COG0410 79 GIGYVPEGRRIFPSlTVEENLLLgAYARRDRAEVRADLERV-----YELFPR-LKERRRQRAGTLSGGEQQMLAIGRALM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1075 ADFPVLVLDEPAEHLdlatADALTADLLAA-----TRGRTTVLITHRL-QGLEAVDEVVVLEAGRVVQRGPYADLTAEEG 1148
Cdd:COG0410 153 SRPKLLLLDEPSLGL----APLIVEEIFEIirrlnREGVTILLVEQNArFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
....*.
gi 2351811981 1149 PLRRML 1154
Cdd:COG0410 229 VREAYL 234
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
19-311 |
1.80e-26 |
|
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: 110.72 E-value: 1.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 19 LAAVVALGVVGAALVIAQAMLVADVVVGGFEDGLtVSGLRTPLILLAAVALGRALVSWLTELAAYRASAAVKSELRGRLL 98
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGD-LSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 99 DRAAELGPGLLSDRRTGSLVTLATRGVDALDDYFARYLPQLGLAVVVPVAVLARIVTEDWVSAAIIVVTLPliplFMILI 178
Cdd:cd07346 80 RHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLP----LYVLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 179 GWATQSRMDRQWR----LLSRLSGHFLDVVAGLPTLKVFGRAKAQAESIRAITSQYRRATLRTLRIAFLSSFALELLATL 254
Cdd:cd07346 156 LRYFRRRIRKASRevreSLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTAL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2351811981 255 SVALVAVTIGMRLVHGELDLYTGLVVLILAPEAYLPIRQVGAQYHAAAEGLSAAEEI 311
Cdd:cd07346 236 GTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
350-539 |
2.81e-26 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 108.54 E-value: 2.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 350 LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLAtlAPE----RWRERIAWVPQRPYLFAG-TI 424
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT--DSKkdinKLRRKVGMVFQQFNLFPHlTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 425 AENVRLA------RPDaddgavaaalrdagaydfvAELPDGAQTLLGEDG---------AGLSAGQRQRLALARAfLADR 489
Cdd:COG1126 95 LENVTLApikvkkMSK-------------------AEAEERAMELLERVGladkadaypAQLSGGQQQRVAIARA-LAME 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2351811981 490 P-LLLLDEPTASLDGETEAGIVEAVRRLAQ-GRTVLLVVH-----RPAllplADRVV 539
Cdd:COG1126 155 PkVMLFDEPTSALDPELVGEVLDVMRDLAKeGMTMVVVTHemgfaREV----ADRVV 207
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
921-1146 |
3.14e-26 |
|
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: 108.81 E-value: 3.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAeRDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGD---TVRGF 997
Cdd:cd03256 1 IEVENLSKTYPNG-KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalrQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 998 VGLCAQDAHIFD-SSIRENL---RLARTGAtdeeLRAALDRARLLDWAEALPA----GLDTLVGEHGARLSGGQRQRLAL 1069
Cdd:cd03256 80 IGMIFQQFNLIErLSVLENVlsgRLGRRST----WRSLFGLFPKEEKQRALAAlervGLLDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1070 ARAiLADFPVLVL-DEPAEHLDLATADALTADL--LAATRGRTTVLITHRLQ-GLEAVDEVVVLEAGRVVQRGPYADLTA 1145
Cdd:cd03256 156 ARA-LMQQPKLILaDEPVASLDPASSRQVMDLLkrINREEGITVIVSLHQVDlAREYADRIVGLKDGRIVFDGPPAELTD 234
|
.
gi 2351811981 1146 E 1146
Cdd:cd03256 235 E 235
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
354-544 |
3.33e-26 |
|
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: 107.64 E-value: 3.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 354 SLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPerWRERIAWVPQRPYLFAG-TIAENVRLA- 431
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAP--YQRPVSMLFQENNLFAHlTVRQNIGLGl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 432 RP-----DADDGAVAAALRDAGAYDFVAELPDGaqtllgedgagLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETE 506
Cdd:TIGR01277 96 HPglklnAEQQEKVVDAAQQVGIADYLDRLPEQ-----------LSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2351811981 507 AGIVEAVRRLA--QGRTVLLVVHRPA-LLPLADRVVRLEPG 544
Cdd:TIGR01277 165 EEMLALVKQLCseRQRTLLMVTHHLSdARAIASQIAVVSQG 205
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
921-1146 |
3.37e-26 |
|
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: 108.63 E-value: 3.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGaeRDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGT------YRIGGVDacVLEgdtV 994
Cdd:COG1119 4 LELRNVTVRRGG--KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrlfgERRGGED--VWE---L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 995 RGFVGLCAQDAHifdSSIRENLR---LARTGATD-----EELRAAlDRARLLDWAEALpaGLDTLVGEHGARLSGGQRQR 1066
Cdd:COG1119 77 RKRIGLVSPALQ---LRFPRDETvldVVLSGFFDsiglyREPTDE-QRERARELLELL--GLAHLADRPFGTLSQGEQRR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1067 LALARAILADFPVLVLDEPAEHLDLATADALTA--DLLAATRGRTTVLITHRLQ-GLEAVDEVVVLEAGRVVQRGPYAD- 1142
Cdd:COG1119 151 VLIARALVKDPELLILDEPTAGLDLGARELLLAllDKLAAEGAPTLVLVTHHVEeIPPGITHVLLLKDGRVVAAGPKEEv 230
|
....
gi 2351811981 1143 LTAE 1146
Cdd:COG1119 231 LTSE 234
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
922-1138 |
4.35e-26 |
|
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: 106.37 E-value: 4.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 922 EVRGLSARYAGaeRDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDacvlegdtvrgfvglc 1001
Cdd:cd03214 1 EVENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKD---------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1002 aqdahIFDSSIREnlrLARTGATdeeLRAALDRARLLDWAEAlpaGLDTLvgehgarlSGGQRQRLALARAILADFPVLV 1081
Cdd:cd03214 63 -----LASLSPKE---LARKIAY---VPQALELLGLAHLADR---PFNEL--------SGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1082 LDEPAEHLDLATADALTADL--LAATRGRTTVLITHRL-QGLEAVDEVVVLEAGRVVQRG 1138
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLrrLARERGKTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
921-1139 |
4.43e-26 |
|
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: 109.08 E-value: 4.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGA---ERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDacvLEGDT---- 993
Cdd:TIGR04521 1 IKLKNVSYIYQPGtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRD---ITAKKkkkl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 994 --VRGFVGLCAQ--DAHIFDSSIRE-------NLrlartGATDEElraALDRARlldwaEALPA-GLD-TLVGEHGARLS 1060
Cdd:TIGR04521 78 kdLRKKVGLVFQfpEHQLFEETVYKdiafgpkNL-----GLSEEE---AEERVK-----EALELvGLDeEYLERSPFELS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1061 GGQRQRLALArAILADFP-VLVLDEPAEHLDLATADALTADL--LAATRGRTTVLITHRLQG-LEAVDEVVVLEAGRVVQ 1136
Cdd:TIGR04521 145 GGQMRRVAIA-GVLAMEPeVLILDEPTAGLDPKGRKEILDLFkrLHKEKGLTVILVTHSMEDvAEYADRVIVMHKGKIVL 223
|
...
gi 2351811981 1137 RGP 1139
Cdd:TIGR04521 224 DGT 226
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
921-1143 |
4.56e-26 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 111.01 E-value: 4.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGaeRDALDSVDLRLTAGRRIAVVGPSGSGKTTLaqvlLR----FLDAREGTYRIGGVDAC----VLEgd 992
Cdd:COG1118 3 IEVRNISKRFGS--FTLLDDVSLEIASGELVALLGPSGSGKTTL----LRiiagLETPDSGRIVLNGRDLFtnlpPRE-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 993 tvRGfVGLCAQDAHIF-DSSIRENLRLartGATDEELRAALDRARLLDWAEALpaGLDTLVGEHGARLSGGQRQRLALAR 1071
Cdd:COG1118 75 --RR-VGFVFQHYALFpHMTVAENIAF---GLRVRPPSKAEIRARVEELLELV--QLEGLADRYPSQLSGGQRQRVALAR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2351811981 1072 AILADFPVLVLDEPAEHLDLATADALTA---DLLAATrGRTTVLITH-RLQGLEAVDEVVVLEAGRVVQRGPYADL 1143
Cdd:COG1118 147 ALAVEPEVLLLDEPFGALDAKVRKELRRwlrRLHDEL-GGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
333-544 |
5.58e-26 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 110.55 E-value: 5.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRGEP--SLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRE-- 408
Cdd:COG1135 2 IELENLSKTFPTKGGPvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 409 -RIAWVPQRPYLFAG-TIAENVrlARPdaddgavaaaLRDAGA-----YDFVAELPDgaqtLLG-EDGAG-----LSAGQ 475
Cdd:COG1135 82 rKIGMIFQHFNLLSSrTVAENV--ALP----------LEIAGVpkaeiRKRVAELLE----LVGlSDKADaypsqLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2351811981 476 RQRLALARAfLADRP-LLLLDEPTASLDGETEAGIVEAVRRLAQ--GRTVLL------VVHRpallpLADRVVRLEPG 544
Cdd:COG1135 146 KQRVGIARA-LANNPkVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLithemdVVRR-----ICDRVAVLENG 217
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
921-1154 |
8.17e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 107.15 E-value: 8.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAERDAldsvDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGD-------- 992
Cdd:COG3840 2 LRLDDLTYRYGDFPLRF----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAerpvsmlf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 993 ---------TVRGFVGLcaqdahifdsSIRENLRLarTGATDEELRAALDRARLLDWAEALPAgldtlvgehgaRLSGGQ 1063
Cdd:COG3840 78 qennlfphlTVAQNIGL----------GLRPGLKL--TAEQRAQVEQALERVGLAGLLDRLPG-----------QLSGGQ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1064 RQRLALARAILADFPVLVLDEPAEHLDLATAD---ALTADlLAATRGRTTVLITHRLQGLEAV-DEVVVLEAGRVVQRGP 1139
Cdd:COG3840 135 RQRVALARCLVRKRPILLLDEPFSALDPALRQemlDLVDE-LCRERGLTVLMVTHDPEDAARIaDRVLLVADGRIAADGP 213
|
250
....*....|....*..
gi 2351811981 1140 YADLTAEEGP--LRRML 1154
Cdd:COG3840 214 TAALLDGEPPpaLAAYL 230
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
890-1154 |
8.18e-26 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 115.78 E-value: 8.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 890 RSAERVYEVLDAPPPVREPdSPAGTPASP--------------FP----LEVRGLSARYAGAERDALDSVDLRLTAGRRI 951
Cdd:TIGR01271 1170 RSVSRVFKFIDLPQEEPRP-SGGGGKYQLstvlvienphaqkcWPsggqMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRV 1248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 952 AVVGPSGSGKTTLAQVLLRFLDArEGTYRIGGVDACVLEGDTVRGFVGLCAQDAHIFDSSIRENLRlARTGATDEELRAA 1031
Cdd:TIGR01271 1249 GLLGRTGSGKSTLLSALLRLLST-EGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD-PYEQWSDEEIWKV 1326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1032 LDRARLLDWAEALPAGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTADLLAATRGRTTV 1111
Cdd:TIGR01271 1327 AEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVI 1406
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2351811981 1112 LITHRLQGLEAVDEVVVLEAGRVVQRGPYADLTAEEGPLRRML 1154
Cdd:TIGR01271 1407 LSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAM 1449
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
921-1142 |
2.23e-25 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 105.98 E-value: 2.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGD-TVRGFVG 999
Cdd:cd03219 1 LEVRGLTKRFGGLV--ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHeIARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1000 LCAQDAHIFDS-SIRENLRLA---RTGATDEELRAALDRARLLDWAEALPA--GLDTLVGEHGARLSGGQRQRLALARAI 1073
Cdd:cd03219 79 RTFQIPRLFPElTVLENVMVAaqaRTGSGLLLARARREEREARERAEELLErvGLADLADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2351811981 1074 LADFPVLVLDEPAEHLDLATADALtADLLA--ATRGRTTVLITHRLQGLEAV-DEVVVLEAGRVVQRGPYAD 1142
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEEL-AELIRelRERGITVLLVEHDMDVVMSLaDRVTVLDQGRVIAEGTPDE 229
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
324-527 |
2.91e-25 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 106.27 E-value: 2.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 324 TADVPESLRLELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLL-------DVVLGFTApdEGRVRVGGV 396
Cdd:COG1117 3 APASTLEPKIEVRNLNVYYGDK--QALKDINLDIPENKVTALIGPSGCGKSTLLrclnrmnDLIPGARV--EGEILLDGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 397 DL--ATLAPERWRERIAWVPQRPYLFAGTIAENV----RLA---RPDADDGAVAAALRDAGAYDfvaELPDGaqtlLGED 467
Cdd:COG1117 79 DIydPDVDVVELRRRVGMVFQKPNPFPKSIYDNVayglRLHgikSKSELDEIVEESLRKAALWD---EVKDR----LKKS 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 468 GAGLSAGQRQRLALARAfLADRP-LLLLDEPTASLDGETEAGIVEAVRRLAQGRTVLLVVH 527
Cdd:COG1117 152 ALGLSGGQQQRLCIARA-LAVEPeVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTH 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
333-539 |
5.13e-25 |
|
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: 102.51 E-value: 5.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGrgEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAP-ERWRERIA 411
Cdd:cd03216 1 LELRGITKRFGG--VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPrDARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 412 WVPQrpylfagtiaenvrlarpdaddgavaaalrdagaydfvaelpdgaqtllgedgagLSAGQRQRLALARAFLADRPL 491
Cdd:cd03216 79 MVYQ-------------------------------------------------------LSVGERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 492 LLLDEPTASLDG-ETEAGIvEAVRRL-AQGRTVLLVVHRPA-LLPLADRVV 539
Cdd:cd03216 104 LILDEPTAALTPaEVERLF-KVIRRLrAQGVAVIFISHRLDeVFEIADRVT 153
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
332-553 |
5.16e-25 |
|
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: 105.76 E-value: 5.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 332 RLELEGVTVRHEGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERIA 411
Cdd:cd03288 19 EIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 412 WVPQRPYLFAGTIAENVRLARpDADDGAVAAALRDAGAYDFVAELPDGAQTLLGEDGAGLSAGQRQRLALARAFLADRPL 491
Cdd:cd03288 99 IILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2351811981 492 LLLDEPTASLDGETEAGIVEAVRRLAQGRTVLLVVHRPALLPLADRVVRLEPGATLRPEKPE 553
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPE 239
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
921-1139 |
5.69e-25 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 107.88 E-value: 5.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGaeRDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDAcvlegDTV----RG 996
Cdd:COG3842 6 LELENVSKRYGD--VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-----TGLppekRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 997 fVGLCAQDAHIFDS-SIREN----LRLARTGATDEELRA--ALDRARLLDWAEALPagldtlvgehgARLSGGQRQRLAL 1069
Cdd:COG3842 79 -VGMVFQDYALFPHlTVAENvafgLRMRGVPKAEIRARVaeLLELVGLEGLADRYP-----------HQLSGGQQQRVAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2351811981 1070 ARAILADFPVLVLDEPAEHLDLATADALTADLLA--ATRGRTTVLITHRLQglEAV---DEVVVLEAGRVVQRGP 1139
Cdd:COG3842 147 ARALAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQE--EALalaDRIAVMNDGRIEQVGT 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
921-1138 |
5.81e-25 |
|
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: 104.20 E-value: 5.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGaeRDALDSVDLRLTAGRrIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDaCVLEGDTVRGFVGL 1000
Cdd:cd03264 1 LQLENLTKRYGK--KRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQD-VLKQPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDAHIFDS-SIRENLR-LAR-TGATDEELRAALDRA-RLLDWAEALpaglDTLVGEhgarLSGGQRQRLALARAILAD 1076
Cdd:cd03264 77 LPQEFGVYPNfTVREFLDyIAWlKGIPSKEVKARVDEVlELVNLGDRA----KKKIGS----LSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2351811981 1077 FPVLVLDEPAEHLDLATADALTADLLAATRGRTTVLITHRLQGLEAV-DEVVVLEAGRVVQRG 1138
Cdd:cd03264 149 PSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
348-1148 |
6.00e-25 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 112.91 E-value: 6.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 348 PSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGrvrvGGVDLatlaperwRERIAWVPQRPYLFAGTIAEN 427
Cdd:PLN03130 631 PTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSD----ASVVI--------RGTVAYVPQVSWIFNATVRDN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 428 VRLARPDADDGAVAAALRDAGAYDfVAELPDGAQTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEA 507
Cdd:PLN03130 699 ILFGSPFDPERYERAIDVTALQHD-LDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGR 777
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 508 GIVEA-VRRLAQGRTVLLVVHRPALLPLADRVVRL------------------------------------EPGATLRPE 550
Cdd:PLN03130 778 QVFDKcIKDELRGKTRVLVTNQLHFLSQVDRIILVhegmikeegtyeelsnngplfqklmenagkmeeyveENGEEEDDQ 857
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 551 KPEGSVAVPRPADASAAGRAAVPEPETL--------RDTAARPGQVLARVREAAGAqrgqLALALLLGSLALGSAVGLMA 622
Cdd:PLN03130 858 TSSKPVANGNANNLKKDSSSKKKSKEGKsvlikqeeRETGVVSWKVLERYKNALGG----AWVVMILFLCYVLTEVFRVS 933
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 623 VSGWLI-----SRASEQPPVLYLM---------VAVTATRAFGLGRAVFRYAERLvsHDAVLKMLaeLRvavyrgleriA 688
Cdd:PLN03130 934 SSTWLSewtdqGTPKTHGPLFYNLiyallsfgqVLVTLLNSYWLIMSSLYAAKRL--HDAMLGSI--LR----------A 999
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 689 PAGLRRSRR-GDLLSRL---VADVDALQDYWLRWLLPA-----GTAVVVGAATAGFIGWLLPaagivlatgLLLAGAGVP 759
Cdd:PLN03130 1000 PMSFFHTNPlGRIINRFakdLGDIDRNVAVFVNMFLGQifqllSTFVLIGIVSTISLWAIMP---------LLVLFYGAY 1070
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 760 LVSGACSRHAERQLAPARADLATRITDLLGGTAELTvagalpARKARTREADgvltriaaraatatalggglIALIGGLT 839
Cdd:PLN03130 1071 LYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIR------AYKAYDRMAE--------------------INGRSMDN 1124
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 840 VVATALVALPAvhdGRLAGVELAV-----VVLTPL------------AAFEAVTGLPLA-----VQYRQRVKRSA----- 892
Cdd:PLN03130 1125 NIRFTLVNMSS---NRWLAIRLETlgglmIWLTASfavmqngraenqAAFASTMGLLLSyalniTSLLTAVLRLAslaen 1201
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 893 -----ERVYEVLDAP---PPVREPDSPA-GTPASPfPLEVRGLSARYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTT 963
Cdd:PLN03130 1202 slnavERVGTYIDLPseaPLVIENNRPPpGWPSSG-SIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSS 1280
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 964 LAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGLCAQDAHIFDSSIRENLRlARTGATDEELRAALDRARLLDWAEA 1043
Cdd:PLN03130 1281 MLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLD-PFNEHNDADLWESLERAHLKDVIRR 1359
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1044 LPAGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATaDALTADLLAAT-RGRTTVLITHRLQGLEA 1122
Cdd:PLN03130 1360 NSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRT-DALIQKTIREEfKSCTMLIIAHRLNTIID 1438
|
890 900
....*....|....*....|....*.
gi 2351811981 1123 VDEVVVLEAGRVVQRGPYADLTAEEG 1148
Cdd:PLN03130 1439 CDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
333-539 |
7.04e-25 |
|
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: 104.12 E-value: 7.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATlAPERWRERIAW 412
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 413 VPQRPYLFAG-TIAENVRL-AR----PDADDGAVAAALRDAGaydfvaELPDGAQTLLGEdgagLSAGQRQRLALARAFL 486
Cdd:cd03263 80 CPQFDALFDElTVREHLRFyARlkglPKSEIKEEVELLLRVL------GLTDKANKRART----LSGGMKRKLSLAIALI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 487 ADRPLLLLDEPTASLDGETEAGIVEAVRRLAQGRTVLLVVHRPALLP-LADRVV 539
Cdd:cd03263 150 GGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEaLCDRIA 203
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
921-1152 |
7.05e-25 |
|
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: 105.71 E-value: 7.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDArEGTYRIGGVDACVLEGDTVRGFVGL 1000
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDAHIFDSSIRENLRlARTGATDEELRAALDRARLLDWAEALPAGLDTLVGEHGARLSGGQRQRLALARAILADFPVL 1080
Cdd:cd03289 82 IPQKVFIFSGTFRKNLD-PYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2351811981 1081 VLDEPAEHLDLATADALTADLLAATRGRTTVLITHRLQGLEAVDEVVVLEAGRVVQRGPYADLTAEEGPLRR 1152
Cdd:cd03289 161 LLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQ 232
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
332-539 |
9.61e-25 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 107.08 E-value: 9.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 332 RLELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPerwRER-I 410
Cdd:COG3839 3 SLELENVSKSYGGV--EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPP---KDRnI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 411 AWVPQRPYLF-AGTIAENVRLArpdaddgavaaaLRDAGAY--------DFVAElpdgaqtLLGEDG------AGLSAGQ 475
Cdd:COG3839 78 AMVFQSYALYpHMTVYENIAFP------------LKLRKVPkaeidrrvREAAE-------LLGLEDlldrkpKQLSGGQ 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 476 RQRLALARAFLADRPLLLLDEPTASLD----GETEAGIVEAVRRLaqGRTVLLVVHRPA-LLPLADRVV 539
Cdd:COG3839 139 RQRVALGRALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRL--GTTTIYVTHDQVeAMTLADRIA 205
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
333-545 |
1.11e-24 |
|
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: 103.81 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTV--RHEGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRE-- 408
Cdd:cd03258 2 IELKNVSKvfGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 409 -RIAWVPQRPYLFAG-TIAENVRLArpdaddgavaaaLRDAGAYDfvAELPDGAQTLLG----EDGAG-----LSAGQRQ 477
Cdd:cd03258 82 rRIGMIFQHFNLLSSrTVFENVALP------------LEIAGVPK--AEIEERVLELLElvglEDKADaypaqLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 478 RLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQ--GRTVLLVVHR-PALLPLADRVVRLEPGA 545
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEmEVVKRICDRVAVMEKGE 218
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
333-544 |
1.23e-24 |
|
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: 103.10 E-value: 1.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPErwrER-IA 411
Cdd:cd03301 1 VELENVTKRFGNV--TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK---DRdIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 412 WVPQRPYLFAG-TIAENVRLArpdaddgavaAALRDAGAYDFVAELPDGAQTL-----LGEDGAGLSAGQRQRLALARAF 485
Cdd:cd03301 76 MVFQNYALYPHmTVYDNIAFG----------LKLRKVPKDEIDERVREVAELLqiehlLDRKPKQLSGGQRQRVALGRAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 486 LADRPLLLLDEPTASLDG----ETEAGIVEAVRRLaqGRTVLLVVH-RPALLPLADRVVRLEPG 544
Cdd:cd03301 146 VREPKVFLMDEPLSNLDAklrvQMRAELKRLQQRL--GTTTIYVTHdQVEAMTMADRIAVMNDG 207
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
921-1138 |
1.54e-24 |
|
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: 103.92 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAeRDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDacVLEGDTV--RGFV 998
Cdd:cd03295 1 IEFENVTKRYGGG-KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGED--IREQDPVelRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 999 GLCAQDAHIFDS-SIRENLRLART--GATDEELRAALDRA-RLLDWAEAlpagldTLVGEHGARLSGGQRQRLALARAIL 1074
Cdd:cd03295 78 GYVIQQIGLFPHmTVEENIALVPKllKWPKEKIRERADELlALVGLDPA------EFADRYPHELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 1075 ADFPVLVLDEPAEHLDLATADALTADLLAATR--GRTTVLITHRLQglEAV---DEVVVLEAGRVVQRG 1138
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDID--EAFrlaDRIAIMKNGEIVQVG 218
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
921-1143 |
2.84e-24 |
|
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: 102.66 E-value: 2.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAERD--ALDSVDLRLTAGRRIAVVGPSGSGKTTLAQvLLRFLDA-REGTYRIGGVDACVLEGDTVRGF 997
Cdd:cd03258 2 IELKNVSKVFGDTGGKvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIR-CINGLERpTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 998 ---VGLCAQDAHIFDS-SIREN----LRLARTGATDEELRAA--LDRARLLDWAEALPAgldtlvgehgaRLSGGQRQRL 1067
Cdd:cd03258 81 rrrIGMIFQHFNLLSSrTVFENvalpLEIAGVPKAEIEERVLelLELVGLEDKADAYPA-----------QLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 1068 ALARAILADFPVLVLDEPAEHLDLATADALTADL--LAATRGRTTVLITHRLQGLEAV-DEVVVLEAGRVVQRGPYADL 1143
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETTQSILALLrdINRELGLTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
333-544 |
5.17e-24 |
|
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: 101.93 E-value: 5.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGrgEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPerWRERIAW 412
Cdd:cd03300 1 IELENVSKFYGG--FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPP--HKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 413 VPQRPYLFAG-TIAENVRLARPDADDGAVAAALRDAGAYDFVaelpdGAQTLLGEDGAGLSAGQRQRLALARAFLADRPL 491
Cdd:cd03300 77 VFQNYALFPHlTVFENIAFGLRLKKLPKAEIKERVAEALDLV-----QLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2351811981 492 LLLDEPTASLDGETEAGIVEAVRRLAQ--GRTVLLVVH-RPALLPLADRVVRLEPG 544
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHdQEEALTMSDRIAVMNKG 207
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
159-553 |
5.55e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 109.68 E-value: 5.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 159 VSAAIIVVTLPLIPLFM-ILIGWATQSRMDRQwrllsrlsghfLDVVAGLPTLKVFGRAKAQAESIRA---------ITS 228
Cdd:PLN03232 1048 VSTISLWAIMPLLILFYaAYLYYQSTSREVRR-----------LDSVTRSPIYAQFGEALNGLSSIRAykaydrmakING 1116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 229 QYRRATLR------------TLRIAFLSSFALELLATLSV---------ALVAVTIGMRLVhgeldlYTGLVVLILApea 287
Cdd:PLN03232 1117 KSMDNNIRftlantssnrwlTIRLETLGGVMIWLTATFAVlrngnaenqAGFASTMGLLLS------YTLNITTLLS--- 1187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 288 ylpirQVGAQYHAAAEGLSAAEEIFSVLETePRRGGTADV--------PESLRLELEGVTVRHEGRGEPSLDHASLVVDE 359
Cdd:PLN03232 1188 -----GVLRQASKAENSLNSVERVGNYIDL-PSEATAIIEnnrpvsgwPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSP 1261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 360 GETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERIAWVPQRPYLFAGTIAENVRlARPDADDGA 439
Cdd:PLN03232 1262 SEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNID-PFSEHNDAD 1340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 440 VAAALRDAGAYDFVAELPDGAQTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQG 519
Cdd:PLN03232 1341 LWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKS 1420
|
410 420 430
....*....|....*....|....*....|....
gi 2351811981 520 RTVLLVVHRPALLPLADRVVRLEPGATLRPEKPE 553
Cdd:PLN03232 1421 CTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQ 1454
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
922-1138 |
1.51e-23 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 99.92 E-value: 1.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 922 EVRGLSARYAGaeRDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDAcvlegDTVRGFVGLC 1001
Cdd:cd03235 1 EVEDLTVSYGG--HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL-----EKERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1002 AQDAHI---FDSSIRENLRLARTG----------ATDEELRAALDRARLLDWAealpaglDTLVGEhgarLSGGQRQRLA 1068
Cdd:cd03235 74 PQRRSIdrdFPISVRDVVLMGLYGhkglfrrlskADKAKVDEALERVGLSELA-------DRQIGE----LSGGQQQRVL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2351811981 1069 LARAILADFPVLVLDEPAEHLDLATADALTaDLLA--ATRGRTTVLITHRLQGLEA-VDEVVVLeAGRVVQRG 1138
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIY-ELLRelRREGMTILVVTHDLGLVLEyFDRVLLL-NRTVVASG 213
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
7-544 |
1.61e-23 |
|
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: 106.42 E-value: 1.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 7 RLLRyaRATRFFLAAVVALGVVGAALVIAQAMLVADVVVGGFEDGLTVSGLrtpLILLAAVALgraLVSWLTELAAYRAS 86
Cdd:COG4615 5 RLLL--RESRWLLLLALLLGLLSGLANAGLIALINQALNATGAALARLLLL---FAGLLVLLL---LSRLASQLLLTRLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 87 AAVKSELRGRLLDR--AAELGPglLSDRRTGSLVTLATRGVDALDDYFARyLPQLGLAVVVPVAVLARIVTEDWVSAAII 164
Cdd:COG4615 77 QHAVARLRLRLSRRilAAPLER--LERIGAARLLAALTEDVRTISQAFVR-LPELLQSVALVLGCLAYLAWLSPPLFLLT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 165 VVTLPLIplfmILIGWATQSRMDRQWRLLS----RLSGHFLDVVAGLPTLKvFGRAKAQA---ESIRAITSQYRRATLRT 237
Cdd:COG4615 154 LVLLGLG----VAGYRLLVRRARRHLRRAReaedRLFKHFRALLEGFKELK-LNRRRRRAffdEDLQPTAERYRDLRIRA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 238 LRIaFLSSFALELLATLsvALVAVTIGMRLVHGELDL--YTGLVVLILapeaYL--PIRQVGAQYHAAAEG---LSAAEE 310
Cdd:COG4615 229 DTI-FALANNWGNLLFF--ALIGLILFLLPALGWADPavLSGFVLVLL----FLrgPLSQLVGALPTLSRAnvaLRKIEE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 311 IFSVLETEPRRGGTADVPESL----RLELEGVTVRHEGRGEPSLDHA---SLVVDEGETVALVGPSGVGKSTLLDVVLGF 383
Cdd:COG4615 302 LELALAAAEPAAADAAAPPAPadfqTLELRGVTYRYPGEDGDEGFTLgpiDLTIRRGELVFIVGGNGSGKSTLAKLLTGL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 384 TAPDEGRVRVGGVDLATLAPERWRERIAWVPQRPYLFAgtiaenvRLARPDAddgavaaalrdagaydfvAELPDGAQTL 463
Cdd:COG4615 382 YRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFD-------RLLGLDG------------------EADPARAREL 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 464 LG----------EDGA----GLSAGQRQRLALARAFLADRPLLLLDEPTASLDGEteagiveaVRRL----------AQG 519
Cdd:COG4615 437 LErleldhkvsvEDGRfsttDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPE--------FRRVfytellpelkARG 508
|
570 580
....*....|....*....|....*
gi 2351811981 520 RTVLLVVHRPALLPLADRVVRLEPG 544
Cdd:COG4615 509 KTVIAISHDDRYFDLADRVLKMDYG 533
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
865-1166 |
1.71e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 108.29 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 865 VLTPLAAFE-----AVTGLPL---------AVQYRQRVKRSAERVY--EVLDAPPPVREPDSPAgtpaspfpLEVR-GLS 927
Cdd:PLN03130 551 DLTPARAFTslslfAVLRFPLfmlpnlitqAVNANVSLKRLEELLLaeERVLLPNPPLEPGLPA--------ISIKnGYF 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 928 ARYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTyriggvdacvleGDTVRGFVGLCAQDAHI 1007
Cdd:PLN03130 623 SWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDA------------SVVIRGTVAYVPQVSWI 690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1008 FDSSIRENLRLartGATDEELR--AALDRARLLDWAEALPAGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEP 1085
Cdd:PLN03130 691 FNATVRDNILF---GSPFDPERyeRAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDP 767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1086 AEHLDLATA----DALTADLLaatRGRTTVLITHRLQGLEAVDEVVVLEAGRVVQRGPYADLTAeEGPL-RRMLERERET 1160
Cdd:PLN03130 768 LSALDAHVGrqvfDKCIKDEL---RGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSN-NGPLfQKLMENAGKM 843
|
....*.
gi 2351811981 1161 EGVAEE 1166
Cdd:PLN03130 844 EEYVEE 849
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
348-544 |
2.45e-23 |
|
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: 100.11 E-value: 2.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 348 PSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPerwRER-IAWVPQRPYLFAG-TIA 425
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV---QERnVGFVFQHYALFRHmTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 426 ENVRL---ARPDADDGAVAAALRDagaydfVAELPDgaqtLLGEDG------AGLSAGQRQRLALARAfLADRP-LLLLD 495
Cdd:cd03296 93 DNVAFglrVKPRSERPPEAEIRAK------VHELLK----LVQLDWladrypAQLSGGQRQRVALARA-LAVEPkVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2351811981 496 EPTASLDGETEAGIVEAVRRLAQ--GRTVLLVVH-RPALLPLADRVVRLEPG 544
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHdQEEALEVADRVVVMNKG 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
921-1143 |
2.76e-23 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 102.84 E-value: 2.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLaqvlLR----FLDAREGTYRIGGVDAcvlegdtvrg 996
Cdd:COG3839 4 LELENVSKSYGGVE--ALKDIDLDIEDGEFLVLLGPSGCGKSTL----LRmiagLEDPTSGEILIGGRDV---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 997 fVGLCAQD---AHIFDS-------SIREN----LRLARTGAT--DEELRAALDRARLLDWAEALPAGLdtlvgehgarlS 1060
Cdd:COG3839 68 -TDLPPKDrniAMVFQSyalyphmTVYENiafpLKLRKVPKAeiDRRVREAAELLGLEDLLDRKPKQL-----------S 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1061 GGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTADL--LAATRGRTTVLITHRLqgLEAV---DEVVVLEAGRVV 1135
Cdd:COG3839 136 GGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIkrLHRRLGTTTIYVTHDQ--VEAMtlaDRIAVMNDGRIQ 213
|
....*...
gi 2351811981 1136 QRGPYADL 1143
Cdd:COG3839 214 QVGTPEEL 221
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
346-541 |
4.09e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 98.07 E-value: 4.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 346 GEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGvdlatlaperwRERIAWVPQR---PYLFAG 422
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRsevPDSLPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 423 TIAENVRLARPDADDGAVAAALRD-AGAYDFVAELpdGAQTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTASL 501
Cdd:NF040873 73 TVRDLVAMGRWARRGLWRRLTRDDrAAVDDALERV--GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2351811981 502 DGETEAGIVEAVRRL-AQGRTVLLVVHRPALLPLADRVVRL 541
Cdd:NF040873 151 DAESRERIIALLAEEhARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
921-1144 |
4.14e-23 |
|
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: 99.12 E-value: 4.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDAcVLEGDTVRGFVGL 1000
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDAHIFDS-SIRENLRL-AR-TGATDEELRAALDR-ARLLDwaeaLPAGLDTLVGEhgarLSGGQRQRLALARAILAD 1076
Cdd:cd03263 80 CPQFDALFDElTVREHLRFyARlKGLPKSEIKEEVELlLRVLG----LTDKANKRART----LSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 1077 FPVLVLDEPAEHLDLATADALTADLLAATRGRTTVLITHRLQGLEAV-DEVVVLEAGRVVQRGPYADLT 1144
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALcDRIAIMSDGKLRCIGSPQELK 220
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
866-1166 |
4.48e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 106.98 E-value: 4.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 866 LTPLAAFEAVT----------GLPLAVQYRQRVKRSAERVYEVLDAPPPVREPDSP--AGTPASPFPlevRGLSARYAGA 933
Cdd:PLN03232 552 LTPARAFTSLSlfavlrsplnMLPNLLSQVVNANVSLQRIEELLLSEERILAQNPPlqPGAPAISIK---NGYFSWDSKT 628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 934 ERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREgtyriggvDACVLegdtVRGFVGLCAQDAHIFDSSIR 1013
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE--------TSSVV----IRGSVAYVPQVSWIFNATVR 696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1014 ENLrLARTGATDEELRAALDRARLLDWAEALPAGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLAT 1093
Cdd:PLN03232 697 ENI-LFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHV 775
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2351811981 1094 A----DALTADLLaatRGRTTVLITHRLQGLEAVDEVVVLEAGRVVQRGPYADLTAEEGPLRRMLERERETEGVAEE 1166
Cdd:PLN03232 776 AhqvfDSCMKDEL---KGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAGKMDATQEV 849
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
921-1143 |
4.76e-23 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 101.28 E-value: 4.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAERD--ALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAR---EGTYRIGGVDACVLEGDTVR 995
Cdd:COG0444 2 LEVRNLKVYFPTRRGVvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 996 GF----VGLCAQDAhiFDS---------SIRENLRLARtGATDEELRA----ALDRARLLDWAEAL---PagldtlvgeH 1055
Cdd:COG0444 82 KIrgreIQMIFQDP--MTSlnpvmtvgdQIAEPLRIHG-GLSKAEAREraieLLERVGLPDPERRLdryP---------H 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1056 gaRLSGGQRQRLALARAILADFPVLVLDEPAEHLDLAT-ADALtaDLLA---ATRGRTTVLITHRLqGL--EAVDEVVVL 1129
Cdd:COG0444 150 --ELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIqAQIL--NLLKdlqRELGLAILFITHDL-GVvaEIADRVAVM 224
|
250
....*....|....
gi 2351811981 1130 EAGRVVQRGPYADL 1143
Cdd:COG0444 225 YAGRIVEEGPVEEL 238
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
921-1138 |
4.78e-23 |
|
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: 99.34 E-value: 4.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLegDTVRGFVGL 1000
Cdd:cd03296 3 IEVRNVSKRFGDFV--ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDV--PVQERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDAHIFDS-SIREN----LRLARTGATDEELRAALDRARLLDWAEalpagLDTLVGEHGARLSGGQRQRLALARAILA 1075
Cdd:cd03296 79 VFQHYALFRHmTVFDNvafgLRVKPRSERPPEAEIRAKVHELLKLVQ-----LDWLADRYPAQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2351811981 1076 DFPVLVLDEPAEHLDLATADALTADL--LAATRGRTTVLITH-RLQGLEAVDEVVVLEAGRVVQRG 1138
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLrrLHDELHVTTVFVTHdQEEALEVADRVVVMNKGRIEQVG 219
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
333-544 |
6.36e-23 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 101.76 E-value: 6.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLAT-LAPerwRER-I 410
Cdd:COG1118 3 IEVRNISKRFGSF--TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTnLPP---RERrV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 411 AWVPQRPYLFAG-TIAENVRLARPDADDGAVAAALRdagaydfVAELPDgaqtLLGEDG------AGLSAGQRQRLALAR 483
Cdd:COG1118 78 GFVFQHYALFPHmTVAENIAFGLRVRPPSKAEIRAR-------VEELLE----LVQLEGladrypSQLSGGQRQRVALAR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2351811981 484 AfLADRP-LLLLDEPTASLDGETEAGIVEAVRRL--AQGRTVLLVVHRP--AlLPLADRVVRLEPG 544
Cdd:COG1118 147 A-LAVEPeVLLLDEPFGALDAKVRKELRRWLRRLhdELGGTTVFVTHDQeeA-LELADRVVVMNQG 210
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
332-544 |
6.80e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 99.55 E-value: 6.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 332 RLELEGVTVRHEGRGE--PSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERwrer 409
Cdd:COG4525 3 MLTVRHVSVRYPGGGQpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 410 iAWVPQR----PYLfagTIAENV----RLARPDADDgavaaalRDAGAYDFVAelpdgaqtLLGEDGAG------LSAGQ 475
Cdd:COG4525 79 -GVVFQKdallPWL---NVLDNVafglRLRGVPKAE-------RRARAEELLA--------LVGLADFArrriwqLSGGM 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2351811981 476 RQRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQ--GRTVLLVVH--RPALLpLADRVVRLEPG 544
Cdd:COG4525 140 RQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQrtGKGVFLITHsvEEALF-LATRLVVMSPG 211
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
921-1139 |
7.39e-23 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 98.91 E-value: 7.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGD--TVRGFV 998
Cdd:COG1126 2 IEIENLHKSFGDLE--VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDinKLRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 999 GLCAQDAHIFDS-SIRENLRLA------RTGATDEEL-RAALDRARLLDWAEALPagldtlvgehgARLSGGQRQRLALA 1070
Cdd:COG1126 80 GMVFQQFNLFPHlTVLENVTLApikvkkMSKAEAEERaMELLERVGLADKADAYP-----------AQLSGGQQQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1071 RAiLADFP-VLVLDEPAEHLDlataDALTADLLA-----ATRGRTTVLITH-----RlqglEAVDEVVVLEAGRVVQRGP 1139
Cdd:COG1126 149 RA-LAMEPkVMLFDEPTSALD----PELVGEVLDvmrdlAKEGMTMVVVTHemgfaR----EVADRVVFMDGGRIVEEGP 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
333-544 |
7.70e-23 |
|
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: 97.86 E-value: 7.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGrGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATL---APERWRER 409
Cdd:cd03292 1 IEFINVTKTYPN-GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 410 IAWVPQRPYLFAG-TIAENVRLARPDADDGAVAAALRDAGAYDFVAeLPDGAQTLlgedGAGLSAGQRQRLALARAFLAD 488
Cdd:cd03292 80 IGVVFQDFRLLPDrNVYENVAFALEVTGVPPREIRKRVPAALELVG-LSHKHRAL----PAELSGGEQQRVAIARAIVNS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2351811981 489 RPLLLLDEPTASLDGETEAGIVEAVRRL-AQGRTVLLVVHRPALL-PLADRVVRLEPG 544
Cdd:cd03292 155 PTILIADEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATHAKELVdTTRHRVIALERG 212
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
333-527 |
8.46e-23 |
|
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: 97.65 E-value: 8.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHegRGEPSLDHASLVVDEGETvALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDlATLAPERWRERIAW 412
Cdd:cd03264 1 LQLENLTKRY--GKKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQD-VLKQPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 413 VPQRPYLFAG-TIAENVR-LAR-----PDADDGAVAAALRDAGAYDFVAELPdgaqtllgedgAGLSAGQRQRLALARAF 485
Cdd:cd03264 77 LPQEFGVYPNfTVREFLDyIAWlkgipSKEVKARVDEVLELVNLGDRAKKKI-----------GSLSGGMRRRVGIAQAL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2351811981 486 LADRPLLLLDEPTASLDGETEAGIVEAVRRLAQGRTVLLVVH 527
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTH 187
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
899-1139 |
8.97e-23 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 104.00 E-value: 8.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 899 LDAPPPVREPDSPAGTPASpfpLEVRGLSARYAG---------AERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLL 969
Cdd:COG4172 257 LAAEPRGDPRPVPPDAPPL---LEARDLKVWFPIkrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 970 RfLDAREGTYRIGGVDACVLEGDTVRGF---VGLCAQDAhiFDS---------SIRENLRLARTGATDEELRAaldRArl 1037
Cdd:COG4172 334 R-LIPSEGEIRFDGQDLDGLSRRALRPLrrrMQVVFQDP--FGSlsprmtvgqIIAEGLRVHGPGLSAAERRA---RV-- 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1038 ldwAEALPA-GLDtlvGEHGAR----LSGGQRQRLALARAILADFPVLVLDEPAEHLDLAT-ADALtaDLLA---ATRGR 1108
Cdd:COG4172 406 ---AEALEEvGLD---PAARHRypheFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVqAQIL--DLLRdlqREHGL 477
|
250 260 270
....*....|....*....|....*....|..
gi 2351811981 1109 TTVLITHRLQGLEAV-DEVVVLEAGRVVQRGP 1139
Cdd:COG4172 478 AYLFISHDLAVVRALaHRVMVMKDGKVVEQGP 509
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
344-545 |
9.14e-23 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 97.79 E-value: 9.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 344 GRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRER----IAWVPQRPYL 419
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 420 FAGTIAENVRLARPDaddgavaaalrDAGAYDFVAE----------LPDGAQTLLGEDGAGLSAGQRQRLALARAFLADR 489
Cdd:cd03290 91 LNATVEENITFGSPF-----------NKQRYKAVTDacslqpdidlLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 490 PLLLLDEPTASLDGE-----TEAGIVEAVRRlaQGRTVLLVVHRPALLPLADRVVRLEPGA 545
Cdd:cd03290 160 NIVFLDDPFSALDIHlsdhlMQEGILKFLQD--DKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
359-544 |
1.06e-22 |
|
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: 97.75 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 359 EGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDL------ATLAPERwrERIAWVPQRPYLFAG-TIAENVRLA 431
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrkkINLPPQQ--RKIGLVFQQYALFPHlNVRENLAFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 432 RPDaddgavaaaLRDAGAYDFVAELPD--GAQTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEAGI 509
Cdd:cd03297 100 LKR---------KRNREDRISVDELLDllGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 2351811981 510 VEAVRRLAQ--GRTVLLVVHRPA-LLPLADRVVRLEPG 544
Cdd:cd03297 171 LPELKQIKKnlNIPVIFVTHDLSeAEYLADRIVVMEDG 208
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
333-544 |
1.27e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 98.69 E-value: 1.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERIAW 412
Cdd:PRK13548 3 LEARNLSVRLGGR--TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 413 VPQRPYL-FAGTIAENVRLAR-PDADDGAVAAALRDAgAYDFVaelpdGAQTLLGEDGAGLSAGQRQRLALARAfLA--- 487
Cdd:PRK13548 81 LPQHSSLsFPFTVEEVVAMGRaPHGLSRAEDDALVAA-ALAQV-----DLAHLAGRDYPQLSGGEQQRVQLARV-LAqlw 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 488 ----DRPLLLLDEPTASLDGETEAGIVEAVRRLA--QGRTVLLVVHRPALLPL-ADRVVRLEPG 544
Cdd:PRK13548 154 epdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAheRGLAVIVVLHDLNLAARyADRIVLLHQG 217
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
921-1153 |
1.30e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 99.32 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVdacVLEGDTV---RGF 997
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETVwdvRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 998 VGLCAQ--DAHIFDSSIR-------ENLRLARTGATdEELRAALDRARLLDWAEALPagldtlvgehgARLSGGQRQRLA 1068
Cdd:PRK13635 83 VGMVFQnpDNQFVGATVQddvafglENIGVPREEMV-ERVDQALRQVGMEDFLNREP-----------HRLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1069 LArAILADFP-VLVLDEPAEHLD-------LATADALTAdllaatRGRTTVL-ITHRLQGLEAVDEVVVLEAGRVVQRGP 1139
Cdd:PRK13635 151 IA-GVLALQPdIIILDEATSMLDprgrrevLETVRQLKE------QKGITVLsITHDLDEAAQADRVIVMNKGEILEEGT 223
|
250
....*....|....
gi 2351811981 1140 YADLTAEEGPLRRM 1153
Cdd:PRK13635 224 PEEIFKSGHMLQEI 237
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
333-544 |
1.35e-22 |
|
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: 98.23 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEG-RVRV-----GGVDLATLaperw 406
Cdd:COG1119 4 LELRNVTVRRGGK--TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLfgerrGGEDVWEL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 407 RERIAWVPQR--PYLFAGTIAENVRLArpdaddgavaaalrdaGAYDFV-------AELPDGAQTLLGEDGAG------- 470
Cdd:COG1119 77 RKRIGLVSPAlqLRFPRDETVLDVVLS----------------GFFDSIglyreptDEQRERARELLELLGLAhladrpf 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 471 --LSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQ--GRTVLLVVHRPA-LLPLADRVVRLEPG 544
Cdd:COG1119 141 gtLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAegAPTLVLVTHHVEeIPPGITHVLLLKDG 219
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
921-1142 |
1.38e-22 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 98.57 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDacvLEGDT------- 993
Cdd:COG0411 5 LEVRGLTKRFGGLV--AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRD---ITGLPphriarl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 994 --VRGFvglcaQDAHIFDS-SIRENLRLA--------------RTGATDEELRAALDRARllDWAEALpaGLDTLVGEHG 1056
Cdd:COG0411 80 giARTF-----QNPRLFPElTVLENVLVAaharlgrgllaallRLPRARREEREARERAE--ELLERV--GLADRADEPA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1057 ARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTADL--LAATRGRTTVLITHRLQGLEAV-DEVVVLEAGR 1133
Cdd:COG0411 151 GNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIrrLRDERGITILLIEHDMDLVMGLaDRIVVLDFGR 230
|
....*....
gi 2351811981 1134 VVQRGPYAD 1142
Cdd:COG0411 231 VIAEGTPAE 239
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
942-1138 |
1.40e-22 |
|
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: 97.18 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 942 DLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDacVLEGDTVRGFVGLCAQDAHIFDS-SIRENLRLAR 1020
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVD--VTAAPPADRPVSMLFQENNLFAHlTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1021 TGAT--DEELRAALDRArlldwaeALPAGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALT 1098
Cdd:cd03298 96 SPGLklTAEDRQAIEVA-------LARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2351811981 1099 ADLLA--ATRGRTTVLITHRLQGLEAVDE-VVVLEAGRVVQRG 1138
Cdd:cd03298 169 DLVLDlhAETKMTVLMVTHQPEDAKRLAQrVVFLDNGRIAAQG 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
921-1138 |
2.17e-22 |
|
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: 97.31 E-value: 2.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDacVLEGDTVRGFVGL 1000
Cdd:cd03300 1 IELENVSKFYGGFV--ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKD--ITNLPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDAHIFDS-SIREN----LRLARTGATD--EELRAALDRARLLDWAEALPAgldtlvgehgaRLSGGQRQRLALARAI 1073
Cdd:cd03300 77 VFQNYALFPHlTVFENiafgLRLKKLPKAEikERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1074 LADFPVLVLDEPAEHLDLATADALTADL--LAATRGRTTVLITHRLQglEAV---DEVVVLEAGRVVQRG 1138
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKDMQLELkrLQKELGITFVFVTHDQE--EALtmsDRIAVMNKGKIQQIG 213
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
346-555 |
2.53e-22 |
|
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: 98.39 E-value: 2.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 346 GEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGvdlatlaperwreRIAWVPQRPYLFAGTIA 425
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 426 ENVrLARPDADDGAVAAALRDAGAYDFVAELPDGAQTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGET 505
Cdd:cd03291 116 ENI-IFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 506 EAGIVEA-VRRLAQGRTVLLVVHRPALLPLADRVVRLEPGAT--------LRPEKPEGS 555
Cdd:cd03291 195 EKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSyfygtfseLQSLRPDFS 253
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
921-1161 |
2.70e-22 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 97.80 E-value: 2.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAgaERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLD----AR-EGTYRIGGVDacVLEGDT-- 993
Cdd:COG1117 12 IEVRNLNVYYG--DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDlipgARvEGEILLDGED--IYDPDVdv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 994 --VRGFVGLCAQDAHIFDSSIREN----LRLA---RTGATDEELRAALDRARLldWAEalpagldtlV----GEHGARLS 1060
Cdd:COG1117 88 veLRRRVGMVFQKPNPFPKSIYDNvaygLRLHgikSKSELDEIVEESLRKAAL--WDE---------VkdrlKKSALGLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1061 GGQRQRLALARAILADFPVLVLDEPAEHLD-LATA--DALTADLlaatRGRTTVLI-THRLQgleavdevvvlEAGRVvq 1136
Cdd:COG1117 157 GGQQQRLCIARALAVEPEVLLMDEPTSALDpISTAkiEELILEL----KKDYTIVIvTHNMQ-----------QAARV-- 219
|
250 260 270
....*....|....*....|....*....|....*
gi 2351811981 1137 rgpyADLTA--------EEGPLRRMLE--RERETE 1161
Cdd:COG1117 220 ----SDYTAffylgelvEFGPTEQIFTnpKDKRTE 250
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
921-1138 |
3.29e-22 |
|
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: 96.17 E-value: 3.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAgaERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEgdtvrgfvgl 1000
Cdd:cd03301 1 VELENVTKRFG--NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLP---------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 cAQD---AHIFDS-------SIREN----LRLARTGatdeelRAALDRaRLLDWAEALpaGLDTLVGEHGARLSGGQRQR 1066
Cdd:cd03301 69 -PKDrdiAMVFQNyalyphmTVYDNiafgLKLRKVP------KDEIDE-RVREVAELL--QIEHLLDRKPKQLSGGQRQR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2351811981 1067 LALARAILADFPVLVLDEPAEHLDLATADALTADL--LAATRGRTTVLITH-RLQGLEAVDEVVVLEAGRVVQRG 1138
Cdd:cd03301 139 VALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELkrLQQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
345-544 |
3.94e-22 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 99.40 E-value: 3.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 345 RGEPSLDhASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLA------TLAPERwReRIAWVPQRPY 418
Cdd:COG4148 11 RGGFTLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQdsargiFLPPHR-R-RIGYVFQEAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 419 LFAG-TIAENVRLARPDADDGavaaalRDAGAYDFVAELPdGAQTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEP 497
Cdd:COG4148 88 LFPHlSVRGNLLYGRKRAPRA------ERRISFDEVVELL-GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2351811981 498 TASLDGETEAGIVEAVRRLAQ--GRTVLLVVHRPA-LLPLADRVVRLEPG 544
Cdd:COG4148 161 LAALDLARKAEILPYLERLRDelDIPILYVSHSLDeVARLADHVVLLEQG 210
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
921-1134 |
5.42e-22 |
|
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: 95.67 E-value: 5.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGG--VDACVLEGDTVRGFV 998
Cdd:cd03262 1 IEIKNLHKSFGDFH--VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkLTDDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 999 GLCAQDAHIFDS-SIRENLRLART---GATDEELRA----ALDRARLLDWAEALPAgldtlvgehgaRLSGGQRQRLALA 1070
Cdd:cd03262 79 GMVFQQFNLFPHlTVLENITLAPIkvkGMSKAEAEEraleLLEKVGLADKADAYPA-----------QLSGGQQQRVAIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1071 RAILADFPVLVLDEPAEHLDlataDALTADLL-----AATRGRTTVLITHRLQ-GLEAVDEVVVLEAGRV 1134
Cdd:cd03262 148 RALAMNPKVMLFDEPTSALD----PELVGEVLdvmkdLAEEGMTMVVVTHEMGfAREVADRVIFMDDGRI 213
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
921-1143 |
6.26e-22 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 98.61 E-value: 6.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAERD--ALDSVDLRLTAGRRIAVVGPSGSGKTTLaqvlLRFLDARE----GTYRIGGVDACVLEGDTV 994
Cdd:COG1135 2 IELENLSKTFPTKGGPvtALDDVSLTIEKGEIFGIIGYSGAGKSTL----IRCINLLErptsGSVLVDGVDLTALSEREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 995 RGF---VGLCAQDAHIFDS-SIREN----LRLARTGATDEELRAA--LDRARLLDWAEALPAgldtlvgehgaRLSGGQR 1064
Cdd:COG1135 78 RAArrkIGMIFQHFNLLSSrTVAENvalpLEIAGVPKAEIRKRVAelLELVGLSDKADAYPS-----------QLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1065 QRLALARAiLADFP-VLVLDEPAEHLDLATADALtADLLAATRGR---TTVLITHRlqgLEAV----DEVVVLEAGRVVQ 1136
Cdd:COG1135 147 QRVGIARA-LANNPkVLLCDEATSALDPETTRSI-LDLLKDINRElglTIVLITHE---MDVVrricDRVAVLENGRIVE 221
|
....*..
gi 2351811981 1137 RGPYADL 1143
Cdd:COG1135 222 QGPVLDV 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
333-539 |
7.83e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 100.48 E-value: 7.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHegRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAP-ERWRERIA 411
Cdd:COG1129 5 LEMRGISKSF--GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrDAQAAGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 412 WVPQRPYLFAG-TIAENVRLARPdaddgavaaaLRDAGAYDFvAELPDGAQTLLGEDG---------AGLSAGQRQRLAL 481
Cdd:COG1129 83 IIHQELNLVPNlSVAENIFLGRE----------PRRGGLIDW-RAMRRRARELLARLGldidpdtpvGDLSVAQQQLVEI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 482 ARAFLADRPLLLLDEPTASLDgETEAGIV-EAVRRL-AQGRTVLLVVHR-PALLPLADRVV 539
Cdd:COG1129 152 ARALSRDARVLILDEPTASLT-EREVERLfRIIRRLkAQGVAIIYISHRlDEVFEIADRVT 211
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
937-1134 |
1.14e-21 |
|
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: 94.78 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 937 ALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTV---RGFVGLCAQDAH-IFDSSI 1012
Cdd:cd03292 16 ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIpylRRKIGVVFQDFRlLPDRNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1013 RENLRLAR--TGATDEELR----AALDRARLLDWAEALPAGldtlvgehgarLSGGQRQRLALARAILADFPVLVLDEPA 1086
Cdd:cd03292 96 YENVAFALevTGVPPREIRkrvpAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTILIADEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 1087 EHLDLATADALtADLLAAT--RGRTTVLITHRLQGLEAVDE-VVVLEAGRV 1134
Cdd:cd03292 165 GNLDPDTTWEI-MNLLKKInkAGTTVVVATHAKELVDTTRHrVIALERGKL 214
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
346-555 |
1.26e-21 |
|
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: 102.30 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 346 GEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGvdlatlaperwreRIAWVPQRPYLFAGTIA 425
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 426 ENVrLARPDADDGAVAAALRDAGAYDFVAELPDGAQTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGET 505
Cdd:TIGR01271 505 DNI-IFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 506 EAGIVEA-VRRLAQGRTVLLVVHRPALLPLADRVVRLEPG--------ATLRPEKPEGS 555
Cdd:TIGR01271 584 EKEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGvcyfygtfSELQAKRPDFS 642
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
333-545 |
1.39e-21 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 92.99 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRhEGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVggvdlatlaPErwRERIAW 412
Cdd:cd03223 1 IELENLSLA-TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PE--GEDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 413 VPQRPYLFAGTiaenvrlarpdaddgavaaaLRDAGAYDFVAElpdgaqtllgedgagLSAGQRQRLALARAFLAdRP-L 491
Cdd:cd03223 69 LPQRPYLPLGT--------------------LREQLIYPWDDV---------------LSGGEQQRLAFARLLLH-KPkF 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 492 LLLDEPTASLDGETEAGIVEAVRRLaqGRTVLLVVHRPALLPLADRVVRLEPGA 545
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQLLKEL--GITVISVGHRPSLWKFHDRVLDLDGEG 164
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
914-1136 |
2.21e-21 |
|
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: 94.42 E-value: 2.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 914 TPASPFPLEVRGLSARYAGAER--DALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEG 991
Cdd:COG4181 2 SSSSAPIIELRGLTKTVGTGAGelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 992 D---TVRG-FVGLCAQDAHIFDS-SIREN----LRLARTGATDEELRAALDRARLLDWAEALPAGldtlvgehgarLSGG 1062
Cdd:COG4181 82 DaraRLRArHVGFVFQSFQLLPTlTALENvmlpLELAGRRDARARARALLERVGLGHRLDHYPAQ-----------LSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2351811981 1063 QRQRLALARAILADFPVLVLDEPAEHLDLATADALtADLL---AATRGRTTVLITHRLQGLEAVDEVVVLEAGRVVQ 1136
Cdd:COG4181 151 EQQRVALARAFATEPAILFADEPTGNLDAATGEQI-IDLLfelNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
333-527 |
2.32e-21 |
|
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: 96.28 E-value: 2.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRGEP--SLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAP---DEGRVRVGGVDLATLAPERWR 407
Cdd:COG0444 2 LEVRNLKVYFPTRRGVvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 408 E----RIAWVPQRPYlfagT-----------IAENVRLARPdaddgavaaaLRDAGAYDFVAE------LPDGAQTLL-- 464
Cdd:COG0444 82 KirgrEIQMIFQDPM----TslnpvmtvgdqIAEPLRIHGG----------LSKAEARERAIEllervgLPDPERRLDry 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2351811981 465 -GEdgagLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQ--GRTVLLVVH 527
Cdd:COG0444 148 pHE----LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRelGLAILFITH 209
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
333-547 |
2.40e-21 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 93.44 E-value: 2.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERwrERIAW 412
Cdd:cd03268 1 LKTNDLTKTYGKK--RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 413 VPQRPYLFAG-TIAENVRLARpdaddgaVAAALRDAGAYDFVAELpdgaqtLLGEDG----AGLSAGQRQRLALARAFLA 487
Cdd:cd03268 77 LIEAPGFYPNlTARENLRLLA-------RLLGIRKKRIDEVLDVV------GLKDSAkkkvKGFSLGMKQRLGIALALLG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 488 DRPLLLLDEPTASLDGEteaGIVEaVRRL-----AQGRTVLLVVHrpaLLP----LADRVVRLEPGATL 547
Cdd:cd03268 144 NPDLLILDEPTNGLDPD---GIKE-LRELilslrDQGITVLISSH---LLSeiqkVADRIGIINKGKLI 205
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
921-1155 |
3.28e-21 |
|
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: 94.87 E-value: 3.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARY-------AGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDT 993
Cdd:TIGR02769 3 LEVRDVTHTYrtgglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 994 VRGF---VGLCAQDAH-------IFDSSIRENLR-LARTGATDEELRAAldraRLLDWAEALPAGLDTLvgehGARLSGG 1062
Cdd:TIGR02769 83 RRAFrrdVQLVFQDSPsavnprmTVRQIIGEPLRhLTSLDESEQKARIA----ELLDMVGLRSEDADKL----PRQLSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1063 QRQRLALARAILADFPVLVLDEPAEHLDLATADALTADL--LAATRGRTTVLITHRLQGLEAV-DEVVVLEAGRVVQRGP 1139
Cdd:TIGR02769 155 QLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLrkLQQAFGTAYLFITHDLRLVQSFcQRVAVMDKGQIVEECD 234
|
250
....*....|....*.
gi 2351811981 1140 YADLTAEEGPLRRMLE 1155
Cdd:TIGR02769 235 VAQLLSFKHPAGRNLQ 250
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
333-544 |
4.98e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 94.70 E-value: 4.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVdlaTLAPER-W--RER 409
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETvWdvRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 410 IAWVPQRP-YLFAG-TIAENVRLARPDADDGAVAAALRDAGAYDFVaelpdGAQTLLGEDGAGLSAGQRQRLALArAFLA 487
Cdd:PRK13635 83 VGMVFQNPdNQFVGaTVQDDVAFGLENIGVPREEMVERVDQALRQV-----GMEDFLNREPHRLSGGQKQRVAIA-GVLA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 488 DRP-LLLLDEPTASLDGETEAGIVEAVRRL--AQGRTVLLVVHRPALLPLADRVVRLEPG 544
Cdd:PRK13635 157 LQPdIIILDEATSMLDPRGRREVLETVRQLkeQKGITVLSITHDLDEAAQADRVIVMNKG 216
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
335-539 |
6.89e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.83 E-value: 6.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 335 LEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGvdlatlaperwRERIAWVP 414
Cdd:COG0488 1 LENLSKSFGGR--PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 415 QRPYLFAG-TIAENV------------RLARPDADDGAVAAALR----------DAGAYDFVAELpdgAQTLLG-----E 466
Cdd:COG0488 68 QEPPLDDDlTVLDTVldgdaelraleaELEELEAKLAEPDEDLErlaelqeefeALGGWEAEARA---EEILSGlgfpeE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 467 DG----AGLSAGQRQRLALARAFLADRPLLLLDEPTASLDgeteagiVEAVRRLAQ-----GRTVLLVVHRPALLplaDR 537
Cdd:COG0488 145 DLdrpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD-------LESIEWLEEflknyPGTVLVVSHDRYFL---DR 214
|
..
gi 2351811981 538 VV 539
Cdd:COG0488 215 VA 216
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
346-527 |
7.08e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.45 E-value: 7.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 346 GEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERIAWVPQRPYL-FAGTI 424
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 425 AENVRLARPDADDGAVAAALRDAGAYDFVAELPDGAQtLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGE 504
Cdd:PRK09536 95 RQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQ-FADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDIN 173
|
170 180
....*....|....*....|....
gi 2351811981 505 TEAGIVEAVRRLAQ-GRTVLLVVH 527
Cdd:PRK09536 174 HQVRTLELVRRLVDdGKTAVAAIH 197
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
350-544 |
7.10e-21 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 92.41 E-value: 7.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 350 LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATL-APERWRER---IAWVPQRPYLFAG-TI 424
Cdd:TIGR02211 21 LKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLsSNERAKLRnkkLGFIYQFHHLLPDfTA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 425 AENVrlARPDADDGAVaaalrdagaydfVAELPDGAQTLLGEDGAG---------LSAGQRQRLALARAFLADRPLLLLD 495
Cdd:TIGR02211 101 LENV--AMPLLIGKKS------------VKEAKERAYEMLEKVGLEhrinhrpseLSGGERQRVAIARALVNQPSLVLAD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 496 EPTASLDGETEAGIVEAVRRL--AQGRTVLLVVHRPALLPLADRVVRLEPG 544
Cdd:TIGR02211 167 EPTGNLDNNNAKIIFDLMLELnrELNTSFLVVTHDLELAKKLDRVLEMKDG 217
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
328-554 |
7.98e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 99.43 E-value: 7.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 328 PESLRLELEGVTVRHEGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWR 407
Cdd:PLN03130 1233 PSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLR 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 408 ERIAWVPQRPYLFAGTIAENVrlaRPDADDGAVAA--ALRDAGAYDFVAELPDGAQTLLGEDGAGLSAGQRQRLALARAF 485
Cdd:PLN03130 1313 KVLGIIPQAPVLFSGTVRFNL---DPFNEHNDADLweSLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARAL 1389
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 486 LADRPLLLLDEPTASLDGETEAGIVEAVRRLAQGRTVLLVVHRPALLPLADRVVRLEPGATLRPEKPEG 554
Cdd:PLN03130 1390 LRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPEN 1458
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
19-289 |
8.10e-21 |
|
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: 93.86 E-value: 8.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 19 LAAVVALGVVGAALVIAQAMLVADVVVGGFEDGLTVSG-LRTPLILLAAVALGRALVSWLTELAAYRASAAVKSELRGRL 97
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQaLNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 98 LDRAAELGPGLLSDRRTGSLVTLATRGVDALDDYFARYLPQLGLAVVVPVAVLARIVTEDWVSAAIIVVTLPLIPLFMIL 177
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 178 IGWATQSRMDRQWRLLSRLSGHFLDVVAGLPTLKVFGRAKAQAESIRAITSQYRRATLRTLRIAFLSSFALELLATLSVA 257
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|...
gi 2351811981 258 LVAVtIGMRLVH-GELDLytGLVVLILAPEAYL 289
Cdd:pfam00664 241 LALW-FGAYLVIsGELSV--GDLVAFLSLFAQL 270
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
332-545 |
8.66e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 91.86 E-value: 8.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 332 RLELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPerwRERIA 411
Cdd:PRK13539 2 MLEGEDLACVRGGR--VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDV---AEACH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 412 WVPQR----PYLfagTIAENVRLARpdaddgavaaALRDAGAYDFVAELPD-GAQTLLGEDGAGLSAGQRQRLALARAFL 486
Cdd:PRK13539 77 YLGHRnamkPAL---TVAENLEFWA----------AFLGGEELDIAAALEAvGLAPLAHLPFGYLSAGQKRRVALARLLV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 487 ADRPLLLLDEPTASLDGETEAGIVEAVR-RLAQGRTVLLVVHRPALLPLAdRVVRLEPGA 545
Cdd:PRK13539 144 SNRPIWILDEPTAALDAAAVALFAELIRaHLAQGGIVIAATHIPLGLPGA-RELDLGPFA 202
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
333-527 |
9.18e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 93.23 E-value: 9.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVR-HEGRGE--PSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRER 409
Cdd:COG1101 2 LELKNLSKTfNPGTVNekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 410 IAWVPQRPylFAGT-----IAENVRLA----RPDADDGAVAAALRDagayDFVAELpdgAQTLLG-----EDGAG-LSAG 474
Cdd:COG1101 82 IGRVFQDP--MMGTapsmtIEENLALAyrrgKRRGLRRGLTKKRRE----LFRELL---ATLGLGlenrlDTKVGlLSGG 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2351811981 475 QRQRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRL--AQGRTVLLVVH 527
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTH 207
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
901-1142 |
1.06e-20 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 99.08 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 901 APPPVREPDSPAGTPASPFPLEV-----RGLSARYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAR 975
Cdd:PTZ00243 634 ASRHIVEGGTGGGHEATPTSERSaktpkMKTDDFFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEIS 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 976 EGTYRIGGVDACVlegdtvrgfvglcAQDAHIFDSSIRENLRLartgaTDEELRAALDRARLLDWAEA----LPAGLDTL 1051
Cdd:PTZ00243 714 EGRVWAERSIAYV-------------PQQAWIMNATVRGNILF-----FDEEDAARLADAVRVSQLEAdlaqLGGGLETE 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1052 VGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTAD-LLAATRGRTTVLITHRLQGLEAVDEVVVLE 1130
Cdd:PTZ00243 776 IGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEEcFLGALAGKTRVLATHQVHVVPRADYVVALG 855
|
250
....*....|..
gi 2351811981 1131 AGRVVQRGPYAD 1142
Cdd:PTZ00243 856 DGRVEFSGSSAD 867
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
938-1138 |
1.13e-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: 91.59 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 938 LDSVDLRL---TAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGV---DACV-LEGDTVRGFVGLCAQDAHIFDS 1010
Cdd:cd03297 10 LPDFTLKIdfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRKkINLPPQQRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1011 -SIRENLRLARTGATDEELRaaldrarllDWAEALPA--GLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAE 1087
Cdd:cd03297 90 lNVRENLAFGLKRKRNREDR---------ISVDELLDllGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 1088 HLDLATADALTADL--LAATRGRTTVLITHRLQGLEAV-DEVVVLEAGRVVQRG 1138
Cdd:cd03297 161 ALDRALRLQLLPELkqIKKNLNIPVIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
307-544 |
1.14e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.06 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 307 AAEEIfsVLETEPRRGGTA--DVPESLR-----LELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDV 379
Cdd:COG0488 285 ALEKL--EREEPPRRDKTVeiRFPPPERlgkkvLELEGLSKSYGDK--TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 380 VLGFTAPDEGRVRVGgvdlATLaperwreRIAWVPQ-RPYLFAG-TIAENVRLARPDADDGAVAAALrdaGAYDFVaelP 457
Cdd:COG0488 361 LAGELEPDSGTVKLG----ETV-------KIGYFDQhQEELDPDkTVLDELRDGAPGGTEQEVRGYL---GRFLFS---G 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 458 DGAQTLLGEdgagLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAvrrLA--QGrTVLLVVHRPALLP-L 534
Cdd:COG0488 424 DDAFKPVGV----LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEA---LDdfPG-TVLLVSHDRYFLDrV 495
|
250
....*....|
gi 2351811981 535 ADRVVRLEPG 544
Cdd:COG0488 496 ATRILEFEDG 505
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
952-1148 |
1.39e-20 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 98.56 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 952 AVVGPSGSGKTTLAQVLLRFLDAR------------------------------------------------------EG 977
Cdd:PTZ00265 1198 AIVGETGSGKSTVMSLLMRFYDLKndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfknSG 1277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 978 TYRIGGVDACVLEGDTVRGFVGLCAQDAHIFDSSIRENLRLARTGATDEELRAALDRARLLDWAEALPAGLDTLVGEHGA 1057
Cdd:PTZ00265 1278 KILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGK 1357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1058 RLSGGQRQRLALARAILADFPVLVLDEPAEHLDlATADALTADLLAATR---GRTTVLITHRLQGLEAVDEVVVL----E 1130
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLD-SNSEKLIEKTIVDIKdkaDKTIITIAHRIASIKRSDKIVVFnnpdR 1436
|
250 260
....*....|....*....|
gi 2351811981 1131 AGRVVQ-RGPYAD-LTAEEG 1148
Cdd:PTZ00265 1437 TGSFVQaHGTHEElLSVQDG 1456
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
921-1146 |
2.37e-20 |
|
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: 2.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAERdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGD---TVRGF 997
Cdd:TIGR02315 2 LEVENLSKVYPNGKQ-ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKklrKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 998 VGLCAQDAHIFD-SSIRENLRLARTGATDEeLRAALDRARLLDWAEALPA----GLDTLVGEHGARLSGGQRQRLALARA 1072
Cdd:TIGR02315 81 IGMIFQHYNLIErLTVLENVLHGRLGYKPT-WRSLLGRFSEEDKERALSAlervGLADKAYQRADQLSGGQQQRVAIARA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2351811981 1073 iLADFPVLVL-DEPAEHLDLATADALTADLLAATR--GRTTVLITHRLQ-GLEAVDEVVVLEAGRVVQRGPYADLTAE 1146
Cdd:TIGR02315 160 -LAQQPDLILaDEPIASLDPKTSKQVMDYLKRINKedGITVIINLHQVDlAKKYADRIVGLKAGEIVFDGAPSELDDE 236
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
333-595 |
2.59e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 96.72 E-value: 2.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTvRHEGRGEPS---LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERW--- 406
Cdd:PRK10535 5 LELKDIR-RSYPSGEEQvevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 407 -RERIAWVPQRPYLFAG-TIAENVRLARPDADDGAVAAALRdagaydfvaelpdgAQTLLGEDGAG---------LSAGQ 475
Cdd:PRK10535 84 rREHFGFIFQRYHLLSHlTAAQNVEVPAVYAGLERKQRLLR--------------AQELLQRLGLEdrveyqpsqLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 476 RQRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRL-AQGRTVLLVVHRPALLPLADRVVRLEPGATLRPEKPEG 554
Cdd:PRK10535 150 QQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLrDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQE 229
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2351811981 555 SVAVprpadasaagraaVPEPETLRDTAARPGQVLARVREA 595
Cdd:PRK10535 230 KVNV-------------AGGTEPVVNTASGWRQFVSGFREA 257
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
333-518 |
2.84e-20 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 91.07 E-value: 2.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAP-ERWRERIA 411
Cdd:cd03218 1 LRAENLSKRYGKR--KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 412 WVPQRPYLFAG-TIAENVRLArpdaddgavaaaLRdaGAYDFVAELPDGAQTLLGE---------DGAGLSAGQRQRLAL 481
Cdd:cd03218 79 YLPQEASIFRKlTVEENILAV------------LE--IRGLSKKEREEKLEELLEEfhithlrksKASSLSGGERRRVEI 144
|
170 180 190
....*....|....*....|....*....|....*..
gi 2351811981 482 ARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQ 518
Cdd:cd03218 145 ARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKD 181
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
354-527 |
2.88e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 91.18 E-value: 2.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 354 SLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPErwRERIAWVPQRPYLFAG-TIAENVRLA- 431
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFSHlTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 432 RP-----DADDGAVAAALRDAGAYDFVAELPdgaqtllgedgAGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETE 506
Cdd:PRK10771 97 NPglklnAAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
|
170 180
....*....|....*....|...
gi 2351811981 507 AGIVEAVRRLAQGR--TVLLVVH 527
Cdd:PRK10771 166 QEMLTLVSQVCQERqlTLLMVSH 188
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
333-541 |
2.94e-20 |
|
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: 90.11 E-value: 2.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPErWRERIAW 412
Cdd:TIGR01189 1 LAARNLACSRGER--MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE-PHENILY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 413 VPQRPYLFAG-TIAENVRLARP--DADDGAVAAALRDAGAYDFvAELPdgaqtllgedGAGLSAGQRQRLALARAFLADR 489
Cdd:TIGR01189 78 LGHLPGLKPElSALENLHFWAAihGGAQRTIEDALAAVGLTGF-EDLP----------AAQLSAGQQRRLALARLWLSRR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 490 PLLLLDEPTASLDGETEAGIVEAVR-RLAQGRTVLLVVHRPalLPLAD-RVVRL 541
Cdd:TIGR01189 147 PLWILDEPTTALDKAGVALLAGLLRaHLARGGIVLLTTHQD--LGLVEaRELRL 198
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
350-547 |
3.69e-20 |
|
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: 90.50 E-value: 3.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 350 LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATlAPERWRERIAWVPQRPYLFAG-TIAENV 428
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYDRlTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 429 RLarpdaddGAVAAALRDAGAYDFVAELPD--GAQTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETE 506
Cdd:cd03266 100 EY-------FAGLYGLKGDELTARLEELADrlGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMAT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2351811981 507 AGIVEAVRRL-AQGRTVLLVVHR-PALLPLADRVVRLEPGATL 547
Cdd:cd03266 173 RALREFIRQLrALGKCILFSTHImQEVERLCDRVVVLHRGRVV 215
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
921-1138 |
4.33e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 91.72 E-value: 4.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAERdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGL 1000
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDA--HIFDSSIRE-------NLRLARTgATDEELRAALDRARLLDWAEALPAgldtlvgehgaRLSGGQRQRLALAR 1071
Cdd:PRK13647 84 VFQDPddQVFSSTVWDdvafgpvNMGLDKD-EVERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 1072 AILADFPVLVLDEPAEHLDLATADALTADLLA-ATRGRTTVLITHRLQ-GLEAVDEVVVLEAGRVVQRG 1138
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEG 220
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
938-1146 |
4.37e-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: 91.84 E-value: 4.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 938 LDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVdacvlegdtvrgfVGLCAQDAHIFDSSIRENLR 1017
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1018 LartGATDEELR--AALDRARLLDWAEALPAGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATA- 1094
Cdd:cd03291 120 F---GVSYDEYRykSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEk 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2351811981 1095 ---DALTADLLAatrGRTTVLITHRLQGLEAVDEVVVLEAGRVVQRGPYADLTAE 1146
Cdd:cd03291 197 eifESCVCKLMA---NKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSL 248
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
350-544 |
4.52e-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: 90.41 E-value: 4.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 350 LDHASLVVDEGETVALVGPSGVGKSTLLDVVlgftapdEGRVRVGG-------VDLATLAPERWRERIAWVPQRPYLFAG 422
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAI-------SGRVEGGGttsgqilFNGQPRKPDQFQKCVAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 423 -TIAENVRLARPDADDGAVAAALRDAGAYDFVaeLPDGAQTLLGEDG-AGLSAGQRQRLALARAFLADRPLLLLDEPTAS 500
Cdd:cd03234 96 lTVRETLTYTAILRLPRKSSDAIRKKRVEDVL--LRDLALTRIGGNLvKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2351811981 501 LDGETEAGIVEAVRRLAQ-GRTVLLVVH--RPALLPLADRVVRLEPG 544
Cdd:cd03234 174 LDSFTALNLVSTLSQLARrNRIVILTIHqpRSDLFRLFDRILLLSSG 220
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
937-1145 |
4.58e-20 |
|
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: 93.24 E-value: 4.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 937 ALDsVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVdacVLEGDTVRGFV-------GLCAQDAHIFD 1009
Cdd:COG4148 15 TLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGE---VLQDSARGIFLpphrrriGYVFQEARLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1010 S-SIRENLRLARTGAtdeelRAALDRARLLDWAEALpaGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEH 1088
Cdd:COG4148 91 HlSVRGNLLYGRKRA-----PRAERRISFDEVVELL--GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 1089 LDLATADALTaDLLAATRGRTT---VLITHRLQGLEAV-DEVVVLEAGRVVQRGPYADLTA 1145
Cdd:COG4148 164 LDLARKAEIL-PYLERLRDELDipiLYVSHSLDEVARLaDHVVLLEQGRVVASGPLAEVLS 223
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
333-544 |
5.31e-20 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 87.50 E-value: 5.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGvdlatlaperwRERIAW 412
Cdd:cd03221 1 IELENLSKTYGGK--LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 413 VPQrpylfagtiaenvrlarpdaddgavaaalrdagaydfvaelpdgaqtllgedgagLSAGQRQRLALARAFLADRPLL 492
Cdd:cd03221 68 FEQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2351811981 493 LLDEPTASLDgeteagiVEAVRRLAQG-----RTVLLVVHRPALL-PLADRVVRLEPG 544
Cdd:cd03221 93 LLDEPTNHLD-------LESIEALEEAlkeypGTVILVSHDRYFLdQVATKIIELEDG 143
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
932-1132 |
6.17e-20 |
|
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: 89.70 E-value: 6.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 932 GAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREG----TYRIGGVDACVLEGDTVRGFVGLCAQDAHI 1007
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGkvhwSNKNESEPSFEATRSRNRYSVAYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1008 FDSSIRENLRLArTGATDEELRAALDRARLLDWAEALPAGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAE 1087
Cdd:cd03290 91 LNATVEENITFG-SPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2351811981 1088 HLDLATADAL-TADLLAATRG--RTTVLITHRLQGLEAVDEVVVLEAG 1132
Cdd:cd03290 170 ALDIHLSDHLmQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
163-528 |
6.76e-20 |
|
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: 96.52 E-value: 6.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 163 IIVVTLPLIPLFMILIGWATQSrmDRQWRLL-----SRLSGHFLDVVAGLPTLKVFGRAK------AQAESIRAITSQYR 231
Cdd:TIGR01271 1027 IFIAAIPVAVIFIMLRAYFLRT--SQQLKQLesearSPIFSHLITSLKGLWTIRAFGRQSyfetlfHKALNLHTANWFLY 1104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 232 RATLRTLRIAFLSSFALELLATLSVALVAVTIGmrlvHGELDLYTGLVVLILAPEAYLPIRQVgaqyhaAAEGL-SAAEE 310
Cdd:TIGR01271 1105 LSTLRWFQMRIDIIFVFFFIAVTFIAIGTNQDG----EGEVGIILTLAMNILSTLQWAVNSSI------DVDGLmRSVSR 1174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 311 IFSVL-----ETEPRRGGTADVPESL----------------RLELEGVTVRHEGRGEPSLDHASLVVDEGETVALVGPS 369
Cdd:TIGR01271 1175 VFKFIdlpqeEPRPSGGGGKYQLSTVlvienphaqkcwpsggQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRT 1254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 370 GVGKSTLLDVVLGFtAPDEGRVRVGGVDLATLAPERWRERIAWVPQRPYLFAGTIAENVRlARPDADDGAVAAALRDAGA 449
Cdd:TIGR01271 1255 GSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD-PYEQWSDEEIWKVAEEVGL 1332
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 450 YDFVAELPDGAQTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQGRTVLLVVHR 528
Cdd:TIGR01271 1333 KSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHR 1411
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
333-540 |
8.04e-20 |
|
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: 89.09 E-value: 8.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRGepSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPErWRERIAW 412
Cdd:cd03231 1 LEADELTCERDGRA--LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDS-IARGLLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 413 VPQRPYLFAG-TIAENVRLARPDADDGAVAAALRDAGAYDFvAELPdgaqtllgedGAGLSAGQRQRLALARAFLADRPL 491
Cdd:cd03231 78 LGHAPGIKTTlSVLENLRFWHADHSDEQVEEALARVGLNGF-EDRP----------VAQLSAGQQRRVALARLLLSGRPL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2351811981 492 LLLDEPTASLDGETEAGIVEAVR-RLAQGRTVLLVVHRPalLPLADRVVR 540
Cdd:cd03231 147 WILDEPTTALDKAGVARFAEAMAgHCARGGMVVLTTHQD--LGLSEAGAR 194
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
923-1142 |
8.37e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 94.36 E-value: 8.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 923 VRGLSARYAGaeRDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGT------YRIGGV--DACVLEGDTV 994
Cdd:COG0488 1 LENLSKSFGG--RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEvsipkgLRIGYLpqEPPLDDDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 995 RGFVglCAQDAHIFDSSIRENLRLARTGATDEELRAALDRARLLD----W-----AEALPAGL-------DTLVGEhgar 1058
Cdd:COG0488 79 LDTV--LDGDAELRALEAELEELEAKLAEPDEDLERLAELQEEFEalggWeaearAEEILSGLgfpeedlDRPVSE---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1059 LSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALtADLLAATRGrTTVLITH-R--LQglEAVDEVVVLEAGRVV 1135
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWL-EEFLKNYPG-TVLVVSHdRyfLD--RVATRILELDRGKLT 228
|
....*...
gi 2351811981 1136 Q-RGPYAD 1142
Cdd:COG0488 229 LyPGNYSA 236
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
921-1138 |
9.06e-20 |
|
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: 89.70 E-value: 9.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAErdaLDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTvRGFVGL 1000
Cdd:cd03299 1 LKVENLSKDWKEFK---LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK-RDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CaQDAHIF-DSSIREN----LRLARtgatdeELRAALDRaRLLDWAEALpaGLDTLVGEHGARLSGGQRQRLALARAILA 1075
Cdd:cd03299 77 P-QNYALFpHMTVYKNiaygLKKRK------VDKKEIER-KVLEIAEML--GIDHLLNRKPETLSGGEQQRVAIARALVV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2351811981 1076 DFPVLVLDEPAEHLDLATADALTADLLAATR-GRTTVL-ITHRLQGLEAV-DEVVVLEAGRVVQRG 1138
Cdd:cd03299 147 NPKILLLDEPFSALDVRTKEKLREELKKIRKeFGVTVLhVTHDFEEAWALaDKVAIMLNGKLIQVG 212
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
942-1138 |
1.14e-19 |
|
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: 88.76 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 942 DLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDacVLEGDTVRGFVGLCAQDAHIFDS-SIRENLRLar 1020
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQS--HTGLAPYQRPVSMLFQENNLFAHlTVRQNIGL-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1021 tGATDEELRAALDRARLLDWAEALpaGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTAD 1100
Cdd:TIGR01277 94 -GLHPGLKLNAEQQEKVVDAAQQV--GIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLAL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2351811981 1101 L--LAATRGRTTVLITHRLQGLEAV-DEVVVLEAGRVVQRG 1138
Cdd:TIGR01277 171 VkqLCSERQRTLLMVTHHLSDARAIaSQIAVVSQGKIKVVS 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
921-1138 |
1.17e-19 |
|
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: 88.96 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAERD--ALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDAcVLEGDTVRGFV 998
Cdd:cd03266 2 ITADALTKRFRDVKKTvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV-VKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 999 GLCAQDAHIFDS-SIRENLR-LART-GATDEELRAALDR-ARLLDWAEALpaglDTLVGEhgarLSGGQRQRLALARAIL 1074
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEyFAGLyGLKGDELTARLEElADRLGMEELL----DRRVGG----FSTGMRQKVAIARALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2351811981 1075 ADFPVLVLDEPAEHLDLATADALTaDLLAATR--GRTTVLITHRLQGLEAV-DEVVVLEAGRVVQRG 1138
Cdd:cd03266 153 HDPPVLLLDEPTTGLDVMATRALR-EFIRQLRalGKCILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
921-1143 |
1.48e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 89.59 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLD----AR-EGTYRIGGVDACVLEGDTVR 995
Cdd:PRK14247 4 IEIRDLKVSFGQVE--VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeARvSGEVYLDGQDIFKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 996 GFVGLCAQDAH-IFDSSIREN----LRLARTGATDEEL----RAALDRARLldWAEalpagLDTLVGEHGARLSGGQRQR 1066
Cdd:PRK14247 82 RRVQMVFQIPNpIPNLSIFENvalgLKLNRLVKSKKELqervRWALEKAQL--WDE-----VKDRLDAPAGKLSGGQQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2351811981 1067 LALARAILADFPVLVLDEPAEHLDLATADALTADLLAATRGRTTVLITH-RLQGLEAVDEVVVLEAGRVVQRGPYADL 1143
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
346-547 |
1.73e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 89.79 E-value: 1.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 346 GEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLaTLAPERW-RERIAWVPQRP--YLFAG 422
Cdd:PRK13647 17 GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV-NAENEKWvRSKVGLVFQDPddQVFSS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 423 TIAENVRLA------RPDADDGAVAAALRDAGAYDFVAELPdgaqtllgedgAGLSAGQRQRLALARAFLADRPLLLLDE 496
Cdd:PRK13647 96 TVWDDVAFGpvnmglDKDEVERRVEEALKAVRMWDFRDKPP-----------YHLSYGQKKRVAIAGVLAMDPDVIVLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2351811981 497 PTASLDGETEAGIVEAVRRL-AQGRTVLLVVHRPAL-LPLADRVVRLEPGATL 547
Cdd:PRK13647 165 PMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDLaAEWADQVIVLKEGRVL 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
921-1171 |
2.24e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.16 E-value: 2.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVdacVLEGDTVR----- 995
Cdd:COG1129 5 LEMRGISKSFGGVK--ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGE---PVRFRSPRdaqaa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 996 GfVGLCAQDAHIFDS-SIRENLRLARtgatdeELRAA--LDRARLLDWAEALPAGL------DTLVGEhgarLSGGQRQR 1066
Cdd:COG1129 80 G-IAIIHQELNLVPNlSVAENIFLGR------EPRRGglIDWRAMRRRARELLARLgldidpDTPVGD----LSVAQQQL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1067 LALARAILADFPVLVLDEPaehldlaTAdALTAD----LLA-----ATRGRTTVLITHRLQGLEAV-DEVVVLEAGRVVQ 1136
Cdd:COG1129 149 VEIARALSRDARVLILDEP-------TA-SLTEReverLFRiirrlKAQGVAIIYISHRLDEVFEIaDRVTVLRDGRLVG 220
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2351811981 1137 RGPYADLTAEEgpL-RRMLERE------RETEGVAEEALGVR 1171
Cdd:COG1129 221 TGPVAELTEDE--LvRLMVGREledlfpKRAAAPGEVVLEVE 260
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
303-541 |
4.42e-19 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 93.94 E-value: 4.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 303 EGLSAAEEIFSVLETEPRRGGTAD---VPESLRLELEGVTVRHEGRGEPSL-DHASLVVDEGETVALVGPSGVGKSTLLD 378
Cdd:PTZ00265 350 KSLEATNSLYEIINRKPLVENNDDgkkLKDIKKIQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILK 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 379 VVLGFTAPDEGRVRVGGV-DLATLAPERWRERIAWVPQRPYLFAGTIAENVRLA-------------------------- 431
Cdd:PTZ00265 430 LIERLYDPTEGDIIINDShNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyynedgndsqenkn 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 432 RPDADDGAVAAALRDAGA-------------------------------YDFVAELPDGAQTLLGEDGAGLSAGQRQRLA 480
Cdd:PTZ00265 510 KRNSCRAKCAGDLNDMSNttdsneliemrknyqtikdsevvdvskkvliHDFVSALPDKYETLVGSNASKLSGGQKQRIS 589
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2351811981 481 LARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLA--QGRTVLLVVHRPALLPLADRVVRL 541
Cdd:PTZ00265 590 IARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVL 652
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
932-1138 |
5.43e-19 |
|
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: 86.07 E-value: 5.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 932 GAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLaqvlLRFLDAR------EGTYRIGGVDacvLEGDTVRGFVGLCAQDA 1005
Cdd:cd03213 19 KSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTL----LNALAGRrtglgvSGEVLINGRP---LDKRSFRKIIGYVPQDD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1006 HIFDS-SIRENLRLArtgatdEELRaaldrarlldwaealpagldtlvgehgaRLSGGQRQRLALARAILADFPVLVLDE 1084
Cdd:cd03213 92 ILHPTlTVRETLMFA------AKLR----------------------------GLSGGERKRVSIALELVSNPSLLFLDE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2351811981 1085 PAEHLDLATAdALTADLLA--ATRGRTTVLITHRL--QGLEAVDEVVVLEAGRVVQRG 1138
Cdd:cd03213 138 PTSGLDSSSA-LQVMSLLRrlADTGRTIICSIHQPssEIFELFDKLLLLSQGRVIYFG 194
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
921-1147 |
5.53e-19 |
|
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: 87.20 E-value: 5.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEG-DTVRGFVG 999
Cdd:TIGR03410 1 LEVSNLNVYYGQSH--ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPhERARAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1000 LCAQDAHIFDS-SIRENLRlarTGAtdeELRAALDRARLLDWAEALPAgLDTLVGEHGARLSGGQRQRLALARAILADFP 1078
Cdd:TIGR03410 79 YVPQGREIFPRlTVEENLL---TGL---AALPRRSRKIPDEIYELFPV-LKEMLGRRGGDLSGGQQQQLAIARALVTRPK 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2351811981 1079 VLVLDEPAEHL------DLATAdaltADLLAATRGRTTVLITHRLQ-GLEAVDEVVVLEAGRVVQRGPYADLTAEE 1147
Cdd:TIGR03410 152 LLLLDEPTEGIqpsiikDIGRV----IRRLRAEGGMAILLVEQYLDfARELADRYYVMERGRVVASGAGDELDEDK 223
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
921-1147 |
5.54e-19 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 87.04 E-value: 5.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDAcVLEGDTVRGFVGL 1000
Cdd:cd03265 1 IEVENLVKKYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV-VREPREVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDAHIFDS-SIRENLRL-ART-GATDEELRAALDraRLLDWAEALPAGlDTLVGEHgarlSGGQRQRLALARAILADF 1077
Cdd:cd03265 78 VFQDLSVDDElTGWENLYIhARLyGVPGAERRERID--ELLDFVGLLEAA-DRLVKTY----SGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2351811981 1078 PVLVLDEPAEHLDLATADALTADL--LAATRGRTTVLITHRLQGLEAV-DEVVVLEAGRVVQRGpyadlTAEE 1147
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIekLKEEFGMTILLTTHYMEEAEQLcDRVAIIDHGRIIAEG-----TPEE 218
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
921-1131 |
5.73e-19 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 86.77 E-value: 5.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAR---EGTYRIGGVDacVLEGDTVRGF 997
Cdd:COG4136 2 LSLENLTITLGGRP--LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRR--LTALPAEQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 998 VGLCAQDAHIFDS-SIRENLRLARTGATDEELR-----AALDRARLLDWAEALPAgldtlvgehgaRLSGGQRQRLALAR 1071
Cdd:COG4136 78 IGILFQDDLLFPHlSVGENLAFALPPTIGRAQRrarveQALEEAGLAGFADRDPA-----------TLSGGQRARVALLR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2351811981 1072 AILADFPVLVLDEPAEHLDLatadALTADLL------AATRGRTTVLITHRLQGLEAVDEVVVLEA 1131
Cdd:COG4136 147 ALLAEPRALLLDEPFSKLDA----ALRAQFRefvfeqIRQRGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
350-527 |
6.04e-19 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 87.46 E-value: 6.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 350 LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVD-LATLAPERW-RERIAWVPQRPYLFAGTIA-E 426
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKvNDPKVDERLiRQEAGMVFQQFYLFPHLTAlE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 427 NVRLArpdaddgavAAALRDAGAydfvAELPDGAQTLLGEDG---------AGLSAGQRQRLALARAfLADRP-LLLLDE 496
Cdd:PRK09493 97 NVMFG---------PLRVRGASK----EEAEKQARELLAKVGlaerahhypSELSGGQQQRVAIARA-LAVKPkLMLFDE 162
|
170 180 190
....*....|....*....|....*....|..
gi 2351811981 497 PTASLDGETEAGIVEAVRRLA-QGRTVLLVVH 527
Cdd:PRK09493 163 PTSALDPELRHEVLKVMQDLAeEGMTMVIVTH 194
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
338-544 |
6.24e-19 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 89.79 E-value: 6.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 338 VTVRHEGR-GEPSLDhASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLAT------LAPERwrERI 410
Cdd:TIGR02142 1 LSARFSKRlGDFSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEK--RRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 411 AWVPQRPYLFAG-TIAENVRLARPDADDGAVAAalrdagAYDFVAELPdGAQTLLGEDGAGLSAGQRQRLALARAFLADR 489
Cdd:TIGR02142 78 GYVFQEARLFPHlSVRGNLRYGMKRARPSERRI------SFERVIELL-GIGHLLGRLPGRLSGGEKQRVAIGRALLSSP 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2351811981 490 PLLLLDEPTASLDGETEAGIVEAVRRLAQ--GRTVLLVVHRPA-LLPLADRVVRLEPG 544
Cdd:TIGR02142 151 RLLLMDEPLAALDDPRKYEILPYLERLHAefGIPILYVSHSLQeVLRLADRVVVLEDG 208
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
346-553 |
6.34e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 90.28 E-value: 6.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 346 GEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPerWRERIAWVPQRPYLFAG-TI 424
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP--YQRPINMMFQSYALFPHmTV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 425 AENVRLARPDADDGAVAAALRDAGAYDFVAelpdgAQTLLGEDGAGLSAGQRQRLALARAfLADRP-LLLLDEPTASLDG 503
Cdd:PRK11607 109 EQNIAFGLKQDKLPKAEIASRVNEMLGLVH-----MQEFAKRKPHQLSGGQRQRVALARS-LAKRPkLLLLDEPMGALDK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2351811981 504 E----TEAGIVEAVRRLaqGRTVLLVVH-RPALLPLADRVVRLEPGATLRPEKPE 553
Cdd:PRK11607 183 KlrdrMQLEVVDILERV--GVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPE 235
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
926-1145 |
8.69e-19 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 89.40 E-value: 8.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 926 LSARYAGAERDaldsVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVdaCVLEGD------TVRGFVG 999
Cdd:TIGR02142 5 FSKRLGDFSLD----ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGR--TLFDSRkgiflpPEKRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1000 LCAQDAHIFDS-SIRENLRLARTGATDEELRAALDR-ARLLdwaealpaGLDTLVGEHGARLSGGQRQRLALARAILADF 1077
Cdd:TIGR02142 79 YVFQEARLFPHlSVRGNLRYGMKRARPSERRISFERvIELL--------GIGHLLGRLPGRLSGGEKQRVAIGRALLSSP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 1078 PVLVLDEPAEHLDLATADALTADL--LAATRGRTTVLITHRLQGLEAV-DEVVVLEAGRVVQRGPYADLTA 1145
Cdd:TIGR02142 151 RLLLMDEPLAALDDPRKYEILPYLerLHAEFGIPILYVSHSLQEVLRLaDRVVVLEDGRVAAAGPIAEVWA 221
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
921-1156 |
9.42e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 87.43 E-value: 9.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARY-------AGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDT 993
Cdd:PRK10419 4 LNVSGLSHHYahgglsgKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 994 VRGF---VGLCAQDA-------HIFDSSIRENLR-LARTGATDEELRAaldrARLLDWAEALPAGLDTLVGEhgarLSGG 1062
Cdd:PRK10419 84 RKAFrrdIQMVFQDSisavnprKTVREIIREPLRhLLSLDKAERLARA----SEMLRAVDLDDSVLDKRPPQ----LSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1063 QRQRLALARAILADFPVLVLDEPAEHLDL---ATADALTADLLAATrGRTTVLITHRLQGLEA-VDEVVVLEAGRVVQRG 1138
Cdd:PRK10419 156 QLQRVCLARALAVEPKLLILDEAVSNLDLvlqAGVIRLLKKLQQQF-GTACLFITHDLRLVERfCQRVMVMDNGQIVETQ 234
|
250
....*....|....*...
gi 2351811981 1139 PYADLTAEEGPLRRMLER 1156
Cdd:PRK10419 235 PVGDKLTFSSPAGRVLQN 252
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
921-1137 |
1.10e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 87.22 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAG--AERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVdacVLEG-DTVRGF 997
Cdd:COG4525 4 LTVRHVSVRYPGggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV---PVTGpGADRGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 998 VglcAQDAHIFD-SSIREN----LRLARTGATDEELRAA--LDRARLLDWAEALPAgldtlvgehgaRLSGGQRQRLALA 1070
Cdd:COG4525 81 V---FQKDALLPwLNVLDNvafgLRLRGVPKAERRARAEelLALVGLADFARRRIW-----------QLSGGMRQRVGIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 1071 RAILADFPVLVLDEPAEHLDLATADALTADLL--AATRGRTTVLITHRLQglEAV---DEVVVLEA--GRVVQR 1137
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDALTREQMQELLLdvWQRTGKGVFLITHSVE--EALflaTRLVVMSPgpGRIVER 218
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
921-1135 |
1.95e-18 |
|
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: 83.63 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGvdacvlegdtvrgfvgl 1000
Cdd:cd03216 1 LELRGITKRFGGVK--ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG----------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 caqdahifdssirenlrlartgatdeelraalDRARLLDWAEALPAGLDTLvgehgARLSGGQRQRLALARAILADFPVL 1080
Cdd:cd03216 62 --------------------------------KEVSFASPRDARRAGIAMV-----YQLSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2351811981 1081 VLDEPAEHLDLATADAL--TADLLAAtRGRTTVLITHRLQGLEAV-DEVVVLEAGRVV 1135
Cdd:cd03216 105 ILDEPTAALTPAEVERLfkVIRRLRA-QGVAVIFISHRLDEVFEIaDRVTVLRDGRVV 161
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
332-528 |
2.12e-18 |
|
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: 86.83 E-value: 2.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 332 RLELEGVTVRHEGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPdEGRVRVGGVDLATLAPERWRERIA 411
Cdd:cd03289 2 QMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 412 WVPQRPYLFAGTIAENVRlARPDADDGAVAAALRDAGAYDFVAELPDGAQTLLGEDGAGLSAGQRQRLALARAFLADRPL 491
Cdd:cd03289 81 VIPQKVFIFSGTFRKNLD-PYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 2351811981 492 LLLDEPTASLDGETEAGIVEAVRRLAQGRTVLLVVHR 528
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHR 196
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
938-1147 |
2.22e-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: 91.51 E-value: 2.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 938 LDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVdacvlegdtvrgfVGLCAQDAHIFDSSIRENLR 1017
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1018 LartGATDEELR--AALDRARLLDWAEALPAGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLAT-A 1094
Cdd:TIGR01271 509 F---GLSYDEYRytSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTeK 585
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2351811981 1095 DALTADLLAATRGRTTVLITHRLQGLEAVDEVVVLEAGRVVQRGPYADLTAEE 1147
Cdd:TIGR01271 586 EIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
942-1154 |
2.32e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 85.40 E-value: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 942 DLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDaCVLEGDTVRGfVGLCAQDAHIFDS-SIREN----- 1015
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSRRP-VSMLFQENNLFSHlTVAQNiglgl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1016 ---LRLarTGATDEELRAALDRARLLDWAEALPagldtlvgehgARLSGGQRQRLALARAILADFPVLVLDEPAEHLDla 1092
Cdd:PRK10771 97 npgLKL--NAAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALD-- 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 1093 taDALTADLLA------ATRGRTTVLITHRLQ-GLEAVDEVVVLEAGRVVQRGPYADLTAEEGPLRRML 1154
Cdd:PRK10771 162 --PALRQEMLTlvsqvcQERQLTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLSGKASASALL 228
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
330-553 |
2.42e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 87.96 E-value: 2.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 330 SLRLELEGVTVRHegRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGV---DLATLAperw 406
Cdd:PRK13536 39 TVAIDLAGVSKSY--GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVpvpARARLA---- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 407 RERIAWVPQRPYL-FAGTIAENVRLARPDADDGAVAAALRDAGAYDFvAELPDGAQTLLGEdgagLSAGQRQRLALARAF 485
Cdd:PRK13536 113 RARIGVVPQFDNLdLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEF-ARLESKADARVSD----LSGGMKRRLTLARAL 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 486 LADRPLLLLDEPTASLDGETEAGIVEAVRR-LAQGRTVLLVVH-RPALLPLADRVVRLEPGATLRPEKPE 553
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHfMEEAERLCDRLCVLEAGRKIAEGRPH 257
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
350-561 |
2.59e-18 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 85.21 E-value: 2.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 350 LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERwreriAWVPQRPYLFAG-TIAENV 428
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDR-----MVVFQNYSLLPWlTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 429 RLA----RPDADDGAVAAALRDagAYDFVAeLPDGAQTLLGEdgagLSAGQRQRLALARAfLADRP-LLLLDEPTASLDG 503
Cdd:TIGR01184 76 ALAvdrvLPDLSKSERRAIVEE--HIALVG-LTEAADKRPGQ----LSGGMKQRVAIARA-LSIRPkVLLLDEPFGALDA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2351811981 504 ETEAGIVEAVRRLAQ--GRTVLLVVH--RPALLpLADRVVRLEPGatlrPEKPEG---SVAVPRP 561
Cdd:TIGR01184 148 LTRGNLQEELMQIWEehRVTVLMVTHdvDEALL-LSDRVVMLTNG----PAANIGqilEVPFPRP 207
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
333-538 |
2.76e-18 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 84.50 E-value: 2.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTA--PDEGRVRVGGVDLATLAP-ERWRER 409
Cdd:cd03217 1 LEIKDLHVSVGGK--EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPeERARLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 410 IAWVPQRPYLFAGtiaenVRLArpdaddgavaaalrdagayDFVAELpdgaqtllgedGAGLSAGQRQRLALARAFLADR 489
Cdd:cd03217 79 IFLAFQYPPEIPG-----VKNA-------------------DFLRYV-----------NEGFSGGEKKRNEILQLLLLEP 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2351811981 490 PLLLLDEPTASLDGETEAGIVEAVRRLA-QGRTVLLVVHRPALLPL--ADRV 538
Cdd:cd03217 124 DLAILDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHYQRLLDYikPDRV 175
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
356-556 |
2.77e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 90.11 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 356 VVDEGETVALVGPSGVGKSTLLDVVLGFTAPdeGRVRVGGVDLATLAPERW--RERIAWVPQRPyLFAGT--------IA 425
Cdd:TIGR00955 47 VAKPGELLAVMGSSGAGKTTLMNALAFRSPK--GVKGSGSVLLNGMPIDAKemRAISAYVQQDD-LFIPTltvrehlmFQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 426 ENVRLARPDADDGAVAA---ALRDAGaydfvaeLPDGAQTLLGEDGA--GLSAGQRQRLALARAFLADRPLLLLDEPTAS 500
Cdd:TIGR00955 124 AHLRMPRRVTKKEKRERvdeVLQALG-------LRKCANTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 501 LDGETEAGIVEAVRRLAQ-GRTVLLVVHRPA--LLPLADRVVRLEPGATLRPEKPEGSV 556
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGLAQkGKTIICTIHQPSseLFELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
920-1146 |
3.77e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 88.36 E-value: 3.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 920 PLEVRGLSARYAGAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVG 999
Cdd:PRK09536 3 MIDVSDLSVEFGDTT--VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1000 LCAQDAHI-FDSSIRENLRLART------GATDEELRAALDRArlldwaeALPAGLDTLVGEHGARLSGGQRQRLALARA 1072
Cdd:PRK09536 81 SVPQDTSLsFEFDVRQVVEMGRTphrsrfDTWTETDRAAVERA-------MERTGVAQFADRPVTSLSGGERQRVLLARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1073 ILADFPVLVLDEPAEHLDLATAD---ALTADLlaATRGRTTVLITHRLQgLEA--VDEVVVLEAGRVVQRGPYAD-LTAE 1146
Cdd:PRK09536 154 LAQATPVLLLDEPTASLDINHQVrtlELVRRL--VDDGKTAVAAIHDLD-LAAryCDELVLLADGRVRAAGPPADvLTAD 230
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
354-527 |
3.77e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 85.60 E-value: 3.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 354 SLVVDEGETVALVGPSGVGKSTLL-------DVVLGFTApdEGRVRVGGVDL--ATLAPERWRERIAWVPQRPYLFAGTI 424
Cdd:PRK14243 30 WLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGFRV--EGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPKSI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 425 AENVRL-AR----PDADDGAVAAALRDAGAYDfvaELPDGaqtlLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTA 499
Cdd:PRK14243 108 YDNIAYgARingyKGDMDELVERSLRQAALWD---EVKDK----LKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCS 180
|
170 180
....*....|....*....|....*...
gi 2351811981 500 SLDGETEAGIVEAVRRLAQGRTVLLVVH 527
Cdd:PRK14243 181 ALDPISTLRIEELMHELKEQYTIIIVTH 208
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
350-527 |
4.13e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 86.40 E-value: 4.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 350 LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPeRWRERIAWVPQRPYLFAG-TIAENV 428
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRAR-HARQRVGVVPQFDNLDPDfTVRENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 429 RLARPDADDGAVAAALRDAGAYDFvAELPDGAQTLLGEdgagLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEAG 508
Cdd:PRK13537 102 LVFGRYFGLSAAAARALVPPLLEF-AKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHL 176
|
170 180
....*....|....*....|
gi 2351811981 509 IVEAVRRL-AQGRTVLLVVH 527
Cdd:PRK13537 177 MWERLRSLlARGKTILLTTH 196
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
332-539 |
6.42e-18 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 82.87 E-value: 6.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 332 RLELEGVTVRHegrgepSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRER-I 410
Cdd:cd03215 4 VLEVRGLSVKG------AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 411 AWVP---QRPYLFAG-TIAENVRLARpdaddgavaaalrdagaydfvaelpdgaqtllgedgaGLSAGQRQRLALARAFL 486
Cdd:cd03215 78 AYVPedrKREGLVLDlSVAENIALSS-------------------------------------LLSGGNQQKVVLARWLA 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2351811981 487 ADRPLLLLDEPTASLDGETEAGIVEAVRRLA-QGRTVLLVVHR-PALLPLADRVV 539
Cdd:cd03215 121 RDPRVLILDEPTRGVDVGAKAEIYRLIRELAdAGKAVLLISSElDELLGLCDRIL 175
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
921-1139 |
7.83e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 86.92 E-value: 7.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDacvlegdtvrgFVGL 1000
Cdd:PRK09452 15 VELRGISKSFDGKE--VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQD-----------ITHV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDAHI---FDS-------SIREN----LRLARTGATDEELRA--ALDRARLLDWAEALPAgldtlvgehgaRLSGGQR 1064
Cdd:PRK09452 82 PAENRHVntvFQSyalfphmTVFENvafgLRMQKTPAAEITPRVmeALRMVQLEEFAQRKPH-----------QLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2351811981 1065 QRLALARAILADFPVLVLDEPAEHLDLATADALTADLLAATR--GRTTVLITH-RLQGLEAVDEVVVLEAGRVVQRGP 1139
Cdd:PRK09452 151 QRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
921-1133 |
8.71e-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: 81.34 E-value: 8.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGaeRDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGgvdacvlegdtvrgfvgl 1000
Cdd:cd03221 1 IELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG------------------ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 caqdahifdssirENLRLArtgatdeelraaldrarlldwaealpagldtlvgeHGARLSGGQRQRLALARAILADFPVL 1080
Cdd:cd03221 61 -------------STVKIG-----------------------------------YFEQLSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 1081 VLDEPAEHLDLATADALtADLLAATRGrTTVLITHRLQGLEAV-DEVVVLEAGR 1133
Cdd:cd03221 93 LLDEPTNHLDLESIEAL-EEALKEYPG-TVILVSHDRYFLDQVaTKIIELEDGK 144
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
334-527 |
9.26e-18 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 86.01 E-value: 9.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 334 ELEGVTVRHEGRGEP--SLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPE---RWRE 408
Cdd:PRK11153 3 ELKNISKVFPQGGRTihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKelrKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 409 RIAWVPQRPYLFAG-TIAENVRLArpdaddgavaaaLRDAGA-----YDFVAELPDgaqtLLG-EDG-----AGLSAGQR 476
Cdd:PRK11153 83 QIGMIFQHFNLLSSrTVFDNVALP------------LELAGTpkaeiKARVTELLE----LVGlSDKadrypAQLSGGQK 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 477 QRLALARAfLADRPLLLL-DEPTASLDGETEAGIVEAVRRLAQ--GRTVLLVVH 527
Cdd:PRK11153 147 QRVAIARA-LASNPKVLLcDEATSALDPATTRSILELLKDINRelGLTIVLITH 199
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
921-1138 |
1.19e-17 |
|
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: 82.65 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGaeRDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRgfVGl 1000
Cdd:cd03268 1 LKTNDLTKTYGK--KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR--IG- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDAHIF--DSSIRENLRLART--GATDEELRAALDRArlldwaealpaGLDTLVGEHGARLSGGQRQRLALARAILAD 1076
Cdd:cd03268 76 ALIEAPGFypNLTARENLRLLARllGIRKKRIDEVLDVV-----------GLKDSAKKKVKGFSLGMKQRLGIALALLGN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 1077 FPVLVLDEPAEHLDLATADALTADLLA-ATRGRTTVLITHRLQGLEAV-DEVVVLEAGRVVQRG 1138
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELILSlRDQGITVLISSHLLSEIQKVaDRIGIINKGKLIEEG 208
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
921-1146 |
1.22e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 84.03 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVdacvlEGDTVRGF--- 997
Cdd:PRK11264 4 IEVKNLVKKFHGQT--VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDI-----TIDTARSLsqq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 998 ----------VGLCAQDAHIF-DSSIRENLRLARTGATDEELRAALDRARLLdwaeALPAGLDTLVGEHGARLSGGQRQR 1066
Cdd:PRK11264 77 kglirqlrqhVGFVFQNFNLFpHRTVLENIIEGPVIVKGEPKEEATARAREL----LAKVGLAGKETSYPRRLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1067 LALARAILADFPVLVLDEPAEHLDlataDALTADLLAATRG-----RTTVLITHRLQ-GLEAVDEVVVLEAGRVVQRGPY 1140
Cdd:PRK11264 153 VAIARALAMRPEVILFDEPTSALD----PELVGEVLNTIRQlaqekRTMVIVTHEMSfARDVADRAIFMDQGRIVEQGPA 228
|
....*.
gi 2351811981 1141 ADLTAE 1146
Cdd:PRK11264 229 KALFAD 234
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
349-527 |
1.52e-17 |
|
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: 82.80 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 349 SLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDlATLAPERWRERIAWVPQRPYLFAG-TIAEN 427
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHD-VVREPREVRRRIGIVFQDLSVDDElTGWEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 428 VRLARPDADDGAVAAALRDAGAYDFVaELPDGAQTLLGEdgagLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEA 507
Cdd:cd03265 94 LYIHARLYGVPGAERRERIDELLDFV-GLLEAADRLVKT----YSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRA 168
|
170 180
....*....|....*....|..
gi 2351811981 508 GIVEAVRRL--AQGRTVLLVVH 527
Cdd:cd03265 169 HVWEYIEKLkeEFGMTILLTTH 190
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
920-1146 |
1.76e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 83.52 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 920 PLEVRGLSARYaGAERdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVL---------- 989
Cdd:PRK11231 2 TLRTENLTVGY-GTKR-ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLssrqlarrla 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 990 ---------EGDTVRGFVGlcaqdahiFDSSIRENLrLARTGATDEELraaldrarlLDWAEAlPAGLDTLVGEHGARLS 1060
Cdd:PRK11231 80 llpqhhltpEGITVRELVA--------YGRSPWLSL-WGRLSAEDNAR---------VNQAME-QTRINHLADRRLTDLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1061 GGQRQRLALARAILADFPVLVLDEPAEHLDLATadalTADLLAATR-----GRTTVLITHRL-QGLEAVDEVVVLEAGRV 1134
Cdd:PRK11231 141 GGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINH----QVELMRLMRelntqGKTVVTVLHDLnQASRYCDHLVVLANGHV 216
|
250
....*....|...
gi 2351811981 1135 VQRG-PYADLTAE 1146
Cdd:PRK11231 217 MAQGtPEEVMTPG 229
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
355-541 |
1.77e-17 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 82.59 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 355 LVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVdlatlAPERWRERIAWVPQR---PYLFAGTIAENVRLA 431
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGA-----SPGKGWRHIGYVPQRhefAWDFPISVAHTVMSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 432 RpdaddGAVAAALRDAGAYDFVA--------ELPDGAQTLLGEdgagLSAGQRQRLALARAfLADRP-LLLLDEPTASLD 502
Cdd:TIGR03771 76 R-----TGHIGWLRRPCVADFAAvrdalrrvGLTELADRPVGE----LSGGQRQRVLVARA-LATRPsVLLLDEPFTGLD 145
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2351811981 503 GETEAGIVEAVRRLAQ-GRTVLLVVHR-PALLPLADRVVRL 541
Cdd:TIGR03771 146 MPTQELLTELFIELAGaGTAILMTTHDlAQAMATCDRVVLL 186
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
332-539 |
1.89e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 88.55 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 332 RLELEGVTVRHEGRGE-PSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGF--------------------------- 383
Cdd:PTZ00265 1165 KIEIMDVNFRYISRPNvPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtndmtneqdyqg 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 384 ---------------------------TAPDEGRVRVGGVDLATLAPERWRERIAWVPQRPYLFAGTIAENVRLARPDAD 436
Cdd:PTZ00265 1245 deeqnvgmknvnefsltkeggsgedstVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDAT 1324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 437 DGAVAAALRDAGAYDFVAELPDGAQTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRL 516
Cdd:PTZ00265 1325 REDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDI 1404
|
250 260
....*....|....*....|....*
gi 2351811981 517 AQ--GRTVLLVVHRPALLPLADRVV 539
Cdd:PTZ00265 1405 KDkaDKTIITIAHRIASIKRSDKIV 1429
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
921-1138 |
2.06e-17 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 83.14 E-value: 2.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLlRFLD-AREGTYRIGG------VDACVLEGDT 993
Cdd:COG4161 3 IQLKNINCFYGSHQ--ALFDINLECPSGETLVLLGPSGAGKSSLLRVL-NLLEtPDSGQLNIAGhqfdfsQKPSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 994 VRGFVGLCAQDAHIFDS-SIRENLRLART---GATDEELRAA----LDRARLLDWAEALPAgldtlvgehgaRLSGGQRQ 1065
Cdd:COG4161 80 LRQKVGMVFQQYNLWPHlTVMENLIEAPCkvlGLSKEQAREKamklLARLRLTDKADRFPL-----------HLSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1066 RLALARAILADFPVLVLDEPAEHLDlataDALTADL------LAATrGRTTVLITHRLQGLEAV-DEVVVLEAGRVVQRG 1138
Cdd:COG4161 149 RVAIARALMMEPQVLLFDEPTAALD----PEITAQVveiireLSQT-GITQVIVTHEVEFARKVaSQVVYMEKGRIIEQG 223
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
919-1139 |
2.53e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 82.97 E-value: 2.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 919 FPLEVRGLSARYAGAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFL----DAR-EGTYRIGGVDACVLEGDT 993
Cdd:PRK14267 3 FAIETVNLRVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneEARvEGEVRLFGRNIYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 994 --VRGFVGLCAQDAHIFDS-SIRENL-------RLART-GATDEELRAALDRARLldWAEalpagLDTLVGEHGARLSGG 1062
Cdd:PRK14267 81 ieVRREVGMVFQYPNPFPHlTIYDNVaigvklnGLVKSkKELDERVEWALKKAAL--WDE-----VKDRLNDYPSNLSGG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2351811981 1063 QRQRLALARAILADFPVLVLDEPAEHLDLATADALTADLLAATRGRTTVLITHR-LQGLEAVDEVVVLEAGRVVQRGP 1139
Cdd:PRK14267 154 QRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGP 231
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
333-544 |
2.75e-17 |
|
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: 81.94 E-value: 2.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHegRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAperwRERIAW 412
Cdd:cd03269 1 LEVENVTKRF--GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 413 VPQRPYLFAG-TIAENVR-LARpdADDGAVAAALRDAGAYDFVAELPDGAQTLLGEdgagLSAGQRQRLALARAFLADRP 490
Cdd:cd03269 75 LPEERGLYPKmKVIDQLVyLAQ--LKGLKKEEARRRIDEWLERLELSEYANKRVEE----LSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2351811981 491 LLLLDEPTASLDGETEAGIVEAVRRLA-QGRTVLLVVHRPALLP-LADRVVRLEPG 544
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELArAGKTVILSTHQMELVEeLCDRVLLLNKG 204
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
333-596 |
2.81e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 82.80 E-value: 2.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLaperwRERIAW 412
Cdd:PRK11247 13 LLLNAVSKRYGER--TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 413 VPQRPYLFA-GTIAENVRLARPDADDGAVAAALRDAGAYDFVAELPdgaqtllgedgAGLSAGQRQRLALARAfLADRP- 490
Cdd:PRK11247 86 MFQDARLLPwKKVIDNVGLGLKGQWRDAALQALAAVGLADRANEWP-----------AALSGGQKQRVALARA-LIHRPg 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 491 LLLLDEPTASLDGETEAGIVEAVRRLAQ--GRTVLLVVHRPA-LLPLADRVVRLEPGATlrpeKPEGSVAVPRPADASAA 567
Cdd:PRK11247 154 LLLLDEPLGALDALTRIEMQDLIESLWQqhGFTVLLVTHDVSeAVAMADRVLLIEEGKI----GLDLTVDLPRPRRRGSA 229
|
250 260
....*....|....*....|....*....
gi 2351811981 568 GRAAVpEPETLRDTAARPGQVLARVREAA 596
Cdd:PRK11247 230 RLAEL-EAEVLQRVMSRGESEPTRLRWAG 257
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
937-1139 |
2.82e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 84.25 E-value: 2.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 937 ALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTV---RGFVGLCAQDAHifdSSIr 1013
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQkllRQKIQIVFQNPY---GSL- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1014 eNLRlARTGATDEE-------LRAALDRARLLDWAEALpaGLDTlvgEHGAR----LSGGQRQRLALARAILADFPVLVL 1082
Cdd:PRK11308 106 -NPR-KKVGQILEEpllintsLSAAERREKALAMMAKV--GLRP---EHYDRyphmFSGGQRQRIAIARALMLDPDVVVA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 1083 DEPAEHLDL---ATADALTADlLAATRGRTTVLITHRLQGLEAV-DEVVVLEAGRVVQRGP 1139
Cdd:PRK11308 179 DEPVSALDVsvqAQVLNLMMD-LQQELGLSYVFISHDLSVVEHIaDEVMVMYLGRCVEKGT 238
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
920-1134 |
2.83e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 82.80 E-value: 2.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 920 PLEVRGLSARYAgaERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFvg 999
Cdd:PRK11247 12 PLLLNAVSKRYG--ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRLMF-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1000 lcaQDAHIFD-SSIRENLRLARTGATDEELRAALDRARLLDWAEALPAGLdtlvgehgarlSGGQRQRLALARAILADFP 1078
Cdd:PRK11247 88 ---QDARLLPwKKVIDNVGLGLKGQWRDAALQALAAVGLADRANEWPAAL-----------SGGQKQRVALARALIHRPG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2351811981 1079 VLVLDEPaehldLATADALT----ADL---LAATRGRTTVLITHRLQglEAV---DEVVVLEAGRV 1134
Cdd:PRK11247 154 LLLLDEP-----LGALDALTriemQDLiesLWQQHGFTVLLVTHDVS--EAVamaDRVLLIEEGKI 212
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
354-544 |
3.12e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 82.37 E-value: 3.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 354 SLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGG--VDLATLAPER----WRERIAWVPQR----PYLfagT 423
Cdd:PRK11124 22 TLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhFDFSKTPSDKaireLRRNVGMVFQQynlwPHL---T 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 424 IAENVRLArPDADDGavaaaLRDAGAYDFVAELpdgAQTLLGEDGAG-----LSAGQRQRLALARAFLADRPLLLLDEPT 498
Cdd:PRK11124 99 VQQNLIEA-PCRVLG-----LSKDQALARAEKL---LERLRLKPYADrfplhLSGGQQQRVAIARALMMEPQVLLFDEPT 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2351811981 499 ASLDGETEAGIVEAVRRLAQ-GRTVLLVVHRPALL-PLADRVVRLEPG 544
Cdd:PRK11124 170 AALDPEITAQIVSIIRELAEtGITQVIVTHEVEVArKTASRVVYMENG 217
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
915-1147 |
3.75e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 83.70 E-value: 3.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 915 PASPFPLEVRGLSARYAgaERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGvDACVLEGDTV 994
Cdd:PRK13537 2 PMSVAPIDFRNVEKRYG--DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG-EPVPSRARHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 995 RGFVGLCAQ-DAHIFDSSIRENLRL-ART-GATDEELRAALdrARLLDWAEaLPAGLDTLVGEhgarLSGGQRQRLALAR 1071
Cdd:PRK13537 79 RQRVGVVPQfDNLDPDFTVRENLLVfGRYfGLSAAAARALV--PPLLEFAK-LENKADAKVGE----LSGGMKRRLTLAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 1072 AILADFPVLVLDEPAEHLDlATADALTADLLAA--TRGRTTVLITHRLQGLEAV-DEVVVLEAGRVVQRGPYADLTAEE 1147
Cdd:PRK13537 152 ALVNDPDVLVLDEPTTGLD-PQARHLMWERLRSllARGKTILLTTHFMEEAERLcDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
341-550 |
4.01e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 81.75 E-value: 4.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 341 RHEGRGEPS---LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRE----RIAWV 413
Cdd:PRK10584 14 KSVGQGEHElsiLTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKlrakHVGFV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 414 PQRPYLFAGTIA-ENVRLarPDADDGAVAAALRDaGAYDFVAELpdGAQTLLGEDGAGLSAGQRQRLALARAFLADRPLL 492
Cdd:PRK10584 94 FQSFMLIPTLNAlENVEL--PALLRGESSRQSRN-GAKALLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 493 LLDEPTASLDGETEAGIVEAVRRLAQ--GRTVLLVVHRPALLPLADRVVRLEPGaTLRPE 550
Cdd:PRK10584 169 FADEPTGNLDRQTGDKIADLLFSLNRehGTTLILVTHDLQLAARCDRRLRLVNG-QLQEE 227
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
350-531 |
4.67e-17 |
|
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: 80.54 E-value: 4.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 350 LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGG--VDLATLAPERWRERIAWVPQRP--YLFAGTIA 425
Cdd:TIGR01166 8 LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGepLDYSRKGLLERRQRVGLVFQDPddQLFAADVD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 426 ENVRLArpdaddgavaaALRDAGAYDFVAELPDGAQTLLGEDGAG------LSAGQRQRLALARAfLADRP-LLLLDEPT 498
Cdd:TIGR01166 88 QDVAFG-----------PLNLGLSEAEVERRVREALTAVGASGLRerpthcLSGGEKKRVAIAGA-VAMRPdVLLLDEPT 155
|
170 180 190
....*....|....*....|....*....|....
gi 2351811981 499 ASLDGETEAGIVEAVRRL-AQGRTVLLVVHRPAL 531
Cdd:TIGR01166 156 AGLDPAGREQMLAILRRLrAEGMTVVISTHDVDL 189
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
334-527 |
5.03e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 82.05 E-value: 5.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 334 ELEGVTVRHegRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERIAWV 413
Cdd:COG4604 3 EIKNVSKRY--GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 414 PQRPYLfagtiaeNVRL---------------ARPDAddgavaaalRD----AGAYDFVaELPDGAQTLLGEdgagLSAG 474
Cdd:COG4604 81 RQENHI-------NSRLtvrelvafgrfpyskGRLTA---------EDreiiDEAIAYL-DLEDLADRYLDE----LSGG 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 475 QRQrlalaRAFLA-----DRPLLLLDEPTASLDGETEAGIVEAVRRLA--QGRTVLLVVH 527
Cdd:COG4604 140 QRQ-----RAFIAmvlaqDTDYVLLDEPLNNLDMKHSVQMMKLLRRLAdeLGKTVVIVLH 194
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
350-527 |
5.84e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 81.98 E-value: 5.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 350 LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERIAWVPQRPYLFAG-TIAENV 428
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVRELV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 429 RLARPDADDGAVAAALRD------AGAYDFVAELpdgAQTLLGEdgagLSAGQRQRLALARAFLADRPLLLLDEPTASLD 502
Cdd:PRK11231 98 AYGRSPWLSLWGRLSAEDnarvnqAMEQTRINHL---ADRRLTD----LSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD 170
|
170 180
....*....|....*....|....*.
gi 2351811981 503 GETEAGIVEAVRRL-AQGRTVLLVVH 527
Cdd:PRK11231 171 INHQVELMRLMRELnTQGKTVVTVLH 196
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
332-539 |
5.89e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 85.46 E-value: 5.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 332 RLELEGVTVRHegrgePS---LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRE 408
Cdd:COG3845 5 ALELRGITKRF-----GGvvaNDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 409 R-IAWVPQRPYLFAG-TIAENVRLARPdaddGAVAAALRDAGAYDFVAEL---------PDgaqTLLGEdgagLSAGQRQ 477
Cdd:COG3845 80 LgIGMVHQHFMLVPNlTVAENIVLGLE----PTKGGRLDRKAARARIRELserygldvdPD---AKVED----LSVGEQQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2351811981 478 RLALARAFLADRPLLLLDEPTASL-DGETEAgIVEAVRRL-AQGRTVLLVVHRpalLP----LADRVV 539
Cdd:COG3845 149 RVEILKALYRGARILILDEPTAVLtPQEADE-LFEILRRLaAEGKSIIFITHK---LRevmaIADRVT 212
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
365-553 |
6.03e-17 |
|
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: 83.31 E-value: 6.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 365 LVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERwrERIAWVPQRPYLFAG-TIAENVRLARPDADDGAVAAA 443
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHL--RHINMVFQSYALFPHmTVEENVAFGLKMRKVPRAEIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 444 LRDAGAYDFVaELPDGAQTLLGEdgagLSAGQRQRLALARAfLADRP-LLLLDEPTASLDGETEAGIVEAVRRLAQ--GR 520
Cdd:TIGR01187 79 PRVLEALRLV-QLEEFADRKPHQ----LSGGQQQRVALARA-LVFKPkILLLDEPLSALDKKLRDQMQLELKTIQEqlGI 152
|
170 180 190
....*....|....*....|....*....|....
gi 2351811981 521 TVLLVVH-RPALLPLADRVVRLEPGATLRPEKPE 553
Cdd:TIGR01187 153 TFVFVTHdQEEAMTMSDRIAIMRKGKIAQIGTPE 186
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
350-510 |
8.17e-17 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 82.86 E-value: 8.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 350 LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRE---RIAWVPQRPY-------L 419
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPlrrRMQMVFQDPYaslnprmT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 420 FAGTIAENVRLARpdaddgavaaALRDAGAYDFVAEL-------PDGAQTLLGEdgagLSAGQRQRLALARAfLADRP-L 491
Cdd:COG4608 114 VGDIIAEPLRIHG----------LASKAERRERVAELlelvglrPEHADRYPHE----FSGGQRQRIGIARA-LALNPkL 178
|
170
....*....|....*....
gi 2351811981 492 LLLDEPTASLDGETEAGIV 510
Cdd:COG4608 179 IVCDEPVSALDVSIQAQVL 197
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
354-544 |
8.77e-17 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 81.21 E-value: 8.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 354 SLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGG--VDLATLAPER----WRERIAWVPQR----PYLfagT 423
Cdd:COG4161 22 NLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqFDFSQKPSEKairlLRQKVGMVFQQynlwPHL---T 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 424 IAENVrLARPdaddgavaaaLRDAGAYDFVAElpDGAQTLLG----EDGAG-----LSAGQRQRLALARAFLADRPLLLL 494
Cdd:COG4161 99 VMENL-IEAP----------CKVLGLSKEQAR--EKAMKLLArlrlTDKADrfplhLSGGQQQRVAIARALMMEPQVLLF 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2351811981 495 DEPTASLDGETEAGIVEAVRRLAQ-GRTVLLVVHRPALL-PLADRVVRLEPG 544
Cdd:COG4161 166 DEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFArKVASQVVYMEKG 217
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
922-1142 |
1.06e-16 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 82.93 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 922 EVRGLSARYAGAERD--ALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGF-- 997
Cdd:PRK11153 3 ELKNISKVFPQGGRTihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 998 -VGLcaqdahIFD-----SS--IREN----LRLARTGATDEELRAA--LDRARLLDWAEALPAgldtlvgehgaRLSGGQ 1063
Cdd:PRK11153 83 qIGM------IFQhfnllSSrtVFDNvalpLELAGTPKAEIKARVTelLELVGLSDKADRYPA-----------QLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1064 RQRLALARAiLADFP-VLVLDEPAEHLDLATADALTaDLLA---ATRGRTTVLITHRLQGLEAV-DEVVVLEAGRVVQRG 1138
Cdd:PRK11153 146 KQRVAIARA-LASNPkVLLCDEATSALDPATTRSIL-ELLKdinRELGLTIVLITHEMDVVKRIcDRVAVIDAGRLVEQG 223
|
....
gi 2351811981 1139 PYAD 1142
Cdd:PRK11153 224 TVSE 227
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
333-544 |
1.07e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 81.28 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWR--ERI 410
Cdd:PRK11248 2 LQISHLYADYGGK--PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVvfQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 411 AWVPQRPYLfaGTIAENVRLArpdaddgAVAAALRDAGAYDFVAelpdgaqtLLGEDGAG------LSAGQRQRLALARA 484
Cdd:PRK11248 80 GLLPWRNVQ--DNVAFGLQLA-------GVEKMQRLEIAHQMLK--------KVGLEGAEkryiwqLSGGQRQRVGIARA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 485 FLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQ--GRTVLLVVH--RPALLpLADRVVRLEPG 544
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQetGKQVLLITHdiEEAVF-MATELVLLSPG 205
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
937-1138 |
1.17e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 81.57 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 937 ALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDAC---VLEGdtVRGFVGLCAQ--DAHIFDSS 1011
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGdfsKLQG--IRKLVGIVFQnpETQFVGRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1012 IRENLRLARTGAT--DEELRAALDRArlldWAEalpAGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHL 1089
Cdd:PRK13644 95 VEEDLAFGPENLClpPIEIRKRVDRA----LAE---IGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSML 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1090 DLATADALTADLLAATR-GRTTVLITHRLQGLEAVDEVVVLEAGRVVQRG 1138
Cdd:PRK13644 168 DPDSGIAVLERIKKLHEkGKTIVYITHNLEELHDADRIIVMDRGKIVLEG 217
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
345-544 |
1.20e-16 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 80.95 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 345 RGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAP--------ERWRERIAWVPQR 416
Cdd:PRK11264 14 HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsqqkgliRQLRQHVGFVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 417 PYLFAG-TIAENVrLARPDADDGAVAAALrDAGAYDFVAELpdgaqTLLGEDGA---GLSAGQRQRLALARAfLADRP-L 491
Cdd:PRK11264 94 FNLFPHrTVLENI-IEGPVIVKGEPKEEA-TARARELLAKV-----GLAGKETSyprRLSGGQQQRVAIARA-LAMRPeV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2351811981 492 LLLDEPTASLDGETEAGIVEAVRRLAQ-GRTVLLVVHRPALL-PLADRVVRLEPG 544
Cdd:PRK11264 166 ILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFArDVADRAIFMDQG 220
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
921-1138 |
1.29e-16 |
|
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: 80.02 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAgaERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDacvlEGDTVRGFVGL 1000
Cdd:cd03269 1 LEVENVTKRFG--RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKP----LDIAARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDAHIF-DSSIRENLR-LAR-TGATDEELraaldRARLLDWAEALpaGLDTLVGEHGARLSGGQRQRLALARAILADF 1077
Cdd:cd03269 75 LPEERGLYpKMKVIDQLVyLAQlKGLKKEEA-----RRRIDEWLERL--ELSEYANKRVEELSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2351811981 1078 PVLVLDEPAEHLDLATADALTADLLA-ATRGRTTVLITHRLQGLEAV-DEVVVLEAGRVVQRG 1138
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVEELcDRVLLLNKGRAVLYG 210
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
929-1129 |
1.39e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 79.20 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 929 RYAGaeRDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGvdacvlegdtvRGFVGLCAQDAHIF 1008
Cdd:NF040873 1 GYGG--RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1009 DS---SIRENLRLARTGATDEELR-AALDRARLLDWAEALpaGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDE 1084
Cdd:NF040873 68 DSlplTVRDLVAMGRWARRGLWRRlTRDDRAAVDDALERV--GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2351811981 1085 PAEHLDLATADALTADLLAAT-RGRTTVLITHRLQGLEAVDEVVVL 1129
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHaRGATVVVVTHDLELVRRADPCVLL 191
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
919-1143 |
1.46e-16 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 82.47 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 919 FPLEvRGLSARYAGAERdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGF- 997
Cdd:COG4608 17 FPVR-GGLFGRTVGVVK-AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 998 --VGLCAQDAHifdSSIreNLRLaRTGATDEE-LRAA--LDRARLLDWAEALpagLDtLVG---EHGAR----LSGGQRQ 1065
Cdd:COG4608 95 rrMQMVFQDPY---ASL--NPRM-TVGDIIAEpLRIHglASKAERRERVAEL---LE-LVGlrpEHADRypheFSGGQRQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1066 RLALARAILADFPVLVLDEPAEHLDL---ATADALTADlLAATRGRTTVLITHRLqgleAV-----DEVVVLEAGRVVQR 1137
Cdd:COG4608 165 RIGIARALALNPKLIVCDEPVSALDVsiqAQVLNLLED-LQDELGLTYLFISHDL----SVvrhisDRVAVMYLGKIVEI 239
|
....*.
gi 2351811981 1138 GPYADL 1143
Cdd:COG4608 240 APRDEL 245
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
350-544 |
1.59e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 82.44 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 350 LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATL-APERwreRIAWVPQRPYLFAG-TIAEN 427
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLhARDR---KVGFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 428 V--------RLARPdaddgavaaalrDAGAYDF-VAELPDGAQT--LLGEDGAGLSAGQRQRLALARAFLADRPLLLLDE 496
Cdd:PRK10851 95 IafgltvlpRRERP------------NAAAIKAkVTQLLEMVQLahLADRYPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 497 PTASLDGETEAGIVEAVRRLAQ--GRTVLLVVH-RPALLPLADRVVRLEPG 544
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQLHEelKFTSVFVTHdQEEAMEVADRVVVMSQG 213
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
350-530 |
1.62e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 80.73 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 350 LDHASLVVDEGETVALVGPSGVGKSTLLDVV-----LGFTAPDEGRVRVGGVDLATLAPERWRERIAWVPQRPYLFAG-T 423
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlieLYPEARVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIPNlS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 424 IAENV----RLARPDADDGAVAAALRDAGAYdfvAELPDGAQTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTA 499
Cdd:PRK14247 99 IFENValglKLNRLVKSKKELQERVRWALEK---AQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTA 175
|
170 180 190
....*....|....*....|....*....|.
gi 2351811981 500 SLDGETEAGIVEAVRRLAQGRTVLLVVHRPA 530
Cdd:PRK14247 176 NLDPENTAKIESLFLELKKDMTIVLVTHFPQ 206
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
355-530 |
1.68e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 80.66 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 355 LVVDEGETVALVGPSGVGKSTLLD-----VVLGFTAPDEGRVRVGGVDLAT--LAPERWRERIAWVPQRPYLFAG-TIAE 426
Cdd:PRK14267 25 LKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGEVRLFGRNIYSpdVDPIEVRREVGMVFQYPNPFPHlTIYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 427 NVRLARPDADDGAVAAALRDAGAYDFV-AELPDGAQTLLGEDGAGLSAGQRQRLALARAfLADRP-LLLLDEPTASLDGE 504
Cdd:PRK14267 105 NVAIGVKLNGLVKSKKELDERVEWALKkAALWDEVKDRLNDYPSNLSGGQRQRLVIARA-LAMKPkILLMDEPTANIDPV 183
|
170 180
....*....|....*....|....*.
gi 2351811981 505 TEAGIVEAVRRLAQGRTVLLVVHRPA 530
Cdd:PRK14267 184 GTAKIEELLFELKKEYTIVLVTHSPA 209
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
934-1136 |
1.74e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 81.41 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 934 ERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDT----VRGFVGLCAQ--DAHI 1007
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlkkLRKKVSLVFQfpEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1008 FDSSIRENLRLA--RTGATDEELRAAldrarLLDWAEALpaGLDTLVGEHGA-RLSGGQRQRLALArAILADFP-VLVLD 1083
Cdd:PRK13641 99 FENTVLKDVEFGpkNFGFSEDEAKEK-----ALKWLKKV--GLSEDLISKSPfELSGGQMRRVAIA-GVMAYEPeILCLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2351811981 1084 EPAEHLDLATADALTADLLAATR-GRTTVLITHRLQGL-EAVDEVVVLEAGRVVQ 1136
Cdd:PRK13641 171 EPAAGLDPEGRKEMMQLFKDYQKaGHTVILVTHNMDDVaEYADDVLVLEHGKLIK 225
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
921-1152 |
1.80e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 81.00 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGaERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGL 1000
Cdd:PRK13652 4 IETRDLCYSYSG-SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQ--DAHIFDSSIRENLRLART--GATDEELRAALDRA-RLLdwaealpaGLDTLVGEHGARLSGGQRQRLALARAILA 1075
Cdd:PRK13652 83 VFQnpDDQIFSPTVEQDIAFGPInlGLDEETVAHRVSSAlHML--------GLEELRDRVPHHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1076 DFPVLVLDEPAEHLDLATADALTADL--LAATRGRTTVLITHRLQGL-EAVDEVVVLEAGRVVQRGPYADLTAEEGPLRR 1152
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLndLPETYGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQPDLLAR 234
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
921-1137 |
1.84e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 80.51 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGaeRDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDacVLEGDTVRGFVgl 1000
Cdd:PRK11248 2 LQISHLYADYGG--KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKP--VEGPGAERGVV-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDAHIFDSSIREN----LRLARTGATDEELRAaLDRARLLDWAEAlpagldtlvgehGAR----LSGGQRQRLALARA 1072
Cdd:PRK11248 76 FQNEGLLPWRNVQDNvafgLQLAGVEKMQRLEIA-HQMLKKVGLEGA------------EKRyiwqLSGGQRQRVGIARA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2351811981 1073 ILADFPVLVLDEPAEHLDLATADALTADLLAATR--GRTTVLITHRLQglEAV---DEVVVLE--AGRVVQR 1137
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQetGKQVLLITHDIE--EAVfmaTELVLLSpgPGRVVER 212
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
934-1147 |
1.96e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 81.22 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 934 ERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGgvdACVLEGDT-------VRGFVGLCAQ--D 1004
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIG---ERVITAGKknkklkpLRKKVGIVFQfpE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1005 AHIFDSSIRENLRLART--GATDEElraALDRARlldwaEALP-AGLDTLVGEHGA-RLSGGQRQRLALArAILADFP-V 1079
Cdd:PRK13634 96 HQLFEETVEKDICFGPMnfGVSEED---AKQKAR-----EMIElVGLPEELLARSPfELSGGQMRRVAIA-GVLAMEPeV 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2351811981 1080 LVLDEPAEHLDLATADALTaDL---LAATRGRTTVLITHRLQGLEA-VDEVVVLEAGRVVQRGpyadlTAEE 1147
Cdd:PRK13634 167 LVLDEPTAGLDPKGRKEMM-EMfykLHKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQG-----TPRE 232
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
921-1115 |
1.96e-16 |
|
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: 78.94 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSarYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGL 1000
Cdd:TIGR01189 1 LAARNLA--CSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDAHIFDSSIRENLRL--ARTGATDEELRAALDRARLLDwAEALPAgldtlvgehgARLSGGQRQRLALARAILADFP 1078
Cdd:TIGR01189 79 GHLPGLKPELSALENLHFwaAIHGGAQRTIEDALAAVGLTG-FEDLPA----------AQLSAGQQRRLALARLWLSRRP 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 2351811981 1079 VLVLDEPAEHLDLATADALTADLLA-ATRGRTTVLITH 1115
Cdd:TIGR01189 148 LWILDEPTTALDKAGVALLAGLLRAhLARGGIVLLTTH 185
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
313-525 |
2.30e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 83.54 E-value: 2.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 313 SVLETEPRRGGTADVPeslRLELEGVTVRHEgRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVR 392
Cdd:COG3845 241 EVLLRVEKAPAEPGEV---VLEVENLSVRDD-RGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIR 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 393 VGGVDLATLAPERWRER-IAWVPQRPY---LFAG-TIAENVRLARPDADDGAVAAALRDAGAYDFVAEL-------PDGA 460
Cdd:COG3845 317 LDGEDITGLSPRERRRLgVAYIPEDRLgrgLVPDmSVAENLILGRYRRPPFSRGGFLDRKAIRAFAEELieefdvrTPGP 396
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 461 QTLLGedgaGLSAGQRQRLALARAFLADRPLLLLDEPTASLDgeteAGIVEAVRRL-----AQGRTVLLV 525
Cdd:COG3845 397 DTPAR----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLD----VGAIEFIHQRllelrDAGAAVLLI 458
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
618-1135 |
2.31e-16 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 83.69 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 618 VGLMAVSGWLISRASEQPPVLYLMVAVTATRAFGLGRAVFRYAERLvSHDAVlkmlAELRVAVYRGLERIAPAGLRRSRR 697
Cdd:COG4615 30 AGLIALINQALNATGAALARLLLLFAGLLVLLLLSRLASQLLLTRL-GQHAV----ARLRLRLSRRILAAPLERLERIGA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 698 GDLLSRLVADVDALQDYwLRWLLPAGTAVVVGAATAGFIGWL-LPAAGIVLATGLLLAGAGVPLVsgacsRHAERQLAPA 776
Cdd:COG4615 105 ARLLAALTEDVRTISQA-FVRLPELLQSVALVLGCLAYLAWLsPPLFLLTLVLLGLGVAGYRLLV-----RRARRHLRRA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 777 RA---DLATRITDLLGGTAELtvagALPARKARtREADGVLTRIAARAATATALGGGLIALIGGLT------VVATALVA 847
Cdd:COG4615 179 REaedRLFKHFRALLEGFKEL----KLNRRRRR-AFFDEDLQPTAERYRDLRIRADTIFALANNWGnllffaLIGLILFL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 848 LPAVHDGR---LAGVELAVV-VLTPLAafEAVTGLPLAVqyrqRVKRSAERVYEV---LDAPPPVREPDSPAGTPASPFP 920
Cdd:COG4615 254 LPALGWADpavLSGFVLVLLfLRGPLS--QLVGALPTLS----RANVALRKIEELelaLAAAEPAAADAAAPPAPADFQT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAERD---ALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVdacVLEGDTVRGF 997
Cdd:COG4615 328 LELRGVTYRYPGEDGDegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ---PVTADNREAY 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 998 VGLCA---QDAHIFDssirenlRLArtGATDEElraalDRARLLDWAEALpaGLDTLVG-EHGA----RLSGGQRQRLAL 1069
Cdd:COG4615 405 RQLFSavfSDFHLFD-------RLL--GLDGEA-----DPARARELLERL--ELDHKVSvEDGRfsttDLSQGQRKRLAL 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2351811981 1070 ARAILADFPVLVLDEPAehldlatAD-----------ALTADLLAatRGRTTVLITHRLQGLEAVDEVVVLEAGRVV 1135
Cdd:COG4615 469 LVALLEDRPILVFDEWA-------ADqdpefrrvfytELLPELKA--RGKTVIAISHDDRYFDLADRVLKMDYGKLV 536
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
340-544 |
2.67e-16 |
|
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: 79.68 E-value: 2.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 340 VRHEGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGvdlatLAPerWRERIAWVPQRPYL 419
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-----LVP--WKRRKKFLRRIGVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 420 FAG--------TIAENVRLARpdaddgaVAAALRDAGAYDFVAELPDGAQT--LLGEDGAGLSAGQRQRLALARAFLADR 489
Cdd:cd03267 100 FGQktqlwwdlPVIDSFYLLA-------AIYDLPPARFKKRLDELSELLDLeeLLDTPVRQLSLGQRMRAEIAAALLHEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2351811981 490 PLLLLDEPTASLDGETEAGIVEAVRRLAQGR--TVLLVVHR-PALLPLADRVVRLEPG 544
Cdd:cd03267 173 EILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYmKDIEALARRVLVIDKG 230
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
852-1129 |
2.84e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 84.70 E-value: 2.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 852 HDGRLAGVELAVVVltplAAFEAVTGLPLAVQYRQRVKrSAERVYEVLDAPPPVREPDSPAGTPASPfPLEVRGLSARYa 931
Cdd:PTZ00265 320 HGGSVISILLGVLI----SMFMLTIILPNITEYMKSLE-ATNSLYEIINRKPLVENNDDGKKLKDIK-KIQFKNVRFHY- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 932 GAERDALDSVDLR--LTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGgvDACVLEGDTV---RGFVGLCAQDAH 1006
Cdd:PTZ00265 393 DTRKDVEIYKDLNftLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLkwwRSKIGVVSQDPL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1007 IFDSSIRENLRLARTGATDEE---------------------------------LRAALDRARLL--------------- 1038
Cdd:PTZ00265 471 LFSNSIKNNIKYSLYSLKDLEalsnyynedgndsqenknkrnscrakcagdlndMSNTTDSNELIemrknyqtikdsevv 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1039 ---------DWAEALPAGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADAL--TADLLAATRG 1107
Cdd:PTZ00265 551 dvskkvlihDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVqkTINNLKGNEN 630
|
330 340
....*....|....*....|..
gi 2351811981 1108 RTTVLITHRLQGLEAVDEVVVL 1129
Cdd:PTZ00265 631 RITIIIAHRLSTIRYANTIFVL 652
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
350-544 |
3.39e-16 |
|
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: 78.05 E-value: 3.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 350 LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPD--EGRVRVGGVDLatlaPERWRERIAWVPQRPYLFAG-TIAE 426
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPL----DKNFQRSTGYVEQQDVHSPNlTVRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 427 NVRLArpdaddgavaAALRdagaydfvaelpdgaqtllgedgaGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETE 506
Cdd:cd03232 99 ALRFS----------ALLR------------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2351811981 507 AGIVEAVRRLA-QGRTVLLVVHRP--ALLPLADRVVRLEPG 544
Cdd:cd03232 145 YNIVRFLKKLAdSGQAILCTIHQPsaSIFEKFDRLLLLKRG 185
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
921-1115 |
3.50e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 78.38 E-value: 3.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGaeRDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGl 1000
Cdd:PRK13539 3 LEGEDLACVRGG--RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 cAQDAHIFDSSIRENLRLART--GATDEELRAALDRARLLDWAEaLPAGLdtlvgehgarLSGGQRQRLALARAILADFP 1078
Cdd:PRK13539 80 -HRNAMKPALTVAENLEFWAAflGGEELDIAAALEAVGLAPLAH-LPFGY----------LSAGQKRRVALARLLVSNRP 147
|
170 180 190
....*....|....*....|....*....|....*....
gi 2351811981 1079 VLVLDEPAEHLDlATADALTADLLAA--TRGRTTVLITH 1115
Cdd:PRK13539 148 IWILDEPTAALD-AAAVALFAELIRAhlAQGGIVIAATH 185
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
350-544 |
4.02e-16 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 84.00 E-value: 4.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 350 LDHASLVVDEGETVALVGPSGVGKSTLLDVVlgftapdEGRVRVG----GVDLATLAP--ERWRERIAWVPQRP-YLFAG 422
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVL-------AERVTTGvitgGDRLVNGRPldSSFQRSIGYVQQQDlHLPTS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 423 TIAENVR----LARPdaddgavaAALRDAGAYDFV------AELPDGAQTLLGEDGAGLSAGQRQRLALARAFLADRPLL 492
Cdd:TIGR00956 852 TVRESLRfsayLRQP--------KSVSKSEKMEYVeeviklLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLL 923
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2351811981 493 L-LDEPTASLDGETEAGIVEAVRRLAQ-GRTVLLVVHRPALLPLA--DRVVRLEPG 544
Cdd:TIGR00956 924 LfLDEPTSGLDSQTAWSICKLMRKLADhGQAILCTIHQPSAILFEefDRLLLLQKG 979
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
921-1140 |
4.30e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 83.23 E-value: 4.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAER--DALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTV---- 994
Cdd:PRK10535 5 LELKDIRRSYPSGEEqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 995 RGFVGLCAQDAHIFDS-SIRENLRLArtgatdeELRAALDRARLLDWAEALPA--GLDTLVGEHGARLSGGQRQRLALAR 1071
Cdd:PRK10535 85 REHFGFIFQRYHLLSHlTAAQNVEVP-------AVYAGLERKQRLLRAQELLQrlGLEDRVEYQPSQLSGGQQQRVSIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1072 AILADFPVLVLDEPAEHLDLATADALTADLLA-ATRGRTTVLITHRLQGLEAVDEVVVLEAGRVVQRGPY 1140
Cdd:PRK10535 158 ALMNGGQVILADEPTGALDSHSGEEVMAILHQlRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPA 227
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
891-1116 |
4.67e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 82.93 E-value: 4.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 891 SAERVYEVLDAPPPVREPDSPAGT--PASPFPLEVRGLS-ARYAGAERdaLDSVDLRLTAGRRIAVVGPSGSGKTTLaqv 967
Cdd:COG4178 331 TVDRLAGFEEALEAADALPEAASRieTSEDGALALEDLTlRTPDGRPL--LEDLSLSLKPGERLLITGPSGSGKSTL--- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 968 lLRFL----DAREGTYRI-GGVDACVLegdtvrgfvglcAQDAHIFDSSIRENLR--LARTGATDEELRAALDRARLLDW 1040
Cdd:COG4178 406 -LRAIaglwPYGSGRIARpAGARVLFL------------PQRPYLPLGTLREALLypATAEAFSDAELREALEAVGLGHL 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2351811981 1041 AEALPAGLDTlvgehGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTADLLAATRGRTTVLITHR 1116
Cdd:COG4178 473 AERLDEEADW-----DQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
921-1143 |
4.87e-16 |
|
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: 79.47 E-value: 4.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGaeRDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGL 1000
Cdd:TIGR03873 2 LRLSRVSWSAGG--RLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSRRARARRVAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDAHI-FDSSIRENLRLARTG-----ATDEELRAALDRARLLDwaealpAGLDTLVGEHGARLSGGQRQRLALARAIL 1074
Cdd:TIGR03873 80 VEQDSDTaVPLTVRDVVALGRIPhrslwAGDSPHDAAVVDRALAR------TELSHLADRDMSTLSGGERQRVHVARALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 1075 ADFPVLVLDEPAEHLDLATADALTADLLAATRGRTTVLIT-HRLQ-GLEAVDEVVVLEAGRVVQRGPYADL 1143
Cdd:TIGR03873 154 QEPKLLLLDEPTNHLDVRAQLETLALVRELAATGVTVVAAlHDLNlAASYCDHVVVLDGGRVVAAGPPREV 224
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
298-527 |
5.01e-16 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 83.91 E-value: 5.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 298 YHAAAEGLSAAEEiFSVLETEPRRGGTAD--VPESLR---LELE------GVTVRH-----EGRGEPSLDHASLVVDEGE 361
Cdd:TIGR01257 879 YWLGGEGCSTREE-RALEKTEPLTEEMEDpeHPEGINdsfFERElpglvpGVCVKNlvkifEPSGRPAVDRLNITFYENQ 957
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 362 TVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATlAPERWRERIAWVPQRPYLFAG-TIAENVRLarpdadDGAV 440
Cdd:TIGR01257 958 ITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHlTVAEHILF------YAQL 1030
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 441 AAALRDAGAYDFVAELPD-GAQTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQG 519
Cdd:TIGR01257 1031 KGRSWEEAQLEMEAMLEDtGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSG 1110
|
....*...
gi 2351811981 520 RTVLLVVH 527
Cdd:TIGR01257 1111 RTIIMSTH 1118
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
17-274 |
5.34e-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: 79.86 E-value: 5.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 17 FFLAAVVALGVVGAALVIA--QAMLVADVVVGGFEDGLTvsGLRTPLIL-LAAVALGRALVSWLTELAAYRASAAVKSEL 93
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPylTKILIDDVLIQLGPGGNT--SLLLLLVLgLAGAYVLSALLGILRGRLLARLGERITADL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 94 RGRLLDRAAELGPGLLSDRRTGSLVTLATRGVDALDDYFARYLPQLGLAVVVPVAVLARIVTEDWVSAAIIVVTLPLIPL 173
Cdd:cd18563 79 RRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 174 FMILIGWATQSRMDRQWRLLSRLSGHFLDVVAGLPTLKVFGRAKAQAESIRAITSQYRRATLRTLRIAFLSSFALELLAT 253
Cdd:cd18563 159 GSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTS 238
|
250 260
....*....|....*....|.
gi 2351811981 254 LSVALVAVTIGMRLVHGELDL 274
Cdd:cd18563 239 LGTLIVWYFGGRQVLSGTMTL 259
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
943-1143 |
5.52e-16 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 78.35 E-value: 5.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 943 LRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGvdACVLEGDTVRGFVGLCAQDAHIFDSSIRENLRLARTG 1022
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAG--ASPGKGWRHIGYVPQRHEFAWDFPISVAHTVMSGRTG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1023 atdeeLRAALDRARLLDWAeALPAGLDTLVGEHGAR-----LSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADAL 1097
Cdd:TIGR03771 79 -----HIGWLRRPCVADFA-AVRDALRRVGLTELADrpvgeLSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2351811981 1098 TADLLA-ATRGRTTVLITHRLQGLEAVDEVVVLEAGRVVQRGPYADL 1143
Cdd:TIGR03771 153 TELFIElAGAGTAILMTTHDLAQAMATCDRVVLLNGRVIADGTPQQL 199
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
937-1138 |
6.08e-16 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 78.52 E-value: 6.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 937 ALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGG------VDACVLEGDTVRGFVGLCAQDAHIFDS 1010
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRRNVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1011 -SIRENLRLART---GATDEELRAA----LDRARLLDWAEALPAgldtlvgehgaRLSGGQRQRLALARAILADFPVLVL 1082
Cdd:PRK11124 97 lTVQQNLIEAPCrvlGLSKDQALARaeklLERLRLKPYADRFPL-----------HLSGGQQQRVAIARALMMEPQVLLF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2351811981 1083 DEPAEHLDlataDALTADL------LAATrGRTTVLITHRLQ-GLEAVDEVVVLEAGRVVQRG 1138
Cdd:PRK11124 166 DEPTAALD----PEITAQIvsiireLAET-GITQVIVTHEVEvARKTASRVVYMENGHIVEQG 223
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
921-1146 |
6.13e-16 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 79.00 E-value: 6.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGaeRDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGL 1000
Cdd:COG4559 2 LEAENLSVRLGG--RTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDAHI-FDSSIRENLRLART------GATDEELRAALDRArlldwaealpaGLDTLVGEHGARLSGGQRQRLALARAI 1073
Cdd:COG4559 80 LPQHSSLaFPFTVEEVVALGRAphgssaAQDRQIVREALALV-----------GLAHLAGRSYQTLSGGEQQRVQLARVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1074 L------ADFP-VLVLDEPAEHLDLA---TADALTADLlaATRGRTTVLITHRLQgLEA--VDEVVVLEAGRVVQRGPYA 1141
Cdd:COG4559 149 AqlwepvDGGPrWLFLDEPTSALDLAhqhAVLRLARQL--ARRGGGVVAVLHDLN-LAAqyADRILLLHQGRLVAQGTPE 225
|
....*.
gi 2351811981 1142 D-LTAE 1146
Cdd:COG4559 226 EvLTDE 231
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
921-1143 |
6.45e-16 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 78.60 E-value: 6.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAgaERDALDSVDLRLTAGRRIAVVGPSGSGKTTlaqvLLRFLDARE----GTYRIGGVDACVLEGD--TV 994
Cdd:PRK09493 2 IEFKNVSKHFG--PTQVLHNIDLNIDQGEVVVIIGPSGSGKST----LLRCINKLEeitsGDLIVDGLKVNDPKVDerLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 995 RGFVGLCAQDAHIFDS-SIRENLRLART---GATDEElraALDRAR-LLDwaealPAGLDTLVGEHGARLSGGQRQRLAL 1069
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHlTALENVMFGPLrvrGASKEE---AEKQAReLLA-----KVGLAERAHHYPSELSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1070 ARAiLADFPVLVL-DEPAEHLDlataDALTADLLA-----ATRGRTTVLITHRLQGLEAV-DEVVVLEAGRVVQRGPYAD 1142
Cdd:PRK09493 148 ARA-LAVKPKLMLfDEPTSALD----PELRHEVLKvmqdlAEEGMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQV 222
|
.
gi 2351811981 1143 L 1143
Cdd:PRK09493 223 L 223
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
332-502 |
7.09e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 78.53 E-value: 7.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 332 RLELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLaP--ERWRER 409
Cdd:COG1137 3 TLEAENLVKSYGKR--TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHL-PmhKRARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 410 IAWVPQRPYLFAG-TIAENVRLarpdaddgavaaalrdagaydfVAEL--PDGAQ------TLLGE---------DGAGL 471
Cdd:COG1137 80 IGYLPQEASIFRKlTVEDNILA----------------------VLELrkLSKKEreerleELLEEfgithlrksKAYSL 137
|
170 180 190
....*....|....*....|....*....|..
gi 2351811981 472 SAGQRQRLALARAfLADRP-LLLLDEPTASLD 502
Cdd:COG1137 138 SGGERRRVEIARA-LATNPkFILLDEPFAGVD 168
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
922-1138 |
1.03e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 78.49 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 922 EVRGLSARYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVdacVLEGDTV---RGFV 998
Cdd:PRK13632 9 KVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGI---TISKENLkeiRKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 999 GLCAQ--DAHIFDSSIR-------ENLRLARtgatdEELRAALDRArlldwaeALPAGLDTLVGEHGARLSGGQRQRLAL 1069
Cdd:PRK13632 86 GIIFQnpDNQFIGATVEddiafglENKKVPP-----KKMKDIIDDL-------AKKVGMEDYLDKEPQNLSGGQKQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2351811981 1070 ARAILADFPVLVLDEPAEHLD-LATADALT-ADLLAATRGRTTVLITHRLQglEAV--DEVVVLEAGRVVQRG 1138
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDpKGKREIKKiMVDLRKTRKKTLISITHDMD--EAIlaDKVIVFSEGKLIAQG 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
921-1146 |
1.08e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 78.27 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGaeRDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGL 1000
Cdd:PRK13548 3 LEARNLSVRLGG--RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDAHI-FDSSIRENLRLART--GATDEELRAALDRARLLdwaealpAGLDTLVGEHGARLSGGQRQRLALARAiLA-- 1075
Cdd:PRK13548 81 LPQHSSLsFPFTVEEVVAMGRAphGLSRAEDDALVAAALAQ-------VDLAHLAGRDYPQLSGGEQQRVQLARV-LAql 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1076 -----DFPVLVLDEPAEHLDLA----TADALTAdlLAATRGRTTVLITHRLqGLEA--VDEVVVLEAGRVVQRGPYAD-L 1143
Cdd:PRK13548 153 wepdgPPRWLLLDEPTSALDLAhqhhVLRLARQ--LAHERGLAVIVVLHDL-NLAAryADRIVLLHQGRLVADGTPAEvL 229
|
...
gi 2351811981 1144 TAE 1146
Cdd:PRK13548 230 TPE 232
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
937-1147 |
1.36e-15 |
|
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: 78.45 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 937 ALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGF----VGLCAQDAHIF-DSS 1011
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLpHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1012 IREN----LRLARTGATDEELRA--ALDRARLLDWAEALPagldtlvGEhgarLSGGQRQRLALARAILADFPVLVLDEP 1085
Cdd:cd03294 119 VLENvafgLEVQGVPRAEREERAaeALELVGLEGWEHKYP-------DE----LSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2351811981 1086 AEHLDLATADALTADLLA--ATRGRTTVLITHRLQglEAV---DEVVVLEAGRVVQRGpyadlTAEE 1147
Cdd:cd03294 188 FSALDPLIRREMQDELLRlqAELQKTIVFITHDLD--EALrlgDRIAIMKDGRLVQVG-----TPEE 247
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
333-558 |
1.71e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 81.00 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTA--PDEGRV--------RVGGVDL---- 398
Cdd:TIGR03269 1 IEVKNLTKKFDGK--EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalceKCGYVERpskv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 399 --------ATLAPE-------------RWRERIAWVPQRPYLFAG--TIAENVRLArpdaddgavaaaLRDAG-----AY 450
Cdd:TIGR03269 79 gepcpvcgGTLEPEevdfwnlsdklrrRIRKRIAIMLQRTFALYGddTVLDNVLEA------------LEEIGyegkeAV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 451 DFVAELPDGAQ-----TLLGEDgagLSAGQRQRLALARAfLADRPLLLL-DEPTASLDGETEAGIVEAVRRLAQ--GRTV 522
Cdd:TIGR03269 147 GRAVDLIEMVQlshriTHIARD---LSGGEKQRVVLARQ-LAKEPFLFLaDEPTGTLDPQTAKLVHNALEEAVKasGISM 222
|
250 260 270
....*....|....*....|....*....|....*..
gi 2351811981 523 LLVVHRPALLP-LADRVVRLEPGATLRPEKPEGSVAV 558
Cdd:TIGR03269 223 VLTSHWPEVIEdLSDKAIWLENGEIKEEGTPDEVVAV 259
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
922-1147 |
1.86e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 77.43 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 922 EVRGLSARYAGAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGLC 1001
Cdd:COG4604 3 EIKNVSKRYGGKV--VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1002 AQDAHIfdssireNLRL---------------ARTGATDEEL-RAALDRARLLDWAEALpagLDTLvgehgarlSGGQRQ 1065
Cdd:COG4604 81 RQENHI-------NSRLtvrelvafgrfpyskGRLTAEDREIiDEAIAYLDLEDLADRY---LDEL--------SGGQRQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1066 RLALARAILADFPVLVLDEPAEHLDLATADALTADL--LAATRGRTTVLITHRLqGLEAV--DEVVVLEAGRVVQRGPYA 1141
Cdd:COG4604 143 RAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLrrLADELGKTVVIVLHDI-NFASCyaDHIVAMKDGRVVAQGTPE 221
|
....*.
gi 2351811981 1142 DLTAEE 1147
Cdd:COG4604 222 EIITPE 227
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
921-1118 |
2.08e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 77.51 E-value: 2.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAgaERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLD-----AREGTYRIGGVDACVLEGDTV- 994
Cdd:PRK14239 6 LQVSDLSVYYN--KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSPRTDTVd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 995 -RGFVGLCAQDAHIFDSSIREN----LRLA---RTGATDEELRAALDRARLldWAEALPAGLDTLVGehgarLSGGQRQR 1066
Cdd:PRK14239 84 lRKEIGMVFQQPNPFPMSIYENvvygLRLKgikDKQVLDEAVEKSLKGASI--WDEVKDRLHDSALG-----LSGGQQQR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2351811981 1067 LALARaILADFP-VLVLDEPAEHLDLATADALTADLLAATRGRTTVLITHRLQ 1118
Cdd:PRK14239 157 VCIAR-VLATSPkIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQ 208
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
333-502 |
2.39e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 79.22 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPErwRERIAW 412
Cdd:PRK09452 15 VELRGISKSFDGK--EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 413 VPQRPYLFAG-TIAENVRLARPDADDGAVAAALRDAGAYDFVaELPDGAQtllgEDGAGLSAGQRQRLALARAfLADRP- 490
Cdd:PRK09452 91 VFQSYALFPHmTVFENVAFGLRMQKTPAAEITPRVMEALRMV-QLEEFAQ----RKPHQLSGGQQQRVAIARA-VVNKPk 164
|
170
....*....|..
gi 2351811981 491 LLLLDEPTASLD 502
Cdd:PRK09452 165 VLLLDESLSALD 176
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
917-1154 |
2.72e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 77.05 E-value: 2.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 917 SPFPLEVRGLSARyagAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAreGTYRIGG---VDACVLEGDT 993
Cdd:PRK10418 1 MPQQIELRNIALQ---AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA--GVRQTAGrvlLDGKPVAPCA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 994 VRG-FVGLCAQD-------AHIFDSSIRENLRLARTGATDEELRAALDRARLLDwaealpagLDTLVGEHGARLSGGQRQ 1065
Cdd:PRK10418 76 LRGrKIATIMQNprsafnpLHTMHTHARETCLALGKPADDATLTAALEAVGLEN--------AARVLKLYPFEMSGGMLQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1066 RLALARAILADFPVLVLDEPAEHLDLaTADALTADLLA---ATRGRTTVLITHRLqGLEA--VDEVVVLEAGRVVQRGPY 1140
Cdd:PRK10418 148 RMMIALALLCEAPFIIADEPTTDLDV-VAQARILDLLEsivQKRALGMLLVTHDM-GVVArlADDVAVMSHGRIVEQGDV 225
|
250
....*....|....*
gi 2351811981 1141 ADL-TAEEGPLRRML 1154
Cdd:PRK10418 226 ETLfNAPKHAVTRSL 240
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
920-1138 |
2.88e-15 |
|
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: 76.16 E-value: 2.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 920 PLEVRGLSARYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLdarEGTYRIGG---VDACVLEGDTVRG 996
Cdd:cd03234 5 PWWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRV---EGGGTTSGqilFNGQPRKPDQFQK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 997 FVGLCAQDAHIFDS-SIRENLRLARTGATDEELRAALDRARLLDWAEALPAglDTLVGehGAR---LSGGQRQRLALARA 1072
Cdd:cd03234 82 CVAYVRQDDILLPGlTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLA--LTRIG--GNLvkgISGGERRRVSIAVQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 1073 ILADFPVLVLDEPAEHLdlataDALTADLLA------ATRGRTTVLITH--RLQGLEAVDEVVVLEAGRVVQRG 1138
Cdd:cd03234 158 LLWDPKVLILDEPTSGL-----DSFTALNLVstlsqlARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
346-545 |
3.87e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 79.71 E-value: 3.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 346 GEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRER-IAWVPQRPYLFAG-T 423
Cdd:PRK15439 23 GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgIYLVPQEPLLFPNlS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 424 IAENV--RLARPDADDGAVAAALrdagaydfvAELpdGAQTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTASL 501
Cdd:PRK15439 103 VKENIlfGLPKRQASMQKMKQLL---------AAL--GCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2351811981 502 D-GETEAGIVEAVRRLAQGRTVLLVVHR-PALLPLADRVVRLEPGA 545
Cdd:PRK15439 172 TpAETERLFSRIRELLAQGVGIVFISHKlPEIRQLADRISVMRDGT 217
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
921-1143 |
4.83e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 77.07 E-value: 4.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAgaERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDacvLEGDTVR--GFV 998
Cdd:COG4152 2 LELKGLTKRFG--DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEP---LDPEDRRriGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 999 ----GLCAqdahifDSSIRENLR-LAR-TGATDEELRAA----LDRARLLDWAealpaglDTLVGEhgarLSGGQRQRLA 1068
Cdd:COG4152 77 peerGLYP------KMKVGEQLVyLARlKGLSKAEAKRRadewLERLGLGDRA-------NKKVEE----LSKGNQQKVQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2351811981 1069 LARAILADFPVLVLDEPAEHLDLATADALtADLL--AATRGRTTVLITHRLQGLEAV-DEVVVLEAGRVVQRGPYADL 1143
Cdd:COG4152 140 LIAALLHDPELLILDEPFSGLDPVNVELL-KDVIreLAAKGTTVIFSSHQMELVEELcDRIVIINKGRKVLSGSVDEI 216
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
953-1138 |
5.01e-15 |
|
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: 77.53 E-value: 5.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 953 VVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDacVLEGDTVRGFVGLCAQDAHIFDS-SIREN----LRLARTGAT--D 1025
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGED--VTNVPPHLRHINMVFQSYALFPHmTVEENvafgLKMRKVPRAeiK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1026 EELRAALDRARLLDWAEALPAgldtlvgehgaRLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTADLLAAT 1105
Cdd:TIGR01187 79 PRVLEALRLVQLEEFADRKPH-----------QLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQ 147
|
170 180 190
....*....|....*....|....*....|....*.
gi 2351811981 1106 R--GRTTVLITH-RLQGLEAVDEVVVLEAGRVVQRG 1138
Cdd:TIGR01187 148 EqlGITFVFVTHdQEEAMTMSDRIAIMRKGKIAQIG 183
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
934-1147 |
7.27e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 76.59 E-value: 7.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 934 ERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGT-----YRIGGVDACVLEGDTVRGFVGLCAQ--DAH 1006
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtivgdYAIPANLKKIKEVKRLRKEIGLVFQfpEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1007 IFDSSIRENLRLA--RTGATDEELRAALdrARLLDWAEaLPaglDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDE 1084
Cdd:PRK13645 103 LFQETIEKDIAFGpvNLGENKQEAYKKV--PELLKLVQ-LP---EDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2351811981 1085 PAEHLDLATADALTA--DLLAATRGRTTVLITHRL-QGLEAVDEVVVLEAGRVVQRG-PYADLTAEE 1147
Cdd:PRK13645 177 PTGGLDPKGEEDFINlfERLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGsPFEIFSNQE 243
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
921-1146 |
8.28e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 78.69 E-value: 8.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAER---DALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTY--RIGG--VDAC---VLE 990
Cdd:TIGR03269 280 IKVRNVSKRYISVDRgvvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvRVGDewVDMTkpgPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 991 GDTVRGFVGLCAQDAHIF-DSSIRENLrlarTGATDEELRAALDRARLL----------DWAEALpagLDTLVGEhgarL 1059
Cdd:TIGR03269 360 RGRAKRYIGILHQEYDLYpHRTVLDNL----TEAIGLELPDELARMKAVitlkmvgfdeEKAEEI---LDKYPDE----L 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1060 SGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTADLLAATR--GRTTVLITHRLQG-LEAVDEVVVLEAGRVVQ 1136
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFvLDVCDRAALMRDGKIVK 508
|
250
....*....|
gi 2351811981 1137 RGPYADLTAE 1146
Cdd:TIGR03269 509 IGDPEEIVEE 518
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
352-553 |
8.81e-15 |
|
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: 75.76 E-value: 8.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 352 HASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRE----RIAWVPQRPYLFAG-TIAE 426
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLPHrTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 427 NVRLARPDADDGAVAAALRDAGAYDFVAeLPDGAQTLLGEdgagLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETE 506
Cdd:cd03294 122 NVAFGLEVQGVPRAEREERAAEALELVG-LEGWEHKYPDE----LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIR 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2351811981 507 AGIVEAVRRLA--QGRTVLLVVHRPA-LLPLADRVVRLEPGATLRPEKPE 553
Cdd:cd03294 197 REMQDELLRLQaeLQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPE 246
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
934-1147 |
9.06e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 75.89 E-value: 9.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 934 ERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGLCAQD-----AhiF 1008
Cdd:COG1101 18 EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDpmmgtA--P 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1009 DSSIRENLRLA-----RTGatdeeLRAAL---DRARLLDWAEALPAGL----DTLVGEhgarLSGGQRQRLALARAILAD 1076
Cdd:COG1101 96 SMTIEENLALAyrrgkRRG-----LRRGLtkkRRELFRELLATLGLGLenrlDTKVGL----LSGGQRQALSLLMATLTK 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2351811981 1077 FPVLVLDEPAEHLDLATAD---ALTADLLAAtRGRTTVLITHRL-QGLEAVDEVVVLEAGRVVqrgpyADLTAEE 1147
Cdd:COG1101 167 PKLLLLDEHTAALDPKTAAlvlELTEKIVEE-NNLTTLMVTHNMeQALDYGNRLIMMHEGRII-----LDVSGEE 235
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
900-1147 |
9.60e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.53 E-value: 9.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 900 DAPPPVREPDSPAGTPAspfpLEVRGLSARyAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTY 979
Cdd:COG3845 241 EVLLRVEKAPAEPGEVV----LEVENLSVR-DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSI 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 980 RIGGVDacvLEGDTVR-------GFV-------GLCAqdahifDSSIRENLRLARTGATDEELRAALDRARLLDWAEAL- 1044
Cdd:COG3845 316 RLDGED---ITGLSPRerrrlgvAYIpedrlgrGLVP------DMSVAENLILGRYRRPPFSRGGFLDRKAIRAFAEELi 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1045 ------PAGLDTLVGehgaRLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTADLLAA-TRGRTTVLITHRL 1117
Cdd:COG3845 387 eefdvrTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELrDAGAAVLLISEDL 462
|
250 260 270
....*....|....*....|....*....|.
gi 2351811981 1118 QGLEAV-DEVVVLEAGRVVQRGPYADLTAEE 1147
Cdd:COG3845 463 DEILALsDRIAVMYEGRIVGEVPAAEATREE 493
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
333-553 |
1.11e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 75.99 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDE---GRVRVGGVDLAtlAPERW--R 407
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLT--AKTVWdiR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 408 ERIAWVPQRP-YLFAGTIA--------ENVRLARPDADDGAVAAaLRDAGAYDFVAELPdgaqtllgedgAGLSAGQRQR 478
Cdd:PRK13640 84 EKVGIVFQNPdNQFVGATVgddvafglENRAVPRPEMIKIVRDV-LADVGMLDYIDSEP-----------ANLSGGQKQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2351811981 479 LALArAFLADRP-LLLLDEPTASLDGETEAGIVEAVRRLAQ--GRTVLLVVHRPALLPLADRVVRLEPGATLRPEKPE 553
Cdd:PRK13640 152 VAIA-GILAVEPkIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPV 228
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
14-311 |
1.14e-14 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 76.04 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 14 ATRFFLAAVVALGVVGAALVIaqaMLVADVVVGGfedgLTVSGLRTPLILLAAVALGRALVSWLTELAAYRASAAVKSEL 93
Cdd:cd18778 3 LTLLCALLSTLLGLVPPWLIR---ELVDLVTIGS----KSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 94 RGRLLDRAAELGPGLLSDRRTGSLVTLATRGVDALDDYFARYLPQLGLAVVVPVAVLARIVTEDWVSAAIIVVTLPLIPL 173
Cdd:cd18778 76 RSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 174 FMILIGWATQSRMDRQWRLLSRLSGHFLDVVAGLPTLKVFGRAKAQAESIRAITSQYRRATLRTLRIAFLSSFALELLAT 253
Cdd:cd18778 156 GAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTS 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 254 LSVALVaVTIGMRLV-HGELDLyTGLVVLILAPEA-YLPIRQVGAQYHAAAEGLSAAEEI 311
Cdd:cd18778 236 LGTVLV-LGFGGRLVlAGELTI-GDLVAFLLYLGLfYEPITSLHGLNEMLQRALAGAERV 293
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
315-518 |
1.25e-14 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 78.19 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 315 LETEPRrGGTADVPESLR--LELEGVTVRHEGRGE---------PSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGF 383
Cdd:COG4172 257 LAAEPR-GDPRPVPPDAPplLEARDLKVWFPIKRGlfrrtvghvKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 384 TaPDEGRVRVGGVDLATLAPE---RWRERIAWVPQRPY-------LFAGTIAENVRLARPDADDGAvaaalRDAGAYDFV 453
Cdd:COG4172 336 I-PSEGEIRFDGQDLDGLSRRalrPLRRRMQVVFQDPFgslsprmTVGQIIAEGLRVHGPGLSAAE-----RRARVAEAL 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2351811981 454 AElpdgaqtlLGEDGAGL-------SAGQRQRLALARAfLADRP-LLLLDEPTASLDGETEAGIVEAVRRLAQ 518
Cdd:COG4172 410 EE--------VGLDPAARhryphefSGGQRQRIAIARA-LILEPkLLVLDEPTSALDVSVQAQILDLLRDLQR 473
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
920-1139 |
1.27e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 75.85 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 920 PLEVRGLSARYAGA---ERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDAC--VLEGDTV 994
Cdd:PRK13637 2 SIKIENLTHIYMEGtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 995 RGFVGLCAQ--DAHIFDSSIRENLRLA--RTGATDEELRAALDRARLLdwaealpAGLD--TLVGEHGARLSGGQRQRLA 1068
Cdd:PRK13637 82 RKKVGLVFQypEYQLFEETIEKDIAFGpiNLGLSEEEIENRVKRAMNI-------VGLDyeDYKDKSPFELSGGQKRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2351811981 1069 LArAILADFP-VLVLDEPAEHLDLATADALTADL--LAATRGRTTVLITHRLQGL-EAVDEVVVLEAGRVVQRGP 1139
Cdd:PRK13637 155 IA-GVVAMEPkILILDEPTAGLDPKGRDEILNKIkeLHKEYNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGT 228
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
333-540 |
1.32e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 73.68 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRhegRGEPSL-DHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRErIA 411
Cdd:PRK13538 2 LEARNLACE---RDERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQD-LL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 412 WVPQRPylfaG-----TIAENVRLArpdaddgavaaaLRDAGAYDfvaelPDGAQTLLGEDG-AG--------LSAGQRQ 477
Cdd:PRK13538 78 YLGHQP----GiktelTALENLRFY------------QRLHGPGD-----DEALWEALAQVGlAGfedvpvrqLSAGQQR 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 478 RLALARAFLADRPLLLLDEPTASLDgeteagiVEAVRRL--------AQGRTVLLVVHRPalLPLADRVVR 540
Cdd:PRK13538 137 RVALARLWLTRAPLWILDEPFTAID-------KQGVARLeallaqhaEQGGMVILTTHQD--LPVASDKVR 198
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
926-1102 |
1.65e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 74.14 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 926 LSARYAGAeRDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTV---RGFVGLCA 1002
Cdd:PRK10908 7 VSKAYLGG-RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVpflRRQIGMIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1003 QDAHIF-DSSIREN--LRLARTGATDEELR----AALDRARLLDWAEALPAgldtlvgehgaRLSGGQRQRLALARAILA 1075
Cdd:PRK10908 86 QDHHLLmDRTVYDNvaIPLIIAGASGDDIRrrvsAALDKVGLLDKAKNFPI-----------QLSGGEQQRVGIARAVVN 154
|
170 180
....*....|....*....|....*..
gi 2351811981 1076 DFPVLVLDEPAEHLDlataDALTADLL 1102
Cdd:PRK10908 155 KPAVLLADEPTGNLD----DALSEGIL 177
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
948-1139 |
1.79e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.17 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 948 GRRIAVVGPSGSGKTTLAQVLLrFLDA----REGTYRIGG----------VDACVLEGDTvrgFVG-LCAQDAHIFDSsi 1012
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALA-FRSPkgvkGSGSVLLNGmpidakemraISAYVQQDDL---FIPtLTVREHLMFQA-- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1013 reNLRLARTGATDEE---LRAALDRARLLDWAealpaglDTLVGEHGAR--LSGGQRQRLALARAILADFPVLVLDEPAE 1087
Cdd:TIGR00955 125 --HLRMPRRVTKKEKrerVDEVLQALGLRKCA-------NTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2351811981 1088 HLDLATADALTADLLA-ATRGRTTVLITH----RLQGLeaVDEVVVLEAGRVVQRGP 1139
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGlAQKGKTIICTIHqpssELFEL--FDKIILMAEGRVAYLGS 250
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
921-1161 |
2.19e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 74.43 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAgaERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREG-------TYRIGGVDACVLEGDT 993
Cdd:PRK14243 11 LRTENLNVYYG--SFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGfrvegkvTFHGKNLYAPDVDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 994 VRGFVGLCAQDAHIFDSSIRENLRL-ART----GATDEELRAALDRARLldWAEALpaglDTLvGEHGARLSGGQRQRLA 1068
Cdd:PRK14243 89 VRRRIGMVFQKPNPFPKSIYDNIAYgARIngykGDMDELVERSLRQAAL--WDEVK----DKL-KQSGLSLSGGQQQRLC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1069 LARAILADFPVLVLDEPAEHLDLATADALTADLLAATRGRTTVLITHRLQgleavdevvvlEAGRVVQRGPYADLTAEEG 1148
Cdd:PRK14243 162 IARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQ-----------QAARVSDMTAFFNVELTEG 230
|
250
....*....|....*
gi 2351811981 1149 PLR--RMLEREReTE 1161
Cdd:PRK14243 231 GGRygYLVEFDR-TE 244
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
909-1143 |
2.20e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 74.75 E-value: 2.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 909 DSPAGTPAspfpLEVRGLSARYAGaeRDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGtYRIGGvdACV 988
Cdd:PRK14271 14 DVDAAAPA----MAAVNLTLGFAG--KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSG--DVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 989 LEGDTV---------RGFVGLCAQDAHIFDSSIRENLRL---ARTGATDEELRAaLDRARLLDwaEALPAGLDTLVGEHG 1056
Cdd:PRK14271 85 LGGRSIfnyrdvlefRRRVGMLFQRPNPFPMSIMDNVLAgvrAHKLVPRKEFRG-VAQARLTE--VGLWDAVKDRLSDSP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1057 ARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTADLLAATRGRTTVLITHRL-QGLEAVDEVVVLEAGRVV 1135
Cdd:PRK14271 162 FRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLV 241
|
....*...
gi 2351811981 1136 QRGPYADL 1143
Cdd:PRK14271 242 EEGPTEQL 249
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
349-527 |
2.33e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 74.43 E-value: 2.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 349 SLDHASLVVDEGETVALVGPSGVGKSTLLDVV--LGFTAPD---EGRVRVGGVDLatLAPE----RWRERIAWVPQRPYL 419
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNI--YSPRtdtvDLRKEIGMVFQQPNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 420 FAGTIAENV----RLA---RPDADDGAVAAALRDAGAYDfvaELPDgaqtLLGEDGAGLSAGQRQRLALARAfLADRP-L 491
Cdd:PRK14239 98 FPMSIYENVvyglRLKgikDKQVLDEAVEKSLKGASIWD---EVKD----RLHDSALGLSGGQQQRVCIARV-LATSPkI 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 2351811981 492 LLLDEPTASLDGETEAGIVEAVRRLAQGRTVLLVVH 527
Cdd:PRK14239 170 ILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTR 205
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
921-1171 |
2.53e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 76.99 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDAcvlegdTVRGfvgl 1000
Cdd:COG3845 6 LELRGITKRFGGVV--ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV------RIRS---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 cAQDAH------------IFDS-SIRENLRLARTGATDEELRAALDRARLLDWAEA--LPAGLDTLVGEhgarLSGGQRQ 1065
Cdd:COG3845 74 -PRDAIalgigmvhqhfmLVPNlTVAENIVLGLEPTKGGRLDRKAARARIRELSERygLDVDPDAKVED----LSVGEQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1066 RLALARAILADFPVLVLDEP--------AEHLdLATADALTADllaatrGRTTVLITHRLQGLEAV-DEVVVLEAGRVVQ 1136
Cdd:COG3845 149 RVEILKALYRGARILILDEPtavltpqeADEL-FEILRRLAAE------GKSIIFITHKLREVMAIaDRVTVLRRGKVVG 221
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2351811981 1137 RGPYADLTAEEgpLRRM-------LERERETEGVAEEALGVR 1171
Cdd:COG3845 222 TVDTAETSEEE--LAELmvgrevlLRVEKAPAEPGEVVLEVE 261
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
909-1147 |
2.67e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 75.64 E-value: 2.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 909 DSPAGTpASPFPLEVRGLSARYAGaeRDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACV 988
Cdd:PRK13536 31 ASIPGS-MSTVAIDLAGVSKSYGD--KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 989 lEGDTVRGFVGLCAQdahiFDS-----SIRENL----RLARTGATDEE--LRAALDRARLLDWAealpaglDTLVGEhga 1057
Cdd:PRK13536 108 -RARLARARIGVVPQ----FDNldlefTVRENLlvfgRYFGMSTREIEavIPSLLEFARLESKA-------DARVSD--- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1058 rLSGGQRQRLALARAILADFPVLVLDEPAEHLDlATADALTADLLAA--TRGRTTVLITHRLQGLEAV-DEVVVLEAGRV 1134
Cdd:PRK13536 173 -LSGGMKRRLTLARALINDPQLLILDEPTTGLD-PHARHLIWERLRSllARGKTILLTTHFMEEAERLcDRLCVLEAGRK 250
|
250
....*....|...
gi 2351811981 1135 VQRGPYADLTAEE 1147
Cdd:PRK13536 251 IAEGRPHALIDEH 263
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
926-1121 |
2.79e-14 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 72.91 E-value: 2.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 926 LSARYAGAERDA---LDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGLCA 1002
Cdd:cd03231 1 LEADELTCERDGralFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1003 QDAHIFDSSIRENLRLARTGATDEELRAALDRARLLDWaEALPAgldtlvgehgARLSGGQRQRLALARAILADFPVLVL 1082
Cdd:cd03231 81 APGIKTTLSVLENLRFWHADHSDEQVEEALARVGLNGF-EDRPV----------AQLSAGQQRRVALARLLLSGRPLWIL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2351811981 1083 DEPAEHLDLATADALTADLLA-ATRGRTTVLITHRLQGLE 1121
Cdd:cd03231 150 DEPTTALDKAGVARFAEAMAGhCARGGMVVLTTHQDLGLS 189
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
932-1138 |
2.95e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 74.35 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 932 GAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACvLEGDT--VRGFVGLCAQD----- 1004
Cdd:PRK13633 20 STEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTS-DEENLwdIRNKAGMVFQNpdnqi 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1005 -AHIFDSSIR---ENLrlartGATDEELRAALDrarlldwaEALPAgldtlVGEHGAR------LSGGQRQRLALArAIL 1074
Cdd:PRK13633 99 vATIVEEDVAfgpENL-----GIPPEEIRERVD--------ESLKK-----VGMYEYRrhaphlLSGGQKQRVAIA-GIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 1075 ADFP-VLVLDEPAEHLDLATADAL--TADLLAATRGRTTVLITHRLQglEAV--DEVVVLEAGRVVQRG 1138
Cdd:PRK13633 160 AMRPeCIIFDEPTAMLDPSGRREVvnTIKELNKKYGITIILITHYME--EAVeaDRIIVMDSGKVVMEG 226
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
921-1135 |
3.17e-14 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 73.15 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARY--AGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVL-EGDTVR-- 995
Cdd:TIGR02211 2 LKCENLGKRYqeGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLsSNERAKlr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 996 ----GFVglcAQDAHIF-DSSIREN----LRLARTGATDEELRAAldrarlldwaEALPA-GLDTLVGEHGARLSGGQRQ 1065
Cdd:TIGR02211 82 nkklGFI---YQFHHLLpDFTALENvampLLIGKKSVKEAKERAY----------EMLEKvGLEHRINHRPSELSGGERQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2351811981 1066 RLALARAiLADFPVLVL-DEPAEHLDLATADALTADLLAATRGRTT--VLITHRLQGLEAVDEVVVLEAGRVV 1135
Cdd:TIGR02211 149 RVAIARA-LVNQPSLVLaDEPTGNLDNNNAKIIFDLMLELNRELNTsfLVVTHDLELAKKLDRVLEMKDGQLF 220
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
350-544 |
3.21e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 74.34 E-value: 3.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 350 LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERW--------------------RER 409
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRkafrrdiqmvfqdsisavnpRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 410 IAWVPQRPYLFAGTIAENVRLARpdaddgaVAAALRDAGAYDFVAE-LPdgaqtllgedgAGLSAGQRQRLALARAFLAD 488
Cdd:PRK10419 108 VREIIREPLRHLLSLDKAERLAR-------ASEMLRAVDLDDSVLDkRP-----------PQLSGGQLQRVCLARALAVE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 489 RPLLLLDEPTASLDGETEAGIVEAVRRLAQ--GRTVLLVVHRPALLP-LADRVVRLEPG 544
Cdd:PRK10419 170 PKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVErFCQRVMVMDNG 228
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
937-1138 |
3.32e-14 |
|
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: 73.52 E-value: 3.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 937 ALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGLCAQDAH-IFDSSIREN 1015
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQlWWDLPVIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1016 LRLART--GATDEELRAALDR-ARLLDWAEAlpagLDTLVgehgARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLA 1092
Cdd:cd03267 116 FYLLAAiyDLPPARFKKRLDElSELLDLEEL----LDTPV----RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2351811981 1093 TADALTADLLAATRGR-TTVLIT-HRLQGLEAV-DEVVVLEAGRVVQRG 1138
Cdd:cd03267 188 AQENIRNFLKEYNRERgTTVLLTsHYMKDIEALaRRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
346-553 |
4.18e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 73.87 E-value: 4.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 346 GEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAP-ERWRERIAWVPQRPYL-FAG- 422
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGIVFQNPETqFVGr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 423 TIAENVRLA------RPDADDGAVAAALRDAGAYDFVAELPDgaqtllgedgaGLSAGQRQRLALARAFLADRPLLLLDE 496
Cdd:PRK13644 94 TVEEDLAFGpenlclPPIEIRKRVDRALAEIGLEKYRHRSPK-----------TLSGGQGQCVALAGILTMEPECLIFDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2351811981 497 PTASLDGETEAGIVEAVRRL-AQGRTVLLVVHRPALLPLADRVVRLEPGATLRPEKPE 553
Cdd:PRK13644 163 VTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPE 220
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
887-1138 |
4.59e-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: 77.36 E-value: 4.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 887 RVKRSAERVYEVLDApppVREPDSPAGTPASPFPLE---------VRGLSARYAGAERDALDSVDLRLTAGRRIAVVGPS 957
Cdd:TIGR01257 889 REERALEKTEPLTEE---MEDPEHPEGINDSFFERElpglvpgvcVKNLVKIFEPSGRPAVDRLNITFYENQITAFLGHN 965
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 958 GSGKTTLAQVLLRFLDAREGTYRIGGVDacvLEG--DTVRGFVGLCAQDAHIFdssirENLRLARTGATDEELRA-ALDR 1034
Cdd:TIGR01257 966 GAGKTTTLSILTGLLPPTSGTVLVGGKD---IETnlDAVRQSLGMCPQHNILF-----HHLTVAEHILFYAQLKGrSWEE 1037
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1035 ARLLDWAEALPAGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTADLLAATRGRTTVLIT 1114
Cdd:TIGR01257 1038 AQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMST 1117
|
250 260
....*....|....*....|....*
gi 2351811981 1115 HRLQGLEAV-DEVVVLEAGRVVQRG 1138
Cdd:TIGR01257 1118 HHMDEADLLgDRIAIISQGRLYCSG 1142
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
934-1139 |
7.31e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 72.81 E-value: 7.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 934 ERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGvdacvlegdTVRGFVGLcaqdAHIFDSSI- 1012
Cdd:COG1134 38 EFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG---------RVSALLEL----GAGFHPELt 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1013 -RENLRL-ART-GATDEELRAALDRArlLDWAEaLPAGLDTLVGehgaRLSGGQRQRLALARAILADFPVLVLDEpAehl 1089
Cdd:COG1134 105 gRENIYLnGRLlGLSRKEIDEKFDEI--VEFAE-LGDFIDQPVK----TYSSGMRARLAFAVATAVDPDILLVDE-V--- 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 1090 dLATADA--------LTADLLAatRGRTTVLITHRLQGLEAV-DEVVVLEAGRVVQRGP 1139
Cdd:COG1134 174 -LAVGDAafqkkclaRIRELRE--SGRTVIFVSHSMGAVRRLcDRAIWLEKGRLVMDGD 229
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
349-544 |
1.00e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 73.16 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 349 SLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLA--TLAPERWRERIAWVPQRP--YLFAGTI 424
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQYPeyQLFEETI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 425 AENVRLArpdaddgAVAAALRDAGAYDFVAElpdgAQTLLGEDGAG--------LSAGQRQRLALArAFLADRP-LLLLD 495
Cdd:PRK13637 102 EKDIAFG-------PINLGLSEEEIENRVKR----AMNIVGLDYEDykdkspfeLSGGQKRRVAIA-GVVAMEPkILILD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2351811981 496 EPTASLDGETEAGIVEAVRRLAQ--GRTVLLVVHR-PALLPLADRVVRLEPG 544
Cdd:PRK13637 170 EPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSmEDVAKLADRIIVMNKG 221
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
938-1138 |
1.04e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 73.96 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 938 LDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRgfVGLCAQDAHIFDS-SIRENL 1016
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK--VGFVFQHYALFRHmTVFDNI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1017 RLARTGATDEEL--RAALDR--ARLLDWAEalpagLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLA 1092
Cdd:PRK10851 96 AFGLTVLPRRERpnAAAIKAkvTQLLEMVQ-----LAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2351811981 1093 TADALTADL--LAATRGRTTVLITH-RLQGLEAVDEVVVLEAGRVVQRG 1138
Cdd:PRK10851 171 VRKELRRWLrqLHEELKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAG 219
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
333-545 |
1.12e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 75.97 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEgRGEP-SLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERIA 411
Cdd:PTZ00243 1309 LVFEGVQMRYR-EGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFS 1387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 412 WVPQRPYLFAGTIAENVrlaRPDADDGAVA--AALRDAGAYDFVAELPDGAQTLLGEDGAGLSAGQRQRLALARAFLA-D 488
Cdd:PTZ00243 1388 MIPQDPVLFDGTVRQNV---DPFLEASSAEvwAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKkG 1464
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2351811981 489 RPLLLLDEPTASLDGETEAGIVEAVRRLAQGRTVLLVVHRPALLPLADRVVRLEPGA 545
Cdd:PTZ00243 1465 SGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGA 1521
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
333-527 |
1.38e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 71.80 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRheGRgepsLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTaPDEGRVRVGGVDLATLAPERWRERIAW 412
Cdd:COG4138 1 LQLNDVAVA--GR----LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 413 VPQR-PYLFAGTIAENVRLARPDADDGAVAAALrdagaydfVAELPD--GAQTLLGEDGAGLSAGQRQRLALARAFL--- 486
Cdd:COG4138 74 LSQQqSPPFAMPVFQYLALHQPAGASSEAVEQL--------LAQLAEalGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvw 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2351811981 487 -ADRP---LLLLDEPTASLDGETEAGIVEAVRRLA-QGRTVLLVVH 527
Cdd:COG4138 146 pTINPegqLLLLDEPMNSLDVAQQAALDRLLRELCqQGITVVMSSH 191
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
921-1133 |
1.40e-13 |
|
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: 71.31 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYA-----GAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRI----GGVDACVLEG 991
Cdd:COG4778 5 LEVENLSKTFTlhlqgGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDLAQASP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 992 DTV----RGFVGLCAQdahiFdssirenLR-LARTGATD---EELRAA-LDRARLLDWAEALPAGLDtlVGEHGARL--- 1059
Cdd:COG4778 85 REIlalrRRTIGYVSQ----F-------LRvIPRVSALDvvaEPLLERgVDREEARARARELLARLN--LPERLWDLppa 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2351811981 1060 --SGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTADLLAA-TRGRTTVLITHRLQGLEAV-DEVVVLEAGR 1133
Cdd:COG4778 152 tfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkARGTAIIGIFHDEEVREAVaDRVVDVTPFS 229
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
17-274 |
1.40e-13 |
|
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: 72.83 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 17 FFLAAVVALGVVGAALVIAQamLVADVVVGGFEDGLTVSGLRTPLILLAAVALGRALVSWLTELAAYRASAAVKSELRGR 96
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPR--IIGRAIDALTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRND 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 97 LLDRAAELGPGLLSDRRTGSLVTLATRGVDALDDYFARYLPQLGLAVVVPVAVLARIVTEDWVSAAIIVVTLPLIPLFMI 176
Cdd:cd18541 79 LFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 177 LIGwatqSRMDRQWRL----LSRLSGHFLDVVAGLPTLKVFGRAKAQAESIRAITSQYRRATLRTLRI-AFLSSFaLELL 251
Cdd:cd18541 159 RLG----KKIHKRFRKvqeaFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVdALFFPL-IGLL 233
|
250 260
....*....|....*....|...
gi 2351811981 252 ATLSVALVAVTIGMRLVHGELDL 274
Cdd:cd18541 234 IGLSFLIVLWYGGRLVIRGTITL 256
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
921-1147 |
1.49e-13 |
|
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: 71.42 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGaeRDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTvRGFVGL 1000
Cdd:cd03218 1 LRAENLSKRYGK--RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 C--AQDAHIF-DSSIRENLRLARTGATDeelraalDRARLLDWAEALPA--GLDTLVGEHGARLSGGQRQRLALARAILA 1075
Cdd:cd03218 78 GylPQEASIFrKLTVEENILAVLEIRGL-------SKKEREEKLEELLEefHITHLRKSKASSLSGGERRRVEIARALAT 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2351811981 1076 DFPVLVLDEPAEHLD-LATAD--ALTADLlaATRGrTTVLIT-HRL-QGLEAVDEVVVLEAGRVVQRGPYADLTAEE 1147
Cdd:cd03218 151 NPKFLLLDEPFAGVDpIAVQDiqKIIKIL--KDRG-IGVLITdHNVrETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
934-1138 |
1.53e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 72.47 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 934 ERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGV----DACVLEGDTVRGFVGLCAQ--DAHI 1007
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlitsTSKNKDIKQIRKKVGLVFQfpESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1008 FDSSIRENLRLA--RTGATDEELRA-ALDRARLLDWAEalpagldTLVGEHGARLSGGQRQRLALArAILADFP-VLVLD 1083
Cdd:PRK13649 99 FEETVLKDVAFGpqNFGVSQEEAEAlAREKLALVGISE-------SLFEKNPFELSGGQMRRVAIA-GILAMEPkILVLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2351811981 1084 EPAEHLDLATADALTaDLLAATR--GRTTVLITHRLQGL-EAVDEVVVLEAGRVVQRG 1138
Cdd:PRK13649 171 EPTAGLDPKGRKELM-TLFKKLHqsGMTIVLVTHLMDDVaNYADFVYVLEKGKLVLSG 227
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
350-540 |
1.56e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 71.39 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 350 LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATL-----APERWRErIAWVPQRPYLFAG-T 423
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaakAELRNQK-LGFIYQFHHLLPDfT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 424 IAENVrlARPDADDGAVAaalrdagaydfvAELPDGAQTLLGEDG---------AGLSAGQRQRLALARAFLADRPLLLL 494
Cdd:PRK11629 104 ALENV--AMPLLIGKKKP------------AEINSRALEMLAAVGlehranhrpSELSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2351811981 495 DEPTASLDGETEAGIVEAVRRL--AQGRTVLLVVHRpalLPLADRVVR 540
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLGELnrLQGTAFLVVTHD---LQLAKRMSR 214
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
19-311 |
1.73e-13 |
|
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: 72.44 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 19 LAAVVALGVVGAALVIAQAMLVA---DVVVGGFEDGLTV--SGLRTPLILLAAVALGRALVSWLTELAAYRASAAVKSEL 93
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGkaiDLIIEGLGGGGGVdfSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 94 RGRLLDRAAELgPglLS--DRRT-GSLVTLATRGVDALDDYFARYLPQLglavvvpvavLARIVT----------EDWVS 160
Cdd:cd18547 81 RKDLFEKLQRL-P--LSyfDTHShGDIMSRVTNDVDNISQALSQSLTQL----------ISSILTivgtlimmlyISPLL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 161 AAIIVVTLPLIPLFMILIGWATQSRMDRQWRLLSRLSGHFLDVVAGLPTLKVFGRAKAQAESIRAITSQYRRATLRTLRI 240
Cdd:cd18547 148 TLIVLVTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFY 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2351811981 241 AFLSSFALELLATLSVALVAVTIGMRLVHGELDLytGLVV--LILAPEAYLPIRQVGAQYHAAAEGLSAAEEI 311
Cdd:cd18547 228 SGLLMPIMNFINNLGYVLVAVVGGLLVINGALTV--GVIQafLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
937-1146 |
1.81e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 72.46 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 937 ALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVL----EGDTVRGFVGLCAQ--DAHIFDS 1010
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTskqkEIKPVRKKVGVVFQfpESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1011 SIRENLRLA--RTGATDEEL-RAALDRARLLdwaealpaGLDTLVGEHGA-RLSGGQRQRLALARAILADFPVLVLDEPA 1086
Cdd:PRK13643 101 TVLKDVAFGpqNFGIPKEKAeKIAAEKLEMV--------GLADEFWEKSPfELSGGQMRRVAIAGILAMEPEVLVLDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2351811981 1087 EHLDlATADALTADLLAATR--GRTTVLITHRLQGL-EAVDEVVVLEAGRVVQRGPYADLTAE 1146
Cdd:PRK13643 173 AGLD-PKARIEMMQLFESIHqsGQTVVLVTHLMDDVaDYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
930-1090 |
2.08e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 70.90 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 930 YAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGLCAQDAHIFD 1009
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1010 SSIRENLRLA---RTGATDEE-LRAALDRArlldwaeALPaglDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEP 1085
Cdd:PRK10247 95 DTVYDNLIFPwqiRNQQPDPAiFLDDLERF-------ALP---DTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
....*
gi 2351811981 1086 AEHLD 1090
Cdd:PRK10247 165 TSALD 169
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
934-1138 |
2.22e-13 |
|
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: 70.64 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 934 ERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTvrGFVGlcaqdahifDSSIR 1013
Cdd:cd03220 34 EFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGG--GFNP---------ELTGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1014 ENLRLART--GATDEELRAALDraRLLDWAEaLPAGLDTLVGEhgarLSGGQRQRLALARAILADFPVLVLDEPaehldL 1091
Cdd:cd03220 103 ENIYLNGRllGLSRKEIDEKID--EIIEFSE-LGDFIDLPVKT----YSSGMKARLAFAIATALEPDILLIDEV-----L 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 1092 ATADALT----ADLLAATR--GRTTVLITHRLQGLEAV-DEVVVLEAGRVVQRG 1138
Cdd:cd03220 171 AVGDAAFqekcQRRLRELLkqGKTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
19-272 |
2.87e-13 |
|
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: 71.75 E-value: 2.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 19 LAAVVALGVVGAALVIAQAMLVAdvvvGGFEDGLtVSGLRTPLILLAAVALGRALVSWLTELAAYRASA----AVKSELR 94
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVR----YGIDSGV-RAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGrtgeRLLYDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 95 GRLLDRAAELGPGLLSDRRTGSLVTLATRGVDALDDYFARYLPQLGLAVVVPVAVLARIVTEDWVSAAIIVVTLPLiplf 174
Cdd:cd18546 76 LRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPP---- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 175 MILIGWATQSRMDRQWRL----LSRLSGHFLDVVAGLPTLKVFGRAKAQAESIRAITSQYRRATLRTLRIAFLSSFALEL 250
Cdd:cd18546 152 LALATRWFRRRSSRAYRRarerIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVEL 231
|
250 260
....*....|....*....|..
gi 2351811981 251 LATLSVALVAVTIGMRLVHGEL 272
Cdd:cd18546 232 LGNLATAAVLLVGAWRVAAGTL 253
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
18-311 |
2.87e-13 |
|
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: 71.68 E-value: 2.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 18 FLAAVVALgVVGAALVIAQAMLVADVVVGGFEDGLTVSGLRTPLILLAAVALgRALVSWLTELAAYRASAAVKSELRGRL 97
Cdd:cd18552 1 LALAILGM-ILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLL-RGLASYLQTYLMAYVGQRVVRDLRNDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 98 LDRAAELGPGLLSDRRTGSLVTLATRGVDALDDYFARYLPQLGLAVVVPVAVLARIVTEDWVSAAIIVVTLPLIPLFMIL 177
Cdd:cd18552 79 FDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 178 IGWATQSRMDRQWRLLSRLSGHFLDVVAGLPTLKVFGRAKAQAESIRAITSQYRRATLRTLRIAFLSSFALELLATLSVA 257
Cdd:cd18552 159 IGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2351811981 258 LVAVTIGMRLVHGELDL--YTGLVVLILApeAYLPIRQVGAQYHAAAEGLSAAEEI 311
Cdd:cd18552 239 LVLWYGGYQVISGELTPgeFISFITALLL--LYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
329-544 |
2.96e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 70.68 E-value: 2.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 329 ESLRLELEGVTVrHEGRGEpSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPER-WR 407
Cdd:PRK11614 2 EKVMLSFDKVSA-HYGKIQ-ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 408 ERIAWVPQRPYLFAG-TIAENvrLARPDADDGAVAAALRDAGAYDFVAELPDGAQTLLGEdgagLSAGQRQRLALARAFL 486
Cdd:PRK11614 80 EAVAIVPEGRRVFSRmTVEEN--LAMGGFFAERDQFQERIKWVYELFPRLHERRIQRAGT----MSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 487 ADRPLLLLDEPTASLDGETEAGIVEAVRRL-AQGRTVLLVVHRP-ALLPLADRVVRLEPG 544
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLrEQGMTIFLVEQNAnQALKLADRGYVLENG 213
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
364-544 |
3.21e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 72.60 E-value: 3.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 364 ALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGG---VDLAT---LAPERwrERIAWVPQRPYLFAG-TIAENVR--LARpd 434
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKgicLPPEK--RRIGYVFQDARLFPHyKVRGNLRygMAK-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 435 addgavaaalRDAGAYDFVAELPdGAQTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVR 514
Cdd:PRK11144 104 ----------SMVAQFDKIVALL-GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLE 172
|
170 180 190
....*....|....*....|....*....|...
gi 2351811981 515 RLAQ--GRTVLLVVHR-PALLPLADRVVRLEPG 544
Cdd:PRK11144 173 RLAReiNIPILYVSHSlDEILRLADRVVVLEQG 205
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
333-527 |
3.55e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 72.44 E-value: 3.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHegrGEPS-LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERwRErIA 411
Cdd:PRK11432 7 VVLKNITKRF---GSNTvIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ-RD-IC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 412 WVPQRPYLFAG-TIAENVRLARPDADDGAVAAALRDAGAYDFVaelpdgaqtllgeDGAG--------LSAGQRQRLALA 482
Cdd:PRK11432 82 MVFQSYALFPHmSLGENVGYGLKMLGVPKEERKQRVKEALELV-------------DLAGfedryvdqISGGQQQRVALA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2351811981 483 RAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQ--GRTVLLVVH 527
Cdd:PRK11432 149 RALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTH 195
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
346-530 |
3.64e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 71.28 E-value: 3.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 346 GEPSLDHASLVVDEGETVALVGPSGVGKSTLL-------DVVLGFTApdEGRVRVGGVDLATLAPE-RWRERIAWVPQRP 417
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLrtlnrmnDKVSGYRY--SGDVLLGGRSIFNYRDVlEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 418 YLFAGTIAENV-------RLARPDADDGAVAAALRDAGAYDFVAELpdgaqtlLGEDGAGLSAGQRQRLALARAFLADRP 490
Cdd:PRK14271 111 NPFPMSIMDNVlagvrahKLVPRKEFRGVAQARLTEVGLWDAVKDR-------LSDSPFRLSGGQQQLLCLARTLAVNPE 183
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2351811981 491 LLLLDEPTASLDGETEAGIVEAVRRLAQGRTVLLVVHRPA 530
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLA 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
333-539 |
4.05e-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: 73.57 E-value: 4.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTV--RHEGRGEPSLDHASLVVDEGETVALVGPSGVGKS----TLLDVVLGFTAPDEGRVRVGGVDLATLAPERW 406
Cdd:COG4172 7 LSVEDLSVafGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 407 RE----RIAWVPQRPY-----LFagTI----AENVRLARPdaddgavaaaLRDAGAYDFVAEL------PDgAQTLLGED 467
Cdd:COG4172 87 RRirgnRIAMIFQEPMtslnpLH--TIgkqiAEVLRLHRG----------LSGAAARARALELlervgiPD-PERRLDAY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 468 GAGLSAGQRQRLALARAfLADRP-LLLLDEPTASLDGETEAGIVEAVRRLAQ--GRTVLL------VVHRpallpLADRV 538
Cdd:COG4172 154 PHQLSGGQRQRVMIAMA-LANEPdLLIADEPTTALDVTVQAQILDLLKDLQRelGMALLLithdlgVVRR-----FADRV 227
|
.
gi 2351811981 539 V 539
Cdd:COG4172 228 A 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
921-1143 |
4.38e-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: 73.18 E-value: 4.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAERD--ALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAR----EGTYRIGGVDACVLEGDTV 994
Cdd:COG4172 7 LSVEDLSVAFGQGGGTveAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 995 RGFVGlcAQDAHIFD---SS----------IRENLRLARTgatdeeLRAALDRARLLDWAEalpagldtLVGEHGAR--- 1058
Cdd:COG4172 87 RRIRG--NRIAMIFQepmTSlnplhtigkqIAEVLRLHRG------LSGAAARARALELLE--------RVGIPDPErrl 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1059 ------LSGGQRQRLALARAILADFPVLVLDEPAEHLDlATADALTADLLA---ATRGRTTVLITHRLqGL--EAVDEVV 1127
Cdd:COG4172 151 dayphqLSGGQRQRVMIAMALANEPDLLIADEPTTALD-VTVQAQILDLLKdlqRELGMALLLITHDL-GVvrRFADRVA 228
|
250
....*....|....*.
gi 2351811981 1128 VLEAGRVVQRGPYADL 1143
Cdd:COG4172 229 VMRQGEIVEQGPTAEL 244
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
333-528 |
5.88e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 70.91 E-value: 5.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAperwRERIAW 412
Cdd:COG4152 2 LELKGLTKRFGDK--TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 413 VPQRPYLFAG-TIAEN-VRLARpdaddgavaaaLRDAGAYDFVA---------ELPDGAQTLLGEdgagLSAGQRQRLAL 481
Cdd:COG4152 76 LPEERGLYPKmKVGEQlVYLAR-----------LKGLSKAEAKRradewlerlGLGDRANKKVEE----LSKGNQQKVQL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2351811981 482 ARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLA-QGRTVLLVVHR 528
Cdd:COG4152 141 IAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAaKGTTVIFSSHQ 188
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
921-1145 |
5.99e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 70.51 E-value: 5.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAG-AERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVG 999
Cdd:PRK13642 5 LEVENLVFKYEKeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1000 LCAQ--DAHIFDSSIRENLR--LARTGATDEELRAALDRARL----LDWAEALPAgldtlvgehgaRLSGGQRQRLALAR 1071
Cdd:PRK13642 85 MVFQnpDNQFVGATVEDDVAfgMENQGIPREEMIKRVDEALLavnmLDFKTREPA-----------RLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2351811981 1072 AILADFPVLVLDEPAEHLDlATADALTADLLAATRGR---TTVLITHRLQGLEAVDEVVVLEAGRVVQRGPYADLTA 1145
Cdd:PRK13642 154 IIALRPEIIILDESTSMLD-PTGRQEIMRVIHEIKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
350-527 |
7.66e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 69.76 E-value: 7.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 350 LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGvdlatlaperwRERIAWVPQRPYLFAG---TIAE 426
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-----------KLRIGYVPQKLYLDTTlplTVNR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 427 NVRLaRPDADDGAVAAALRDAgaydfvaelpdGAQTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETE 506
Cdd:PRK09544 89 FLRL-RPGTKKEDILPALKRV-----------QAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
|
170 180
....*....|....*....|...
gi 2351811981 507 AGIVEAVRRLAQ--GRTVLLVVH 527
Cdd:PRK09544 157 VALYDLIDQLRRelDCAVLMVSH 179
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
349-544 |
1.10e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.15 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 349 SLDHASLVVD-----EGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRvggvdlatlaperWRERIAWVPQrpYL---F 420
Cdd:PRK13409 349 KLGDFSLEVEggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD-------------PELKISYKPQ--YIkpdY 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 421 AGTIAENVRLARPdaddgavaaalrDAGAYDFVAEL--PDGAQTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPT 498
Cdd:PRK13409 414 DGTVEDLLRSITD------------DLGSSYYKSEIikPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 499 ASLDGETEAGIVEAVRRLAQGR--TVLLVVHRPALLP-LADR--VVRLEPG 544
Cdd:PRK13409 482 AHLDVEQRLAVAKAIRRIAEEReaTALVVDHDIYMIDyISDRlmVFEGEPG 532
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
349-552 |
1.11e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 70.04 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 349 SLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGgvDLATLAP-------ERWRERIAWVPQRP--YL 419
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVG--DYAIPANlkkikevKRLRKEIGLVFQFPeyQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 420 FAGTIAENVRLArPDADDGAVAAalrdagAYDFVAELPDGAQtlLGEDGAG-----LSAGQRQRLALARAFLADRPLLLL 494
Cdd:PRK13645 104 FQETIEKDIAFG-PVNLGENKQE------AYKKVPELLKLVQ--LPEDYVKrspfeLSGGQKRRVALAGIIAMDGNTLVL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 495 DEPTASLDGETEAGIVEAVRRL--AQGRTVLLVVHR-PALLPLADRVVRLEPGATLRPEKP 552
Cdd:PRK13645 175 DEPTGGLDPKGEEDFINLFERLnkEYKKRIIMVTHNmDQVLRIADEVIVMHEGKVISIGSP 235
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
921-1159 |
1.14e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.96 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGvDACVLEG--DTVRGFV 998
Cdd:PRK10762 5 LQLKGIDKAFPGVK--ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG-KEVTFNGpkSSQEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 999 GLCAQDAHIFDS-SIRENLRLART-----GATD-EELRAALDR--ARLldwaeALPAGLDTLVGEhgarLSGGQRQRLAL 1069
Cdd:PRK10762 82 GIIHQELNLIPQlTIAENIFLGREfvnrfGRIDwKKMYAEADKllARL-----NLRFSSDKLVGE----LSIGEQQMVEI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1070 ARAILADFPVLVLDEPAEhldlATADALTADLLAATR-----GRTTVLITHRLQGL-EAVDEVVVLEAGRVVQRGPYADL 1143
Cdd:PRK10762 153 AKVLSFESKVIIMDEPTD----ALTDTETESLFRVIRelksqGRGIVYISHRLKEIfEICDDVTVFRDGQFIAEREVADL 228
|
250
....*....|....*.
gi 2351811981 1144 TaEEGPLRRMLERERE 1159
Cdd:PRK10762 229 T-EDSLIEMMVGRKLE 243
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
921-1143 |
1.19e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 70.90 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLaqvlLR-------------FLDAREGTYR-IGGVDA 986
Cdd:PRK11432 7 VVLKNITKRFGSNT--VIDNLNLTIKQGTMVTLLGPSGCGKTTV----LRlvaglekptegqiFIDGEDVTHRsIQQRDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 987 CVlegdtvrgfvglcaqdahIFDS-------SIRENLR--LARTGATDEELRAALDRA-RLLDWAealpaGL-DTLVGEh 1055
Cdd:PRK11432 81 CM------------------VFQSyalfphmSLGENVGygLKMLGVPKEERKQRVKEAlELVDLA-----GFeDRYVDQ- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1056 garLSGGQRQRLALARAILADFPVLVLDEPAEHLDlatadaltADLLAATR----------GRTTVLITHRLQGLEAV-D 1124
Cdd:PRK11432 137 ---ISGGQQQRVALARALILKPKVLLFDEPLSNLD--------ANLRRSMRekirelqqqfNITSLYVTHDQSEAFAVsD 205
|
250
....*....|....*....
gi 2351811981 1125 EVVVLEAGRVVQRGPYADL 1143
Cdd:PRK11432 206 TVIVMNKGKIMQIGSPQEL 224
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
343-544 |
1.21e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 69.73 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 343 EGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDlATLAPERW--RERIAWVPQRP--Y 418
Cdd:PRK13633 19 ESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD-TSDEENLWdiRNKAGMVFQNPdnQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 419 LFAGTIAENVRLA------RPDADDGAVAAALRDAGAYDFVAELPDgaqtllgedgaGLSAGQRQRLALArAFLADRP-L 491
Cdd:PRK13633 98 IVATIVEEDVAFGpenlgiPPEEIRERVDESLKKVGMYEYRRHAPH-----------LLSGGQKQRVAIA-GILAMRPeC 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2351811981 492 LLLDEPTASLDGETEAGIVEAVRRLAQ--GRTVLLVVHRPALLPLADRVVRLEPG 544
Cdd:PRK13633 166 IIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSG 220
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
921-1171 |
1.22e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 71.76 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLlRFLDAREGT-----YRIGGVDACVLEGdtVR 995
Cdd:TIGR03269 1 IEVKNLTKKFDGKE--VLKNISFTIEEGEVLGILGRSGAGKSVLMHVL-RGMDQYEPTsgriiYHVALCEKCGYVE--RP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 996 GFVG---------LCAQDAHIFDSS--IRENLR------LARTGATDEELRAALDRARLLDWA-----EALPAGLDtLVG 1053
Cdd:TIGR03269 76 SKVGepcpvcggtLEPEEVDFWNLSdkLRRRIRkriaimLQRTFALYGDDTVLDNVLEALEEIgyegkEAVGRAVD-LIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1054 E--------HGAR-LSGGQRQRLALARAiLADFPVLVL-DEPAEHLDLATADALTADLLAATR--GRTTVLITHRLQGLE 1121
Cdd:TIGR03269 155 MvqlshritHIARdLSGGEKQRVVLARQ-LAKEPFLFLaDEPTGTLDPQTAKLVHNALEEAVKasGISMVLTSHWPEVIE 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 1122 AV-DEVVVLEAGRVVQRGPYADLTAEEGPLRRMLERERETEgVAEEALGVR 1171
Cdd:TIGR03269 234 DLsDKAIWLENGEIKEEGTPDEVVAVFMEGVSEVEKECEVE-VGEPIIKVR 283
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
333-528 |
1.36e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.48 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGrgEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLA-TLAPERWRERIA 411
Cdd:PRK11288 5 LSFDGIGKTFPG--VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 412 WVPQR----PYLfagTIAENVRLAR-PDADDGAVAAALRdAGAYDFVAELPD--GAQTLLGEdgagLSAGQRQRLALARA 484
Cdd:PRK11288 83 IIYQElhlvPEM---TVAENLYLGQlPHKGGIVNRRLLN-YEAREQLEHLGVdiDPDTPLKY----LSIGQRQMVEIAKA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2351811981 485 FLADRPLLLLDEPTASLDG-ETEA--GIVEAVRrlAQGRTVLLVVHR 528
Cdd:PRK11288 155 LARNARVIAFDEPTSSLSArEIEQlfRVIRELR--AEGRVILYVSHR 199
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
346-553 |
1.45e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 69.34 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 346 GEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGG--VDLATLAPERWRERIAWVPQRP--YLFA 421
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTVGIVFQNPddQLFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 422 GTIAENV-----RLARPD-ADDGAVAAALRDAGAYDFVAELPDgaqtllgedgaGLSAGQRQRLALArAFLADRP-LLLL 494
Cdd:PRK13639 94 PTVEEDVafgplNLGLSKeEVEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIA-GILAMKPeIIVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 495 DEPTASLDGETEAGIVEAVRRL-AQGRTVLLVVHRPALLPL-ADRVVRLEPGATLRPEKPE 553
Cdd:PRK13639 162 DEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPK 222
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
350-544 |
1.55e-12 |
|
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: 68.33 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 350 LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGvdlatlaperwreRIAWVpqrpyLFAG------- 422
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-------------RVSSL-----LGLGggfnpel 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 423 TIAENVRL-ARPDADDGAVAAALRDAgAYDFvAELPDGAQTLLGEdgagLSAGQRQRLALARAFLADRPLLLLDEPTASL 501
Cdd:cd03220 100 TGRENIYLnGRLLGLSRKEIDEKIDE-IIEF-SELGDFIDLPVKT----YSSGMKARLAFAIATALEPDILLIDEVLAVG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2351811981 502 DGETEAGIVEAVR-RLAQGRTVLLVVHRPALL-PLADRVVRLEPG 544
Cdd:cd03220 174 DAAFQEKCQRRLReLLKQGKTVILVSHDPSSIkRLCDRALVLEKG 218
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
344-557 |
1.84e-12 |
|
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: 68.59 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 344 GRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVrvgGVDLATlaperwrerIAWVPQrpYL---F 420
Cdd:cd03237 9 TLGEFTLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI---EIELDT---------VSYKPQ--YIkadY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 421 AGTIAENVRlarpdaddgavaAALRDAGAYD-FVAEL--PDGAQTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEP 497
Cdd:cd03237 75 EGTVRDLLS------------SITKDFYTHPyFKTEIakPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEP 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2351811981 498 TASLDGETEAGIVEAVRRLAQG--RTVLLVVHRPALLP-LADRVVRLE--PGATLRPEKPEGSVA 557
Cdd:cd03237 143 SAYLDVEQRLMASKVIRRFAENneKTAFVVEHDIIMIDyLADRLIVFEgePSVNGVANPPQSLRS 207
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
941-1138 |
1.86e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 70.44 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 941 VDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEgDTVRGfVGLCAQDAHIFDS-SIREN---- 1015
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVP-PAERG-VGMVFQSYALYPHlSVAENmsfg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1016 LRLArtGATDEELRAALDRArlldwAEALPagLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATAD 1095
Cdd:PRK11000 100 LKLA--GAKKEEINQRVNQV-----AEVLQ--LAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2351811981 1096 ALTADL--LAATRGRTTVLITH-RLQGLEAVDEVVVLEAGRVVQRG 1138
Cdd:PRK11000 171 QMRIEIsrLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
934-1138 |
1.88e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 68.92 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 934 ERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGV------DACVLEGDTVRGFVGLCAQDAHI 1007
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1008 FDS-SIRENLR--LARTGATDE-ELRAALDRA--RLLDWAEALpaglDTLvGEHGARLSGGQRQRLALARAILADFPVLV 1081
Cdd:PRK14246 102 FPHlSIYDNIAypLKSHGIKEKrEIKKIVEEClrKVGLWKEVY----DRL-NSPASQLSGGQQQRLTIARALALKPKVLL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2351811981 1082 LDEPAEHLDLATADALTADLLAATRGRTTVLITHRLQGLEAV-DEVVVLEAGRVVQRG 1138
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVaDYVAFLYNGELVEWG 234
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
921-1134 |
2.09e-12 |
|
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: 66.69 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARyagaerDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVL-EGDTVRGFVG 999
Cdd:cd03215 5 LEVRGLSVK------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRsPRDAIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1000 LCAQDAH----IFDSSIRENLRLARtgatdeelraaldrarlldwaealpagldtlvgehgaRLSGGQRQRLALARAILA 1075
Cdd:cd03215 79 YVPEDRKreglVLDLSVAENIALSS-------------------------------------LLSGGNQQKVVLARWLAR 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 1076 DFPVLVLDEPAEHLDLATADALTADLL-AATRGRTTVLITHRLQGLEAV-DEVVVLEAGRV 1134
Cdd:cd03215 122 DPRVLILDEPTRGVDVGAKAEIYRLIReLADAGKAVLLISSELDELLGLcDRILVMYEGRI 182
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
921-1147 |
2.32e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 68.48 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGD------TV 994
Cdd:PRK11300 6 LSVSGLMMRFGGLL--AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHqiarmgVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 995 RGFvglcaQDAHIFDS-SIRENLRLA--------------RTGATDEELRAALDRArlLDWAEALpaGLDTLVGEHGARL 1059
Cdd:PRK11300 84 RTF-----QHVRLFREmTVIENLLVAqhqqlktglfsgllKTPAFRRAESEALDRA--ATWLERV--GLLEHANRQAGNL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1060 SGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTA--DLLAATRGRTTVLITHRLQGLEAV-DEVVVLEAGRvvq 1136
Cdd:PRK11300 155 AYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDEliAELRNEHNVTVLLIEHDMKLVMGIsDRIYVVNQGT--- 231
|
250
....*....|.
gi 2351811981 1137 rgPYADLTAEE 1147
Cdd:PRK11300 232 --PLANGTPEE 240
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
347-552 |
2.40e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 68.88 E-value: 2.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 347 EPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGG--VDLATLAPERWRERIAWVPQRP--YLFAG 422
Cdd:PRK13638 14 EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQDPeqQIFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 423 TIAENVRLArpdaddgavaaaLRDAG-AYDFVAELPDGAQTLLGEDG------AGLSAGQRQRLALARAFLADRPLLLLD 495
Cdd:PRK13638 94 DIDSDIAFS------------LRNLGvPEAEITRRVDEALTLVDAQHfrhqpiQCLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 496 EPTASLDGETEAGIVEAVRRL-AQGRTVLLVVHRPALL-PLADRVVRLEPGATLRPEKP 552
Cdd:PRK13638 162 EPTAGLDPAGRTQMIAIIRRIvAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAP 220
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
338-527 |
2.75e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 68.46 E-value: 2.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 338 VTVRHEGRGEPS-LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAP------------- 403
Cdd:PRK10619 8 VIDLHKRYGEHEvLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkvadknql 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 404 ERWRERIAWVPQRPYLFAG-TIAENVRLARPDADDGAVAAALRDAGAYDFVAELPDGAQtllGEDGAGLSAGQRQRLALA 482
Cdd:PRK10619 88 RLLRTRLTMVFQHFNLWSHmTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQ---GKYPVHLSGGQQQRVSIA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2351811981 483 RAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLA-QGRTVLLVVH 527
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTH 210
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
618-799 |
2.95e-12 |
|
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: 68.85 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 618 VGLMAVSGWLISRASEQ----PPVLYLMVAVTATRAFGLGRAVFRYAERLVSHDAVLKMLAELRVAVYRGLERIAPAGLR 693
Cdd:cd18561 9 TALYIAQAWLLARALARifagGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLLKLGPGYLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 694 RSRRGDLLSRLVADVDALQDYWLRWLLPAGTAVVVGAATAGFIGWLLPAAGIVLATGLLLAGAGVPLVSGACSRHAERQL 773
Cdd:cd18561 89 GERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLAKDTGRRHW 168
|
170 180
....*....|....*....|....*.
gi 2351811981 774 ApARADLATRITDLLGGTAELTVAGA 799
Cdd:cd18561 169 A-AYGRLSAQFLDSLQGMTTLKAFGA 193
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
345-502 |
3.24e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 67.61 E-value: 3.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 345 RGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLA-PERWRERIAWVPQRPYLFAGT 423
Cdd:PRK10895 14 KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLPQEASIFRRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 424 IAENVRLArpdaddgavAAALRDagayDFVAEL-PDGAQTLLGED---------GAGLSAGQRQRLALARAFLADRPLLL 493
Cdd:PRK10895 94 SVYDNLMA---------VLQIRD----DLSAEQrEDRANELMEEFhiehlrdsmGQSLSGGERRRVEIARALAANPKFIL 160
|
....*....
gi 2351811981 494 LDEPTASLD 502
Cdd:PRK10895 161 LDEPFAGVD 169
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
333-544 |
3.57e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 68.22 E-value: 3.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVR-HEGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGvDLATlAPERW--RER 409
Cdd:PRK13650 5 IEVKNLTFKyKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG-DLLT-EENVWdiRHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 410 IAWVPQRP-YLFAG-TIAENVRLARPDADDGAVAAALRDAGAYDFVaelpdGAQTLLGEDGAGLSAGQRQRLALARAfLA 487
Cdd:PRK13650 83 IGMVFQNPdNQFVGaTVEDDVAFGLENKGIPHEEMKERVNEALELV-----GMQDFKEREPARLSGGQKQRVAIAGA-VA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 488 DRP-LLLLDEPTASLDGETEAGIVEAVRRLAQ--GRTVLLVVHRPALLPLADRVVRLEPG 544
Cdd:PRK13650 157 MRPkIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNG 216
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
937-1138 |
3.79e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 68.12 E-value: 3.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 937 ALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFL--DAREGTY--RIGGVDACvlEGDTVRGFVGLCAQDAHIFDS-- 1010
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGSHieLLGRTVQR--EGRLARDIRKSRANTGYIFQQfn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1011 -----SIRENLRLARTGATdEELRAALDRARLLDWAEALPA----GLDTLVGEHGARLSGGQRQRLALARAILADFPVLV 1081
Cdd:PRK09984 97 lvnrlSVLENVLIGALGST-PFWRTCFSWFTREQKQRALQAltrvGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1082 LDEPAEHLDLATADALTADL--LAATRGRTTVLITHRLQ-GLEAVDEVVVLEAGRVVQRG 1138
Cdd:PRK09984 176 ADEPIASLDPESARIVMDTLrdINQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDG 235
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
921-1138 |
4.33e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 68.29 E-value: 4.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDT---VRGF 997
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTvwdIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 998 VGLCAQ--DAHIFDSSIRENLR--LARTGATDEEL----RAALDRARLLDWAEALPagldtlvgehgARLSGGQRQRLAL 1069
Cdd:PRK13640 86 VGIVFQnpDNQFVGATVGDDVAfgLENRAVPRPEMikivRDVLADVGMLDYIDSEP-----------ANLSGGQKQRVAI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2351811981 1070 ArAILADFP-VLVLDEPAEHLDLATADALTADL--LAATRGRTTVLITHRLQGLEAVDEVVVLEAGRVVQRG 1138
Cdd:PRK13640 155 A-GILAVEPkIIILDESTSMLDPAGKEQILKLIrkLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQG 225
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
360-544 |
4.36e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 66.82 E-value: 4.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 360 GETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPER---WRERIAWVPQRPYLFAG-TIAENVRLARPDA 435
Cdd:PRK10908 28 GEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLLMDrTVYDNVAIPLIIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 436 DDGAVAAALRDAGAYDFVAELpDGAQTLLGEdgagLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRR 515
Cdd:PRK10908 108 GASGDDIRRRVSAALDKVGLL-DKAKNFPIQ----LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEE 182
|
170 180 190
....*....|....*....|....*....|.
gi 2351811981 516 LAQ-GRTVLLVVHRPALLPLAD-RVVRLEPG 544
Cdd:PRK10908 183 FNRvGVTVLMATHDIGLISRRSyRMLTLSDG 213
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
354-527 |
4.46e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 67.27 E-value: 4.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 354 SLVVDEGETVALVGPSGVGKSTLLDVVLGFTaPDEGRVRVGGVDLATL-APERWRERIAWVPQRPYLFAGTIAENVRLAR 432
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWsAAELARHRAYLSQQQTPPFAMPVFQYLTLHQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 433 PDADDGAVaaalrDAGAYDFVAELPdGAQTLLGEDGAGLSAGQRQRLALARAFLADRP-------LLLLDEPTASLDGET 505
Cdd:PRK03695 95 PDKTRTEA-----VASALNEVAEAL-GLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPdinpagqLLLLDEPMNSLDVAQ 168
|
170 180
....*....|....*....|...
gi 2351811981 506 EAGIVEAVRRLA-QGRTVLLVVH 527
Cdd:PRK03695 169 QAALDRLLSELCqQGIAVVMSSH 191
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
917-1171 |
5.52e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.57 E-value: 5.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 917 SPFPLEVRGLSARYAGAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLlrfldarEGTYRIGGVDACVL-EGDTVR 995
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVK--ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVL-------SGVYPHGTYEGEIIfEGEELQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 996 GfvglcaqdAHIFDSS------IRENLRLAR--TGATDEELRAALDRARLLDW------AEALPAGL------DTLVGEH 1055
Cdd:PRK13549 73 A--------SNIRDTEragiaiIHQELALVKelSVLENIFLGNEITPGGIMDYdamylrAQKLLAQLkldinpATPVGNL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1056 GarlsGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTA---DLLAatRGRTTVLITHRLQGLEAV-DEVVVLEA 1131
Cdd:PRK13549 145 G----LGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDiirDLKA--HGIACIYISHKLNEVKAIsDTICVIRD 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2351811981 1132 GRVVQRGPYADLTaEEGPLRRMLERE------RETEGVAEEALGVR 1171
Cdd:PRK13549 219 GRHIGTRPAAGMT-EDDIITMMVGREltalypREPHTIGEVILEVR 263
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
355-552 |
5.66e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 67.84 E-value: 5.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 355 LVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPER----WRERIAWVPQRP--YLFAGTIAENV 428
Cdd:PRK13643 27 LEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikpVRKKVGVVFQFPesQLFEETVLKDV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 429 RLArPDADDGAVAAALRDAGAYdfvAELPDGAQTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEAG 508
Cdd:PRK13643 107 AFG-PQNFGIPKEKAEKIAAEK---LEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2351811981 509 IVEAVRRLAQ-GRTVLLVVH-RPALLPLADRVVRLEPGATLRPEKP 552
Cdd:PRK13643 183 MMQLFESIHQsGQTVVLVTHlMDDVADYADYVYLLEKGHIISCGTP 228
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
921-1143 |
6.91e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 66.92 E-value: 6.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAgaERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVlegdtVRGFVGl 1000
Cdd:PRK10619 6 LNVIDLHKRYG--EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINL-----VRDKDG- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 caqDAHIFDssiRENLRLARTGATD--------------EELRAALDRARLLDWAEAL--------PAGLDTLV-GEHGA 1057
Cdd:PRK10619 78 ---QLKVAD---KNQLRLLRTRLTMvfqhfnlwshmtvlENVMEAPIQVLGLSKQEAReravkylaKVGIDERAqGKYPV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1058 RLSGGQRQRLALARAILADFPVLVLDEPAEHLDlataDALTADLLA-----ATRGRTTVLITHRLQGLEAV-DEVVVLEA 1131
Cdd:PRK10619 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALD----PELVGEVLRimqqlAEEGKTMVVVTHEMGFARHVsSHVIFLHQ 227
|
250
....*....|..
gi 2351811981 1132 GRVVQRGPYADL 1143
Cdd:PRK10619 228 GKIEEEGAPEQL 239
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
316-539 |
7.28e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 69.28 E-value: 7.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 316 ETEPRRGGTADVPeslRLELEGVTVRHEgrgepsLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGG 395
Cdd:COG1129 243 DLFPKRAAAPGEV---VLEVEGLSVGGV------VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 396 VDLATLAP-ERWRERIAWVP---QRPYLFAG-TIAENVRLARpdADDGAVAAALRDAGAYDFVAEL-------PDGAQTL 463
Cdd:COG1129 314 KPVRIRSPrDAIRAGIAYVPedrKGEGLVLDlSIRENITLAS--LDRLSRGGLLDRRRERALAEEYikrlrikTPSPEQP 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 464 LGEdgagLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLA-QGRTVLLV---VhrPALLPLADRVV 539
Cdd:COG1129 392 VGN----LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAaEGKAVIVIsseL--PELLGLSDRIL 465
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
350-527 |
7.49e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.59 E-value: 7.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 350 LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVG-GVDLA-------TLAPERwreriawvpqrpylfa 421
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGtKLEVAyfdqhraELDPEK---------------- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 422 gTIAENVRLARPDADDGAVAaalRDAGAY--DFVAElPDGAQTLLgedgAGLSAGQRQRLALARAFLADRPLLLLDEPTA 499
Cdd:PRK11147 399 -TVMDNLAEGKQEVMVNGRP---RHVLGYlqDFLFH-PKRAMTPV----KALSGGERNRLLLARLFLKPSNLLILDEPTN 469
|
170 180 190
....*....|....*....|....*....|.
gi 2351811981 500 SLDGETeagiVEAVRRLA---QGrTVLLVVH 527
Cdd:PRK11147 470 DLDVET----LELLEELLdsyQG-TVLLVSH 495
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
345-554 |
7.70e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 67.16 E-value: 7.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 345 RGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLG-FTAPDE-------GRVRVGGVDLATLAPERWRERIAWVPQ- 415
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 416 -RPyLFAGTIAENVRLARPDADDGAVAAALRDAGAYDFVAELPdGAQTLLGEDGAGLSAGQRQRLALARAFLADRP---- 490
Cdd:PRK13547 92 aQP-AFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALA-GATALVGRDVTTLSGGELARVQFARVLAQLWPphda 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2351811981 491 -----LLLLDEPTASLDGETEAGIVEAVRRLAQ--GRTVLLVVHRPALLPL-ADRVVRLEPGATLRPEKPEG 554
Cdd:PRK13547 170 aqpprYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNLAARhADRIAMLADGAIVAHGAPAD 241
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
349-557 |
9.32e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 69.06 E-value: 9.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 349 SLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGR--VRVGG--VDLATLAPE---RWRERIAWVPQRPYLFA 421
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDewVDMTKPGPDgrgRAKRYIGILHQEYDLYP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 422 -GTIAENV----------RLARPDADDGAVAAALRDAGAYDFVAELPDgaqtllgedgaGLSAGQRQRLALARAFLADRP 490
Cdd:TIGR03269 379 hRTVLDNLteaiglelpdELARMKAVITLKMVGFDEEKAEEILDKYPD-----------ELSEGERHRVALAQVLIKEPR 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 491 LLLLDEPTASLDGETEAGIVEAV--RRLAQGRTVLLVVH-RPALLPLADRVVRLEPGATLRPEKPEGSVA 557
Cdd:TIGR03269 448 IVILDEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHdMDFVLDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
329-544 |
1.13e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 66.80 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 329 ESLRLELEGVTVRHEGrGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGG--VDLATLAPERW 406
Cdd:PRK13636 2 EDYILKVEELNYNYSD-GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 407 RERIAWVPQRP--YLFAGTIAENV-----RLARPDADDGAVaaaLRDAGAYDFVAELPDgaqtllgEDGAGLSAGQRQRL 479
Cdd:PRK13636 81 RESVGMVFQDPdnQLFSASVYQDVsfgavNLKLPEDEVRKR---VDNALKRTGIEHLKD-------KPTHCLSFGQKKRV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2351811981 480 ALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQ--GRTVLLVVHRPALLPL-ADRVVRLEPG 544
Cdd:PRK13636 151 AIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLyCDNVFVMKEG 218
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
921-1097 |
1.22e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 68.77 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGaeRDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIggvdacvlegdTVRGFVGL 1000
Cdd:PRK15064 320 LEVENLTKGFDN--GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW-----------SENANIGY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQD-AHIF--DSSIRENLRLARTGATDEE-LRAALdrARLLDWAEAlpagldtlVGEHGARLSGGQRQRLALARAILAD 1076
Cdd:PRK15064 387 YAQDhAYDFenDLTLFDWMSQWRQEGDDEQaVRGTL--GRLLFSQDD--------IKKSVKVLSGGEKGRMLFGKLMMQK 456
|
170 180
....*....|....*....|.
gi 2351811981 1077 FPVLVLDEPAEHLDLATADAL 1097
Cdd:PRK15064 457 PNVLVMDEPTNHMDMESIESL 477
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
335-527 |
1.28e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 66.44 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 335 LEGVTVRHEGrGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFtapdegrVRVGGVDLATLA-PERWRER---I 410
Cdd:PRK15056 9 VNDVTVTWRN-GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGF-------VRLASGKISILGqPTRQALQknlV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 411 AWVPQRP---YLFAGTIAENVRLARPDADDGAVAAALRDAGAYDFVAELPDGAQTLLGEDGAgLSAGQRQRLALARAFLA 487
Cdd:PRK15056 81 AYVPQSEevdWSFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGE-LSGGQKKRVFLARAIAQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2351811981 488 DRPLLLLDEPTASLDGETEAGIVEAVRRL-AQGRTVLLVVH 527
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEARIISLLRELrDEGKTMLVSTH 200
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
350-544 |
1.33e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 65.87 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 350 LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGvdlatlaperwreRIAWvpqrpyLF---AG---- 422
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-------------RVSA------LLelgAGfhpe 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 423 -TIAENVRLarpdaddgavaaalrdAGA------------YDFVAELpdgaqtllgedgAGL-----------SAGQRQR 478
Cdd:COG1134 103 lTGRENIYL----------------NGRllglsrkeidekFDEIVEF------------AELgdfidqpvktySSGMRAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 479 LALARAFLADRPLLLLDEPTASLDGE----TEAGIVEavrRLAQGRTVLLVVH-RPALLPLADRVVRLEPG 544
Cdd:COG1134 155 LAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIRE---LRESGRTVIFVSHsMGAVRRLCDRAIWLEKG 222
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
351-538 |
1.59e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 67.04 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 351 DHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRER---IAWVPQRP-------YLF 420
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdIQMIFQDPlaslnprMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 421 AGTIAENVRLARPDADDGAVAAALRDAGAYdfVAELPDgaqtLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTAS 500
Cdd:PRK15079 118 GEIIAEPLRTYHPKLSRQEVKDRVKAMMLK--VGLLPN----LINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 191
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2351811981 501 LDGETEAGIVEAVRRLAQ--GRTVLLVVHRPALLP-LADRV 538
Cdd:PRK15079 192 LDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKhISDRV 232
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
908-1171 |
1.71e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 67.55 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 908 PDSPAGTPASPFpLEVRGLSARYAGaeRDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDAC 987
Cdd:PRK11607 8 PQAKTRKALTPL-LEIRNLTKSFDG--QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 988 VLEgdTVRGFVGLCAQDAHIFDS-SIRENLRLartGATDEELRAALDRARLldwAEALpagldTLV--GEHGAR----LS 1060
Cdd:PRK11607 85 HVP--PYQRPINMMFQSYALFPHmTVEQNIAF---GLKQDKLPKAEIASRV---NEML-----GLVhmQEFAKRkphqLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1061 GGQRQRLALARAILADFPVLVLDEPAEHLDLATADAL---TADLLAATrGRTTVLITH-RLQGLEAVDEVVVLEAGRVVQ 1136
Cdd:PRK11607 152 GGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqleVVDILERV-GVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQ 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 1137 RG--------PYADLTAE--------EGPLrrmleRERETEGVAEEALGVR 1171
Cdd:PRK11607 231 IGepeeiyehPTTRYSAEfigsvnvfEGVL-----KERQEDGLVIDSPGLV 276
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
334-553 |
1.72e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 66.17 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 334 ELEGVTVRHEGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERIAWV 413
Cdd:PRK13632 9 KVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 414 PQRP-YLFAGT-----IA---ENVRLARPDADdgavaaalrdagayDFVAELPD--GAQTLLGEDGAGLSAGQRQRLALA 482
Cdd:PRK13632 89 FQNPdNQFIGAtveddIAfglENKKVPPKKMK--------------DIIDDLAKkvGMEDYLDKEPQNLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2351811981 483 RAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQGR--TVLLVVHRPALLPLADRVVRLEPGATLRPEKPE 553
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPK 227
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
355-552 |
1.79e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 67.36 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 355 LVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPErwrER-IAWVPQR----PYLfagTIAENVR 429
Cdd:PRK11000 24 LDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA---ERgVGMVFQSyalyPHL---SVAENMS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 430 LArpdaddgavaaaLRDAGA--------YDFVAELPDGAQtLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTASL 501
Cdd:PRK11000 98 FG------------LKLAGAkkeeinqrVNQVAEVLQLAH-LLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 502 DGETEAGIVEAVRRLAQ--GRTVLLVVH-RPALLPLADRVVRLEPGATLRPEKP 552
Cdd:PRK11000 165 DAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKP 218
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
349-544 |
1.88e-11 |
|
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: 68.27 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 349 SLDHASLVVD-----EGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGgvdlatlaperwrERIAWVPQrpYL---F 420
Cdd:COG1245 350 SYGGFSLEVEggeirEGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-------------LKISYKPQ--YIspdY 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 421 AGTIAENVRLARPDAddgavaaaLRDAGAYDFVAElPDGAQTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTAS 500
Cdd:COG1245 415 DGTVEEFLRSANTDD--------FGSSYYKTEIIK-PLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAH 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2351811981 501 LDGETEAGIVEAVRRLA--QGRTVLLVVHRPALLPL-ADR--VVRLEPG 544
Cdd:COG1245 486 LDVEQRLAVAKAIRRFAenRGKTAMVVDHDIYLIDYiSDRlmVFEGEPG 534
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
914-1143 |
2.17e-11 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 65.59 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 914 TPASPFPLEVRGLSARYAGAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLaqvlLR---FL-DAREGTYRIGGvDACVL 989
Cdd:COG4598 2 TDTAPPALEVRDLHKSFGDLE--VLKGVSLTARKGDVISIIGSSGSGKSTF----LRcinLLeTPDSGEIRVGG-EEIRL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 990 EGDTVRGFVG--------LCAQDAHIFDS-------SIREN--------LRLARTGATdEELRAALDRARLLDWAEALPA 1046
Cdd:COG4598 75 KPDRDGELVPadrrqlqrIRTRLGMVFQSfnlwshmTVLENvieapvhvLGRPKAEAI-ERAEALLAKVGLADKRDAYPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1047 gldtlvgehgaRLSGGQRQRLALARAILADFPVLVLDEPAEHLDlataDALTADLLA-----ATRGRTTVLITHRLQ-GL 1120
Cdd:COG4598 154 -----------HLSGGQQQRAAIARALAMEPEVMLFDEPTSALD----PELVGEVLKvmrdlAEEGRTMLVVTHEMGfAR 218
|
250 260
....*....|....*....|...
gi 2351811981 1121 EAVDEVVVLEAGRVVQRGPYADL 1143
Cdd:COG4598 219 DVSSHVVFLHQGRIEEQGPPAEV 241
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
357-542 |
2.62e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 64.48 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 357 VDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATlaPERWReRIAWVPQRPYLFAGTIA-ENVRLarpdA 435
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR--GDRSR-FMAYLGHLPGLKADLSTlENLHF----L 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 436 DDGAVAAALRDAGAYDFVAELPDGAQTLLGEdgagLSAGQRQRLALARAFLADRPLLLLDEPTASLDGEteaGIVEAVRR 515
Cdd:PRK13543 107 CGLHGRRAKQMPGSALAIVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE---GITLVNRM 179
|
170 180 190
....*....|....*....|....*....|..
gi 2351811981 516 LA-----QGRTVLLVVHRPALLPLADRVVRLE 542
Cdd:PRK13543 180 ISahlrgGGAALVTTHGAYAAPPVRTRMLTLE 211
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
921-1138 |
2.72e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 65.54 E-value: 2.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGT--YRIGGVDACVLEgdTVRGFV 998
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEifYNNQAITDDNFE--KLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 999 GLCAQDA-HIFDSSI--------RENlRLARTGATDEELRAALDRARLLDWAEALPAGLdtlvgehgarlSGGQRQRLAL 1069
Cdd:PRK13648 86 GIVFQNPdNQFVGSIvkydvafgLEN-HAVPYDEMHRRVSEALKQVDMLERADYEPNAL-----------SGGQKQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 1070 ArAILADFP-VLVLDEPAEHLDLATADALTaDL---LAATRGRTTVLITHRL-QGLEAvDEVVVLEAGRVVQRG 1138
Cdd:PRK13648 154 A-GVLALNPsVIILDEATSMLDPDARQNLL-DLvrkVKSEHNITIISITHDLsEAMEA-DHVIVMNKGTVYKEG 224
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
934-1133 |
3.08e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.60 E-value: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 934 ERDALDSVDLRLTAGRRIAVVGPSGSGKTTLaqvllrfLDAREGTYRIGGVDACVLEGD-----TVRGFVGLCAQDAHIF 1008
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTL-------LNALAGRIQGNNFTGTILANNrkptkQILKRTGFVTQDDILY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1009 DS-SIRENL------RLARTGATDEELRAALDRARLLdwaeALPAGLDTLVGEHGAR-LSGGQRQRLALARAILADFPVL 1080
Cdd:PLN03211 153 PHlTVRETLvfcsllRLPKSLTKQEKILVAESVISEL----GLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLL 228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2351811981 1081 VLDEPAEHLDLATADALTADLLA-ATRGRTTVLITHRLQG--LEAVDEVVVLEAGR 1133
Cdd:PLN03211 229 ILDEPTSGLDATAAYRLVLTLGSlAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGR 284
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
326-540 |
3.13e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.21 E-value: 3.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 326 DVPESLRLELEGVTVRHEGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLG--FTAPDEGRVRVGGVDLatlap 403
Cdd:COG2401 22 DLSERVAIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQF----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 404 erWRERiawvpqrpylfagTIAENVRLARPdadDGAVAAALRDAG---AYDFVAELPDgaqtllgedgagLSAGQRQRLA 480
Cdd:COG2401 97 --GREA-------------SLIDAIGRKGD---FKDAVELLNAVGlsdAVLWLRRFKE------------LSTGQKFRFR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2351811981 481 LARAfLADRP-LLLLDEPTASLDGETEAGIVEAVRRLAQ--GRTVLLVVHRP----ALLPlaDRVVR 540
Cdd:COG2401 147 LALL-LAERPkLLVIDEFCSHLDRQTAKRVARNLQKLARraGITLVVATHHYdvidDLQP--DLLIF 210
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
343-552 |
3.31e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 65.54 E-value: 3.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 343 EGRgepSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPER----WRERIAWVPQRP- 417
Cdd:PRK13649 19 EGR---ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikqIRKKVGLVFQFPe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 418 -YLFAGTIAENV---------------RLARPDADDGAVAAALRDAGAYDfvaelpdgaqtllgedgagLSAGQRQRLAL 481
Cdd:PRK13649 96 sQLFEETVLKDVafgpqnfgvsqeeaeALAREKLALVGISESLFEKNPFE-------------------LSGGQMRRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 482 ArAFLADRP-LLLLDEPTASLDGETEAGIVEAVRRLAQ-GRTVLLVVH-RPALLPLADRVVRLEPGATLRPEKP 552
Cdd:PRK13649 157 A-GILAMEPkILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHlMDDVANYADFVYVLEKGKLVLSGKP 229
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
903-1139 |
3.33e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.57 E-value: 3.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 903 PPVREPDSPAGTPASPFP-LEVRGLSARY---------AGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFL 972
Cdd:PRK10261 295 PAKQEPPIEQDTVVDGEPiLQVRNLVTRFplrsgllnrVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLV 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 973 DAREGTY-----RIGGVDACVLEgdTVRGFVGLCAQDA-------HIFDSSIRENLRLARTGATDEelrAALDRARLLDW 1040
Cdd:PRK10261 375 ESQGGEIifngqRIDTLSPGKLQ--ALRRDIQFIFQDPyasldprQTVGDSIMEPLRVHGLLPGKA---AAARVAWLLER 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1041 AEALPagldtlvgEHGAR----LSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTADLLAATR--GRTTVLIT 1114
Cdd:PRK10261 450 VGLLP--------EHAWRypheFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRdfGIAYLFIS 521
|
250 260
....*....|....*....|....*.
gi 2351811981 1115 HRLQGLEAVD-EVVVLEAGRVVQRGP 1139
Cdd:PRK10261 522 HDMAVVERIShRVAVMYLGQIVEIGP 547
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
17-311 |
3.47e-11 |
|
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: 65.49 E-value: 3.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 17 FFLAAVVALGVVGAALV---IAQaMLVADVVVGGFEDgltVSGLRTPLILLAAVALGRALVSWLTELAAYRASAAVKSEL 93
Cdd:cd18544 1 FILALLLLLLATALELLgplLIK-RAIDDYIVPGQGD---LQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 94 RGRLLDRAAELGPGLLSDRRTGSLVTLATRGVDALDDYFARYLPQLGLAVVVPVAVLARIVTEDWVSAAIIVVTLPlipl 173
Cdd:cd18544 77 RRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLP---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 174 FMILIGWATQSRMDRQWR----LLSRLSGHFLDVVAGLPTLKVFGRAKAQAESIRAITSQYRRATLRTLRIAFLSSFALE 249
Cdd:cd18544 153 LLLLATYLFRKKSRKAYRevreKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVE 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2351811981 250 LLATLSVALVAVTIGMRLVHGELDLytGLVVLILapeAYL-----PIRQVGAQYHAAAEGLSAAEEI 311
Cdd:cd18544 233 LLSSLALALVLWYGGGQVLSGAVTL--GVLYAFI---QYIqrffrPIRDLAEKFNILQSAMASAERI 294
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
19-311 |
3.55e-11 |
|
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: 65.53 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 19 LAAVVALGVVGAALVIAQAMLVADVVVGGFEDGLtvsgLRTPLILLAAVALGRALVSWLTELAAYRASAAVKSELRGRLL 98
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGGS----SGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 99 DRAAELGPGLLSDRRTGSLVTLATRGVDALDDYFARYLPQLGLAVVVPVAVLARIVTEDWVSAAIIVVTLPLIPLFMILI 178
Cdd:cd18551 77 RRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 179 GWATQSRMDRQWRLLSRLSGHFLDVVAGLPTLKVFGrakAQAESIRAITSQYRRATLRTLRIAFLSSF---ALELLATLS 255
Cdd:cd18551 157 GRRIRKASKRAQDALGELSAALERALSAIRTVKASN---AEERETKRGGEAAERLYRAGLKAAKIEALigpLMGLAVQLA 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 256 VALVAVTIGMRLVHGELDLYTgLVVLILapeaYL-----PIRQVGAQYHAAAEGLSAAEEI 311
Cdd:cd18551 234 LLVVLGVGGARVASGALTVGT-LVAFLL----YLfqlitPLSQLSSFFTQLQKALGALERI 289
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
926-1115 |
3.81e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 63.67 E-value: 3.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 926 LSARYAGAERDA---LDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGLCA 1002
Cdd:PRK13538 2 LEARNLACERDErilFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1003 QDAHIFDSSIRENLRLA---RTGATDEELRAALDRARLLDWaEALPAGldtlvgehgaRLSGGQRQRLALARAILADFPV 1079
Cdd:PRK13538 82 QPGIKTELTALENLRFYqrlHGPGDDEALWEALAQVGLAGF-EDVPVR----------QLSAGQQRRVALARLWLTRAPL 150
|
170 180 190
....*....|....*....|....*....|....*..
gi 2351811981 1080 LVLDEPAEHLDLATADALTADLLA-ATRGRTTVLITH 1115
Cdd:PRK13538 151 WILDEPFTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
904-1139 |
4.78e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 66.65 E-value: 4.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 904 PVREPDsPAGTPASPFpLEVRGLSARYAG---------AERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDA 974
Cdd:PRK15134 261 PSGDPV-PLPEPASPL-LDVEQLQVAFPIrkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 975 REGTYriggVDACVLEGDTVRGFVGLCAQDAHIF-DSSIRENLRLARTGATDEELR-------AALDRARLLDWAEALpa 1046
Cdd:PRK15134 339 QGEIW----FDGQPLHNLNRRQLLPVRHRIQVVFqDPNSSLNPRLNVLQIIEEGLRvhqptlsAAQREQQVIAVMEEV-- 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1047 GLD-TLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTADL--LAATRGRTTVLITHRLQGLEAV 1123
Cdd:PRK15134 413 GLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLksLQQKHQLAYLFISHDLHVVRAL 492
|
250
....*....|....*..
gi 2351811981 1124 -DEVVVLEAGRVVQRGP 1139
Cdd:PRK15134 493 cHQVIVLRQGEVVEQGD 509
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
350-553 |
4.79e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 64.85 E-value: 4.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 350 LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGvdlATLAPE-------RWRERIAWVPQRP--YLF 420
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAG---YHITPEtgnknlkKLRKKVSLVFQFPeaQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 421 AGTIAENVRLArPdaddgavaaalRDAGAYDFVAE---LPDGAQTLLGEDGAG-----LSAGQRQRLALArAFLADRP-L 491
Cdd:PRK13641 100 ENTVLKDVEFG-P-----------KNFGFSEDEAKekaLKWLKKVGLSEDLISkspfeLSGGQMRRVAIA-GVMAYEPeI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 492 LLLDEPTASLDGETEAGIVEA-VRRLAQGRTVLLVVHR-PALLPLADRVVRLEPGATLRPEKPE 553
Cdd:PRK13641 167 LCLDEPAAGLDPEGRKEMMQLfKDYQKAGHTVILVTHNmDDVAEYADDVLVLEHGKLIKHASPK 230
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
333-536 |
5.90e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 64.40 E-value: 5.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRhegRGE-PSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERW---RE 408
Cdd:PRK11831 8 VDMRGVSFT---RGNrCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 409 RIAWVPQRPYLFAG-TIAENVrlARPDAD-DGAVAAALRDAGAYDFVAELPDGAQTLLgedGAGLSAGQRQRLALARAFL 486
Cdd:PRK11831 85 RMSMLFQSGALFTDmNVFDNV--AYPLREhTQLPAPLLHSTVMMKLEAVGLRGAAKLM---PSELSGGMARRAALARAIA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2351811981 487 ADRPLLLLDEPTASLDGETEAGIVEAVRRL--AQGRTVLLVVHR-PALLPLAD 536
Cdd:PRK11831 160 LEPDLIMFDEPFVGQDPITMGVLVKLISELnsALGVTCVVVSHDvPEVLSIAD 212
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
346-528 |
6.45e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.18 E-value: 6.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 346 GEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRER-IAWVPQRPYLFAG-T 423
Cdd:PRK10762 16 GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgIGIIHQELNLIPQlT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 424 IAENVRLAR-PDADDGAVAAALRDAGAYDFVAEL--PDGAQTLLGEdgagLSAGQRQRLALARAFLADRPLLLLDEPTAS 500
Cdd:PRK10762 96 IAENIFLGReFVNRFGRIDWKKMYAEADKLLARLnlRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPTDA 171
|
170 180 190
....*....|....*....|....*....|
gi 2351811981 501 L-DGETEAgIVEAVRRL-AQGRTVLLVVHR 528
Cdd:PRK10762 172 LtDTETES-LFRVIRELkSQGRGIVYISHR 200
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
934-1143 |
6.51e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 64.80 E-value: 6.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 934 ERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGD----TVRGFVGLCAQ--DAHI 1007
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDkyirPVRKRIGMVFQfpESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1008 FDSSI-RENLRLARTGATDeeLRAALDRA-RLLdwaeaLPAGLDTLVGEHGA-RLSGGQRQRLALArAILADFP-VLVLD 1083
Cdd:PRK13646 99 FEDTVeREIIFGPKNFKMN--LDEVKNYAhRLL-----MDLGFSRDVMSQSPfQMSGGQMRKIAIV-SILAMNPdIIVLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2351811981 1084 EPAEHLDLATADALTADL--LAATRGRTTVLITHRLQGL-EAVDEVVVLEAGRVVQRGPYADL 1143
Cdd:PRK13646 171 EPTAGLDPQSKRQVMRLLksLQTDENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKEL 233
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
921-1147 |
7.50e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 64.87 E-value: 7.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARY---AGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGV---DACVLEGDT- 993
Cdd:PRK13631 22 LRVKNLYCVFdekQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIyigDKKNNHELIt 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 994 ------------VRGFVGLCAQ--DAHIFDSSIRENLRLARTGATDEELRAALDRARLLDwaealPAGLD-TLVGEHGAR 1058
Cdd:PRK13631 102 npyskkiknfkeLRRRVSMVFQfpEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLN-----KMGLDdSYLERSPFG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1059 LSGGQRQRLALArAILADFP-VLVLDEPAEHLDLATADALTADLL-AATRGRTTVLITHRL-QGLEAVDEVVVLEAGRVV 1135
Cdd:PRK13631 177 LSGGQKRRVAIA-GILAIQPeILIFDEPTAGLDPKGEHEMMQLILdAKANNKTVFVITHTMeHVLEVADEVIVMDKGKIL 255
|
250
....*....|...
gi 2351811981 1136 QRG-PYADLTAEE 1147
Cdd:PRK13631 256 KTGtPYEIFTDQH 268
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
333-553 |
7.54e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 63.86 E-value: 7.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPER-WRERIA 411
Cdd:PRK11300 6 LSVSGLMMRFGGL--LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiARMGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 412 WVPQRPYLFAG-TIAENVRLARPDADDGAVAAALRDAGAYDFV-AELPDGAQTLLGEDG--------AG-LSAGQRQRLA 480
Cdd:PRK11300 84 RTFQHVRLFREmTVIENLLVAQHQQLKTGLFSGLLKTPAFRRAeSEALDRAATWLERVGllehanrqAGnLAYGQQRRLE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2351811981 481 LARAFLADRPLLLLDEPTASLD-GETEA--GIVEAVRRlAQGRTVLLVVHRPAL-LPLADRVVRLEPGATLRPEKPE 553
Cdd:PRK11300 164 IARCMVTQPEILMLDEPAAGLNpKETKEldELIAELRN-EHNVTVLLIEHDMKLvMGISDRIYVVNQGTPLANGTPE 239
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
921-1138 |
7.61e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 63.79 E-value: 7.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGaeRDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGT--YRI-GGVDACVLE------- 990
Cdd:PRK11701 7 LSVRGLTKLYGP--RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEvhYRMrDGQLRDLYAlseaerr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 991 --GDTVRGFVglcAQDAhifdssiRENLRLART--GATDEELRAALD------RARLLDWAEALPAGLDTLvGEHGARLS 1060
Cdd:PRK11701 85 rlLRTEWGFV---HQHP-------RDGLRMQVSagGNIGERLMAVGArhygdiRATAGDWLERVEIDAARI-DDLPTTFS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1061 GGQRQRLALARAiLADFPVLVL-DEPAEHLDLatadALTADLLAATRGRTT------VLITHRLqgleAV-----DEVVV 1128
Cdd:PRK11701 154 GGMQQRLQIARN-LVTHPRLVFmDEPTGGLDV----SVQARLLDLLRGLVRelglavVIVTHDL----AVarllaHRLLV 224
|
250
....*....|
gi 2351811981 1129 LEAGRVVQRG 1138
Cdd:PRK11701 225 MKQGRVVESG 234
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
349-544 |
8.07e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 63.88 E-value: 8.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 349 SLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEgrvrvggvdlatlAPERWRERIAWVPQRpylfAGTIAENV 428
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDK-------------SAGSHIELLGRTVQR----EGRLARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 429 RLARPDADDGAVAAALRD---------AGAYD-----------FVAELPDGAQTLLGEDG---------AGLSAGQRQRL 479
Cdd:PRK09984 82 RKSRANTGYIFQQFNLVNrlsvlenvlIGALGstpfwrtcfswFTREQKQRALQALTRVGmvhfahqrvSTLSGGQQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2351811981 480 ALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQ--GRTVLLVVHR-PALLPLADRVVRLEPG 544
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQvDYALRYCERIVALRQG 229
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
937-1143 |
9.25e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 64.73 E-value: 9.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 937 ALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGD---TVRGFVGLCAQD--------- 1004
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDewrAVRSDIQMIFQDplaslnprm 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1005 --AHIfdssIRENLRLARTGATDEELRaalDRARlldwAEALPAGL-DTLVGEHGARLSGGQRQRLALARAILADFPVLV 1081
Cdd:PRK15079 116 tiGEI----IAEPLRTYHPKLSRQEVK---DRVK----AMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLII 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2351811981 1082 LDEPAEHLDLATaDALTADLLAATR---GRTTVLITHRLQGLEAV-DEVVVLEAGRVVQRGPYADL 1143
Cdd:PRK15079 185 CDEPVSALDVSI-QAQVVNLLQQLQremGLSLIFIAHDLAVVKHIsDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
350-536 |
9.43e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 63.90 E-value: 9.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 350 LDHASLVVDEGETVALVGPSGVGKSTLLDVvLGFTAPDEGRVRVGG-------------VDLatlapERWRERIAWVPQR 416
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGrveffnqniyerrVNL-----NRLRRQVSMVHPK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 417 PYLFAGTIAENVRLA------RPDADD-GAVAAALRDAgaydfvaELPDGAQTLLGEDGAGLSAGQRQRLALARAFLADR 489
Cdd:PRK14258 97 PNLFPMSVYDNVAYGvkivgwRPKLEIdDIVESALKDA-------DLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2351811981 490 PLLLLDEPTASLDGETEAGIVEAVR--RLAQGRTVLLVVHR-PALLPLAD 536
Cdd:PRK14258 170 KVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNlHQVSRLSD 219
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
880-1116 |
1.02e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.05 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 880 LAVQYRQRVKRSaERVYEVLDApppvrepdspagtpaspFPLEVRGLsaryagaERDALDSVDLRLTAGRRIAVVGPSGS 959
Cdd:COG2401 13 VTKVYSSVLDLS-ERVAIVLEA-----------------FGVELRVV-------ERYVLRDLNLEIEPGEIVLIVGASGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 960 GKTTLAQVLLRfldAREGTYRIGGVDACVLEgdtvrgfvglCAQDAHIFDSsirenlrLARTGATDEELRAaLDRARLLD 1039
Cdd:COG2401 68 GKSTLLRLLAG---ALKGTPVAGCVDVPDNQ----------FGREASLIDA-------IGRKGDFKDAVEL-LNAVGLSD 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 1040 waealPAGLDTLVGEhgarLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTADLLAATR--GRTTVLITHR 1116
Cdd:COG2401 127 -----AVLWLRRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARraGITLVVATHH 196
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
334-498 |
1.03e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 66.30 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 334 ELEGVTVRHegRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATlapERWRE----R 409
Cdd:NF033858 3 RLEGVSHRY--GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD---ARHRRavcpR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 410 IAWVPQ------RPYLfagTIAENV-------------RLARpdaddgaVAAALRDAGAYDFvAELPdgaqtllgedgAG 470
Cdd:NF033858 78 IAYMPQglgknlYPTL---SVFENLdffgrlfgqdaaeRRRR-------IDELLRATGLAPF-ADRP-----------AG 135
|
170 180
....*....|....*....|....*....
gi 2351811981 471 -LSAGQRQRLALARAFLADRPLLLLDEPT 498
Cdd:NF033858 136 kLSGGMKQKLGLCCALIHDPDLLILDEPT 164
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
350-552 |
1.40e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 64.10 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 350 LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVG--------GVDLATLAP--------ERWRERIAWV 413
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdkkNNHELITNPyskkiknfKELRRRVSMV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 414 PQRP--YLFAGTIAENVRLArPDADDGAVAAALRDAGAYDFVAELPDgaqTLLGEDGAGLSAGQRQRLALArAFLADRP- 490
Cdd:PRK13631 122 FQFPeyQLFKDTIEKDIMFG-PVALGVKKSEAKKLAKFYLNKMGLDD---SYLERSPFGLSGGQKRRVAIA-GILAIQPe 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 491 LLLLDEPTASLDGETEAGIVEAVRRL-AQGRTVLLVVHR-PALLPLADRVVRLEPGATLRPEKP 552
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLILDAkANNKTVFVITHTmEHVLEVADEVIVMDKGKILKTGTP 260
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
921-1118 |
1.61e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 62.53 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARY--AGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLlrfldaregtyriGGVDA-----CVLEGDT 993
Cdd:PRK11629 6 LQCDNLCKRYqeGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLL-------------GGLDTptsgdVIFNGQP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 994 VRGF------------VGLCAQDAHIF-DSSIREN--LRLARTGATDEElraALDRARlldwaEALPA-GLDTLVGEHGA 1057
Cdd:PRK11629 73 MSKLssaakaelrnqkLGFIYQFHHLLpDFTALENvaMPLLIGKKKPAE---INSRAL-----EMLAAvGLEHRANHRPS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 1058 RLSGGQRQRLALARAiLADFPVLVL-DEPAEHLDLATADALTADL--LAATRGRTTVLITHRLQ 1118
Cdd:PRK11629 145 ELSGGERQRVAIARA-LVNNPRLVLaDEPTGNLDARNADSIFQLLgeLNRLQGTAFLVVTHDLQ 207
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
921-1137 |
1.69e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.11 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSA--RYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGV---DACVLEGD--T 993
Cdd:PRK15134 6 LAIENLSVafRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIrfhGESLLHASeqT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 994 VRGFVGlcAQDAHIFDS---------SIRENL-------RLARTGATDEELRAALDRARLLDWAEALpagldtlvGEHGA 1057
Cdd:PRK15134 86 LRGVRG--NKIAMIFQEpmvslnplhTLEKQLyevlslhRGMRREAARGEILNCLDRVGIRQAAKRL--------TDYPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1058 RLSGGQRQRLALARAILADFPVLVLDEPAEHLDLaTADALTADLLAATR---GRTTVLITHRLQGLEAV-DEVVVLEAGR 1133
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDV-SVQAQILQLLRELQqelNMGLLFITHNLSIVRKLaDRVAVMQNGR 234
|
....
gi 2351811981 1134 VVQR 1137
Cdd:PRK15134 235 CVEQ 238
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
937-1138 |
1.75e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 63.57 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 937 ALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRI----------GGVDACVLEGDTV------------ 994
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkkTKEKEKVLEKLVIqktrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 995 --RGFVGLCAQDA--HIFDSSIRENLRLA--RTGATDEElraALDRARllDWAEALpaGLDTlvgEHGAR----LSGGQR 1064
Cdd:PRK13651 102 eiRRRVGVVFQFAeyQLFEQTIEKDIIFGpvSMGVSKEE---AKKRAA--KYIELV--GLDE---SYLQRspfeLSGGQK 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 1065 QRLALArAILADFP-VLVLDEPAEHLD-LATADALtaDLLAA--TRGRTTVLITHRLQG-LEAVDEVVVLEAGRVVQRG 1138
Cdd:PRK13651 172 RRVALA-GILAMEPdFLVFDEPTAGLDpQGVKEIL--EIFDNlnKQGKTIILVTHDLDNvLEWTKRTIFFKDGKIIKDG 247
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
937-1157 |
2.26e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.42 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 937 ALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLE-GDTVRGFVGLCAQDAHIFDS-SIRE 1014
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhKLAAQLGIGIIYQELSVIDElTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1015 NLRLAR------TGATDEELRAALDRARLLDWAEALPAGLDTLVGEhgarLSGGQRQRLALARAILADFPVLVLDEPAEH 1088
Cdd:PRK09700 100 NLYIGRhltkkvCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2351811981 1089 LDLATADALTAdLLAATR--GRTTVLITHRLQGLEAV-DEVVVLEAGRVVQRGPYADLTAEEgPLRRMLERE 1157
Cdd:PRK09700 176 LTNKEVDYLFL-IMNQLRkeGTAIVYISHKLAEIRRIcDRYTVMKDGSSVCSGMVSDVSNDD-IVRLMVGRE 245
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
921-1139 |
2.81e-10 |
|
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: 61.00 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDaregtYRIggvdacvlegdtVRGFVGL 1000
Cdd:cd03217 1 LEIKDLHVSVGGKE--ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPK-----YEV------------TEGEILF 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDahIFDSSIREnlrlartgatdeelraaldRARL---LDWAEalPA-----GLDTLVGEHGARLSGGQRQRLALARA 1072
Cdd:cd03217 62 KGED--ITDLPPEE-------------------RARLgifLAFQY--PPeipgvKNADFLRYVNEGFSGGEKKRNEILQL 118
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2351811981 1073 ILADFPVLVLDEPAEHLDLataDAL--TADLLA--ATRGRTTVLITHRLQGLEAV--DEVVVLEAGRVVQRGP 1139
Cdd:cd03217 119 LLLEPDLAILDEPDSGLDI---DALrlVAEVINklREEGKSVLIITHYQRLLDYIkpDRVHVLYDGRIVKSGD 188
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
921-1138 |
2.99e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 62.40 E-value: 2.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYA-GAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLaqvLLRF---LDAREGTYRIGGV-----DACVLEg 991
Cdd:PRK13639 2 LETRDLKYSYPdGTE--ALKGINFKAEKGEMVALLGPNGAGKSTL---FLHFngiLKPTSGEVLIKGEpikydKKSLLE- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 992 dtVRGFVGLCAQ--DAHIFDSSIRE-------NLRLARTgATDEELRAALDRARLLDWAEALPagldtlvgEHgarLSGG 1062
Cdd:PRK13639 76 --VRKTVGIVFQnpDDQLFAPTVEEdvafgplNLGLSKE-EVEKRVKEALKAVGMEGFENKPP--------HH---LSGG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 1063 QRQRLALArAILADFP-VLVLDEPAEHLDLATADALTADLLAATR-GRTTVLITHRLQGLEA-VDEVVVLEAGRVVQRG 1138
Cdd:PRK13639 142 QKKRVAIA-GILAMKPeIIVLDEPTSGLDPMGASQIMKLLYDLNKeGITIIISTHDVDLVPVyADKVYVMSDGKIIKEG 219
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
921-1156 |
3.39e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.11 E-value: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSA--RY-AGAER----DALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDT 993
Cdd:PRK15112 5 LEVRNLSKtfRYrTGWFRrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 994 VRGFVGLCAQDA-----------HIFDSSIRENLRLArTGATDEELRAALDRARLL-DWAEALPagldtlvgeHgaRLSG 1061
Cdd:PRK15112 85 RSQRIRMIFQDPstslnprqrisQILDFPLRLNTDLE-PEQREKQIIETLRQVGLLpDHASYYP---------H--MLAP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1062 GQRQRLALARAILADFPVLVLDEPAEHLDLATADALTADL--LAATRGRTTVLITHRLQGLEAV-DEVVVLEAGRVVQRG 1138
Cdd:PRK15112 153 GQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMleLQEKQGISYIYVTQHLGMMKHIsDQVLVMHQGEVVERG 232
|
250
....*....|....*...
gi 2351811981 1139 PYADLTAeeGPLRRMLER 1156
Cdd:PRK15112 233 STADVLA--SPLHELTKR 248
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
353-553 |
4.46e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 63.13 E-value: 4.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 353 ASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRE----RIAWVPQRPYLFAG-TIAEN 427
Cdd:PRK10070 47 ASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPHmTVLDN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 428 VRLARPDADDGAVAA------ALRDAGAYDFVAELPDgaqtllgedgaGLSAGQRQRLALARAFLADRPLLLLDEPTASL 501
Cdd:PRK10070 127 TAFGMELAGINAEERrekaldALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2351811981 502 DGETEAGIVEAVRRL--AQGRTVLLVVHR-PALLPLADRVVRLEPGATLRPEKPE 553
Cdd:PRK10070 196 DPLIRTEMQDELVKLqaKHQRTIVFISHDlDEAMRIGDRIAIMQNGEVVQVGTPD 250
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
906-1147 |
4.63e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 63.50 E-value: 4.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 906 REPDSPAGTPAspfpLEVRGLSARyagaerDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVD 985
Cdd:COG1129 246 PKRAAAPGEVV----LEVEGLSVG------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKP 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 986 acvLEGDTVR-----GfVGLCAQDAH----IFDSSIRENL------RLARTGAtdeeLRAALDRARLLDWAEAL---PAG 1047
Cdd:COG1129 316 ---VRIRSPRdairaG-IAYVPEDRKgeglVLDLSIRENItlasldRLSRGGL----LDRRRERALAEEYIKRLrikTPS 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1048 LDTLVGEhgarLSGGQRQRLALARAILADFPVLVLDEPAEHLDL-ATAD--ALTADLlaATRGRTTVLITHRLQGLEAV- 1123
Cdd:COG1129 388 PEQPVGN----LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVgAKAEiyRLIREL--AAEGKAVIVISSELPELLGLs 461
|
250 260
....*....|....*....|....
gi 2351811981 1124 DEVVVLEAGRVVQRGPYADLTAEE 1147
Cdd:COG1129 462 DRILVMREGRIVGELDREEATEEA 485
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
943-1138 |
4.96e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 63.13 E-value: 4.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 943 LRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGlcAQDAHIFDS-SIRENLRLART 1021
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRR--KKIAMVFQSfALMPHMTVLDN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1022 GATDEELRAALDRARLLDWAEAL-PAGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTAD 1100
Cdd:PRK10070 127 TAFGMELAGINAEERREKALDALrQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDE 206
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2351811981 1101 L--LAATRGRTTVLITHRL-QGLEAVDEVVVLEAGRVVQRG 1138
Cdd:PRK10070 207 LvkLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVG 247
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
335-527 |
5.21e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 61.73 E-value: 5.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 335 LEGVTVRHEGRgepSLDHA-SLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERIAWV 413
Cdd:PRK10575 14 LRNVSFRVPGR---TLLHPlSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 414 PQR-PYLFAGTIAENVRLARpdaddGAVAAALRDAGAYDfvAELPDGAQTLLGEDGAG------LSAGQRQRLALARAFL 486
Cdd:PRK10575 91 PQQlPAAEGMTVRELVAIGR-----YPWHGALGRFGAAD--REKVEEAISLVGLKPLAhrlvdsLSGGERQRAWIAMLVA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2351811981 487 ADRPLLLLDEPTASLDGETEAGIVEAVRRLAQGR--TVLLVVH 527
Cdd:PRK10575 164 QDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLH 206
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
350-502 |
6.25e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 62.29 E-value: 6.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 350 LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERW---RERIAWVPQRPYlfaGTIae 426
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQkllRQKIQIVFQNPY---GSL-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 427 NVR------LARPDADDGAVAAALRDAGAYDFVAELpdgaqtllgedgaGL------------SAGQRQRLALARAFLAD 488
Cdd:PRK11308 106 NPRkkvgqiLEEPLLINTSLSAAERREKALAMMAKV-------------GLrpehydryphmfSGGQRQRIAIARALMLD 172
|
170
....*....|....
gi 2351811981 489 RPLLLLDEPTASLD 502
Cdd:PRK11308 173 PDVVVADEPVSALD 186
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
921-1118 |
7.11e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 60.56 E-value: 7.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAERD--ALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDtvrGFV 998
Cdd:PRK10584 7 VEVHHLKKSVGQGEHElsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEE---ARA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 999 GLCAQD-AHIFDS-------SIRENLRLAR--TGATDEELRaalDRARLLDWAEALPAGLDTLvgehGARLSGGQRQRLA 1068
Cdd:PRK10584 84 KLRAKHvGFVFQSfmliptlNALENVELPAllRGESSRQSR---NGAKALLEQLGLGKRLDHL----PAQLSGGEQQRVA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2351811981 1069 LARAILADFPVLVLDEPAEHLDLATADALtADLLAATR---GRTTVLITHRLQ 1118
Cdd:PRK10584 157 LARAFNGRPDVLFADEPTGNLDRQTGDKI-ADLLFSLNrehGTTLILVTHDLQ 208
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
938-1161 |
7.99e-10 |
|
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: 60.56 E-value: 7.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 938 LDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFvglcaQDAHIFD-SSIRENL 1016
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVF-----QNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1017 RLA----RTGATDEELRAALDRARLLdwaealpAGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLA 1092
Cdd:TIGR01184 76 ALAvdrvLPDLSKSERRAIVEEHIAL-------VGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 1093 TADALTADLL--AATRGRTTVLITHRlqgleaVDEVVVLeAGRVVQ--RGPYADL-TAEEGPLRRMLERERETE 1161
Cdd:TIGR01184 149 TRGNLQEELMqiWEEHRVTVLMVTHD------VDEALLL-SDRVVMltNGPAANIgQILEVPFPRPRDRLEVVE 215
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
343-527 |
8.31e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 61.19 E-value: 8.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 343 EGRGepsLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVG------GVDLATLAPerWRERIAWVPQR 416
Cdd:PRK13634 19 ERRA---LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGervitaGKKNKKLKP--LRKKVGIVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 417 P--YLFAGTIAENVRLArPDADDGAVAAALRDAGAYDFVAELPdgaQTLLGEDGAGLSAGQRQRLALArAFLADRP-LLL 493
Cdd:PRK13634 94 PehQLFEETVEKDICFG-PMNFGVSEEDAKQKAREMIELVGLP---EELLARSPFELSGGQMRRVAIA-GVLAMEPeVLV 168
|
170 180 190
....*....|....*....|....*....|....*.
gi 2351811981 494 LDEPTASLDGETEAGIVEAVRRLAQ--GRTVLLVVH 527
Cdd:PRK13634 169 LDEPTAGLDPKGRKEMMEMFYKLHKekGLTTVLVTH 204
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
914-1147 |
8.61e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 62.76 E-value: 8.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 914 TPASPFPL-EVRGLSARYAGAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGD 992
Cdd:PRK15439 4 SDTTAPPLlCARSISKQYSGVE--VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 993 TVRGF-VGLCAQDAHIFDS-SIREN--LRLARTGATDEELRAALdrarlldwaEALPAGLDTLVgeHGARLSGGQRQRLA 1068
Cdd:PRK15439 82 KAHQLgIYLVPQEPLLFPNlSVKENilFGLPKRQASMQKMKQLL---------AALGCQLDLDS--SAGSLEVADRQIVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1069 LARAILADFPVLVLDEPAEHLDLATADALTADLLA-ATRGRTTVLITHRLQGLEAV-DEVVVLEAGRVVQRGPYADLTAE 1146
Cdd:PRK15439 151 ILRGLMRDSRILILDEPTASLTPAETERLFSRIRElLAQGVGIVFISHKLPEIRQLaDRISVMRDGTIALSGKTADLSTD 230
|
.
gi 2351811981 1147 E 1147
Cdd:PRK15439 231 D 231
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
305-505 |
8.99e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 62.65 E-value: 8.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 305 LSAAEEIFSvlETEPRRGGTAD--VPESLRL-----ELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLL 377
Cdd:TIGR03719 290 LARYEELLS--QEFQKRNETAEiyIPPGPRLgdkviEAENLTKAFGDK--LLIDDLSFKLPPGGIVGVIGPNGAGKSTLF 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 378 DVVLGFTAPDEGRVRVG-GVDLA-------TLAPER--WRErIA-----------WVPQRPYLfagtiaenvrlarpdad 436
Cdd:TIGR03719 366 RMITGQEQPDSGTIEIGeTVKLAyvdqsrdALDPNKtvWEE-ISggldiiklgkrEIPSRAYV----------------- 427
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 437 dgavaaalrdaGAYDFvaelpDGA--QTLLGEdgagLSAGQRQRLALARAFLADRPLLLLDEPTASLDGET 505
Cdd:TIGR03719 428 -----------GRFNF-----KGSdqQKKVGQ----LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVET 478
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
331-543 |
9.13e-10 |
|
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: 59.54 E-value: 9.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 331 LRLELEGVTVRHegrgepslDHASLVVDEGETVaLVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERwrERI 410
Cdd:cd03240 2 DKLSIRNIRSFH--------ERSEIEFFSPLTL-IVGQNGAGKTTIIEALKYALTGELPPNSKGGAHDPKLIREG--EVR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 411 AWVpqrpYL-FAGTIAENVRLarpdaddgavaaaLRDAGAYDFVAELPDGAQTLLGEDGAG-LSAGQRQ------RLALA 482
Cdd:cd03240 71 AQV----KLaFENANGKKYTI-------------TRSLAILENVIFCHQGESNWPLLDMRGrCSGGEKVlasliiRLALA 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 483 RAFLADRPLLLLDEPTASLDGET-EAGIVEAVRRLAQGRTVLLVV--HRPALLPLADRVVRLEP 543
Cdd:cd03240 134 ETFGSNCGILALDEPTTNLDEENiEESLAEIIEERKSQKNFQLIVitHDEELVDAADHIYRVEK 197
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
470-543 |
1.00e-09 |
|
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: 58.53 E-value: 1.00e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 470 GLSAGQRQRLALARAF----LADRPLLLLDEPTASLDGETEAGIVEAVRRLAQ-GRTVLLVVHRPALLPLADRVVRLEP 543
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVkGAQVIVITHLPELAELADKLIHIKK 155
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
921-1171 |
1.08e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 62.53 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLlrfldarEGTYRIGGVDACVL-EG-------- 991
Cdd:TIGR02633 2 LEMKGIVKTFGGVK--ALDGIDLEVRPGECVGLCGENGAGKSTLMKIL-------SGVYPHGTWDGEIYwSGsplkasni 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 992 -DTVRGFVGLCAQD-AHIFDSSIRENLRLART-----GATDEElrAALDRARLLDWAEALPAGLDTL-VGEHGarlsGGQ 1063
Cdd:TIGR02633 73 rDTERAGIVIIHQElTLVPELSVAENIFLGNEitlpgGRMAYN--AMYLRAKNLLRELQLDADNVTRpVGDYG----GGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1064 RQRLALARAILADFPVLVLDEPAEHLDLATADAL---TADLLAatRGRTTVLITHRLQGLEAV-DEVVVLEAGRVVQRGP 1139
Cdd:TIGR02633 147 QQLVEIAKALNKQARLLILDEPSSSLTEKETEILldiIRDLKA--HGVACVYISHKLNEVKAVcDTICVIRDGQHVATKD 224
|
250 260 270
....*....|....*....|....*....|....*...
gi 2351811981 1140 YADLTaEEGPLRRMLERE------RETEGVAEEALGVR 1171
Cdd:TIGR02633 225 MSTMS-EDDIITMMVGREitslypHEPHEIGDVILEAR 261
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
356-554 |
1.28e-09 |
|
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: 58.74 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 356 VVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVdlatlaperwreRIAWVPQRpylfagtiaenvrlarpda 435
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGI------------TPVYKPQY------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 436 ddgavaaalrdagaydfvaelpdgaqtllgedgAGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRR 515
Cdd:cd03222 70 ---------------------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2351811981 516 LAQ--GRTVLLVVHRPALLP-LADR--VVRLEPGATLRPEKPEG 554
Cdd:cd03222 117 LSEegKKTALVVEHDLAVLDyLSDRihVFEGEPGVYGIASQPKG 160
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
921-1151 |
1.36e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 60.63 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAErDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGG--VDACVLEGDTVRGFV 998
Cdd:PRK13636 6 LKVEELNYNYSDGT-HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 999 GLCAQ--DAHIFDSSIRENLRLA--RTGATDEELRAALDRArlldwaeALPAGLDTLVGEHGARLSGGQRQRLALARAIL 1074
Cdd:PRK13636 85 GMVFQdpDNQLFSASVYQDVSFGavNLKLPEDEVRKRVDNA-------LKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1075 ADFPVLVLDEPAEHLDLATADALTADLLAATR--GRTTVLITHRLQGLEA-VDEVVVLEAGRVVQRGPYADLTAEEGPLR 1151
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLyCDNVFVMKEGRVILQGNPKEVFAEKEMLR 237
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
622-810 |
1.39e-09 |
|
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: 60.50 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 622 AVSGWLISRASEQPPVLYLMVAVtatrAFGLGRAVFRYAERLVSHDAVLKMLAELRVAVYRGLERIAPAGLRRSRRGDLL 701
Cdd:cd18584 22 IIAGVFLEGAGLAALLPLLLLLL----AALLLRALLAWAQERLAARAAARVKAELRRRLLARLLALGPALLRRQSSGELA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 702 SRLVADVDALQDYWLRWLLPAGTAVVVGAATAGFIGWL-LPAAGIVLATGLLlagagVP----LVSGACSRHAERQLApA 776
Cdd:cd18584 98 TLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLdWVSALILLVTAPL-----IPlfmiLIGKAAQAASRRQWA-A 171
|
170 180 190
....*....|....*....|....*....|....
gi 2351811981 777 RADLATRITDLLGGTAELTVAGALPARKARTREA 810
Cdd:cd18584 172 LSRLSGHFLDRLRGLPTLKLFGRARAQAARIARA 205
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
360-518 |
1.44e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.03 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 360 GETVALVGPSGVGKST----LLDVVlgftaPDEGRVRVGGVDLATLAPER---WRERIAWVPQRPYL-------FAGTIA 425
Cdd:PRK15134 312 GETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQllpVRHRIQVVFQDPNSslnprlnVLQIIE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 426 ENVRLARPDADDGAvaaalRDAGAYDFVAEL---PDGAQTLLGEdgagLSAGQRQRLALARAFLADRPLLLLDEPTASLD 502
Cdd:PRK15134 387 EGLRVHQPTLSAAQ-----REQQVIAVMEEVgldPETRHRYPAE----FSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
170
....*....|....*.
gi 2351811981 503 GETEAGIVEAVRRLAQ 518
Cdd:PRK15134 458 KTVQAQILALLKSLQQ 473
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
364-544 |
1.59e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 60.06 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 364 ALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGV------DLATLAPERWRERIAWVPQRPYLFAG-TIAENVR------- 429
Cdd:PRK14246 40 GIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPHlSIYDNIAyplkshg 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 430 LARPDADDGAVAAALRDAGAYDFVAELpdgaqtlLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEAGI 509
Cdd:PRK14246 120 IKEKREIKKIVEECLRKVGLWKEVYDR-------LNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAI 192
|
170 180 190
....*....|....*....|....*....|....*.
gi 2351811981 510 VEAVRRLAQGRTVLLVVHRPALLP-LADRVVRLEPG 544
Cdd:PRK14246 193 EKLITELKNEIAIVIVSHNPQQVArVADYVAFLYNG 228
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
349-527 |
1.60e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 60.56 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 349 SLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERW----RERIAWVPQRP--YLFAG 422
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYirpvRKRIGMVFQFPesQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 423 TIAENVRLarpdaddgavaaalrdaGAYDF---VAELPDGAQTLLGEDGAG----------LSAGQRQRLALARAFLADR 489
Cdd:PRK13646 102 TVEREIIF-----------------GPKNFkmnLDEVKNYAHRLLMDLGFSrdvmsqspfqMSGGQMRKIAIVSILAMNP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2351811981 490 PLLLLDEPTASLDGETEAGIVEAVRRLA--QGRTVLLVVH 527
Cdd:PRK13646 165 DIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSH 204
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
360-547 |
1.63e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 62.20 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 360 GETVALVGPSGVGKSTLLDVVlgftapdEGRVRVGGVDLATLAPER-----WRERIAWVPQRPYLFAG-TIAENVRLARP 433
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNAL-------AGRIQGNNFTGTILANNRkptkqILKRTGFVTQDDILYPHlTVRETLVFCSL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 434 DADDGAVAAALRDAGAYDFVAEL--PDGAQTLLGEDGA-GLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEAGIV 510
Cdd:PLN03211 167 LRLPKSLTKQEKILVAESVISELglTKCENTIIGNSFIrGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLV 246
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2351811981 511 EAVRRLAQ-GRTVLLVVHRPA--LLPLADRVVRLEPGATL 547
Cdd:PLN03211 247 LTLGSLAQkGKTIVTSMHQPSsrVYQMFDSVLVLSEGRCL 286
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
332-544 |
1.80e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 59.71 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 332 RLELEGVTVRHEGrgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPD----EGRVRVGGVdlaTLAPERWR 407
Cdd:PRK10418 4 QIELRNIALQAAQ---PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGK---PVAPCALR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 408 ER-IAWVPQRP-------YLFAGTIAENVRLARPDADDGAVAAALRDAGaydfvaeLPDgAQTLLGEDGAGLSAGQRQRL 479
Cdd:PRK10418 78 GRkIATIMQNPrsafnplHTMHTHARETCLALGKPADDATLTAALEAVG-------LEN-AARVLKLYPFEMSGGMLQRM 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2351811981 480 ALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQGRT--VLLVVHRPALLP-LADRVVRLEPG 544
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVArLADDVAVMSHG 217
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
350-527 |
1.86e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 60.49 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 350 LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEG----------------RVRVGGVDLATLAPER-------- 405
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtiewifkdeknkkktkEKEKVLEKLVIQKTRFkkikkike 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 406 WRERIAWVPQ-RPY-LFAGTIAENVRLArPDADDGAVAAALRDAGAYDFVAELPdgaQTLLGEDGAGLSAGQRQRLALAr 483
Cdd:PRK13651 103 IRRRVGVVFQfAEYqLFEQTIEKDIIFG-PVSMGVSKEEAKKRAAKYIELVGLD---ESYLQRSPFELSGGQKRRVALA- 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2351811981 484 AFLADRP-LLLLDEPTASLDGETEAGIVEAVRRL-AQGRTVLLVVH 527
Cdd:PRK13651 178 GILAMEPdFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTH 223
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
920-1146 |
2.05e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 59.61 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 920 PLEVRGLSARYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVG 999
Cdd:PRK10253 5 VARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1000 LCAQDAHI-FDSSIRENLR---------LARTGATDEELRAALDRArlldwaealpAGLDTLVGEHGARLSGGQRQRLAL 1069
Cdd:PRK10253 85 LLAQNATTpGDITVQELVArgryphqplFTRWRKEDEEAVTKAMQA----------TGITHLADQSVDTLSGGQRQRAWI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1070 ARAILADFPVLVLDEPAEHLDLATADALTADL--LAATRGRTTVLITHRL-QGLEAVDEVVVLEAGRVVQRG-PYADLTA 1145
Cdd:PRK10253 155 AMVLAQETAIMLLDEPTTWLDISHQIDLLELLseLNREKGYTLAAVLHDLnQACRYASHLIALREGKIVAQGaPKEIVTA 234
|
.
gi 2351811981 1146 E 1146
Cdd:PRK10253 235 E 235
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
356-545 |
2.44e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.36 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 356 VVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRV-----------RVGGVDLATLApERWRE---RIAWVPQR----P 417
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYeeepswdevlkRFRGTELQNYF-KKLYNgeiKVVHKPQYvdliP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 418 YLFAGTIAENVRLARpdaddgavaaalrDAGAYDFVAELPdGAQTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEP 497
Cdd:PRK13409 174 KVFKGKVRELLKKVD-------------ERGKLDEVVERL-GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 498 TASLDGETEAGIVEAVRRLAQGRTVLLVVHRPALLP-LADRVVRL--EPGA 545
Cdd:PRK13409 240 TSYLDIRQRLNVARLIRELAEGKYVLVVEHDLAVLDyLADNVHIAygEPGA 290
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
333-552 |
3.30e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 59.34 E-value: 3.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRGEPS-LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERIA 411
Cdd:PRK13642 5 LEVENLVFKYEKESDVNqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 412 WVPQRP--YLFAGTIAENVRLARPDADDGAVAAALRDAGAYDFVAELpdgaqTLLGEDGAGLSAGQRQRLALArAFLADR 489
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNML-----DFKTREPARLSGGQKQRVAVA-GIIALR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2351811981 490 P-LLLLDEPTASLDGETEAGIVEAVRRLAQGR--TVLLVVHRPALLPLADRVVRLEPGATLRPEKP 552
Cdd:PRK13642 159 PeIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAP 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
921-1134 |
4.44e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 58.97 E-value: 4.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARY-AGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIggvDACVLEGDTV---RG 996
Cdd:PRK13650 5 IEVKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIII---DGDLLTEENVwdiRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 997 FVGLCAQ--DAHIFDSSIRENLR--LARTGATDEELRA----ALDRARLLDWAEALPagldtlvgehgARLSGGQRQRLA 1068
Cdd:PRK13650 82 KIGMVFQnpDNQFVGATVEDDVAfgLENKGIPHEEMKErvneALELVGMQDFKEREP-----------ARLSGGQKQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2351811981 1069 LARAILADFPVLVLDEPAEHLDLATADAL--TADLLAATRGRTTVLITHRLQGLEAVDEVVVLEAGRV 1134
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDPEGRLELikTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
952-1139 |
4.57e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 61.02 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 952 AVVGPSGSGKTTLAQVLLrfldAR------EGTYRIGGVDAcvlEGDTVRGFVGLCAQ-DAHIFDSSIRENL------RL 1018
Cdd:PLN03140 910 ALMGVSGAGKTTLMDVLA----GRktggyiEGDIRISGFPK---KQETFARISGYCEQnDIHSPQVTVRESLiysaflRL 982
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1019 ARTGATDEELRAALDRARLLDwaeaLPAGLDTLVGEHGAR-LSGGQRQRLALARAILADFPVLVLDEPAEHLDlATADAL 1097
Cdd:PLN03140 983 PKEVSKEEKMMFVDEVMELVE----LDNLKDAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD-ARAAAI 1057
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2351811981 1098 TADLLAAT--RGRTTVLITHR--LQGLEAVDEVVVLE-AGRVVQRGP 1139
Cdd:PLN03140 1058 VMRTVRNTvdTGRTVVCTIHQpsIDIFEAFDELLLMKrGGQVIYSGP 1104
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
347-536 |
5.03e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 57.65 E-value: 5.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 347 EPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGV----DLATlaperWRERIAWVPQR----PY 418
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsikkDLCT-----YQKQLCFVGHRsginPY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 419 LfagTIAENVRLARPDADDGAVAAALRDAGAYDFVAELPDGAqtllgedgagLSAGQRQRLALARAFLADRPLLLLDEPT 498
Cdd:PRK13540 89 L---TLRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGL----------LSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 2351811981 499 ASLDGETEAGIVEAVR-RLAQGRTVLLVVHRPALLPLAD 536
Cdd:PRK13540 156 VALDELSLLTIITKIQeHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
934-1129 |
6.18e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.20 E-value: 6.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 934 ERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTyriggvdacVLEGDTVRgfVGLCAQDAHIFDS--- 1010
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGV---------IKRNGKLR--IGYVPQKLYLDTTlpl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1011 SIRENLRLaRTGATDEELRAALDR---ARLLDWAEAlpagldtlvgehgaRLSGGQRQRLALARAILADFPVLVLDEPAE 1087
Cdd:PRK09544 85 TVNRFLRL-RPGTKKEDILPALKRvqaGHLIDAPMQ--------------KLSGGETQRVLLARALLNRPQLLVLDEPTQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2351811981 1088 HLDLATADALTaDLLAATR---GRTTVLITHRLQGLEA-VDEVVVL 1129
Cdd:PRK09544 150 GVDVNGQVALY-DLIDQLRrelDCAVLMVSHDLHLVMAkTDEVLCL 194
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
354-531 |
6.34e-09 |
|
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: 60.15 E-value: 6.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 354 SLVVDEGETVALVGPSGVGKSTLLDVvLGFTAPDEGRVRVggvdlatlAPERwrERIAWVPQRPYLFAGTIAENVrlARP 433
Cdd:TIGR00954 472 SFEVPSGNNLLICGPNGCGKSSLFRI-LGELWPVYGGRLT--------KPAK--GKLFYVPQRPYMTLGTLRDQI--IYP 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 434 DADDGAVAAALRDAgayDFVAELPDGAQTLLGEDGAGLSA----------GQRQRLALARAFLADRPLLLLDEPTASLDG 503
Cdd:TIGR00954 539 DSSEDMKRRGLSDK---DLEQILDNVQLTHILEREGGWSAvqdwmdvlsgGEKQRIAMARLFYHKPQFAILDECTSAVSV 615
|
170 180
....*....|....*....|....*...
gi 2351811981 504 ETEAGIVEAVRRLaqGRTVLLVVHRPAL 531
Cdd:TIGR00954 616 DVEGYMYRLCREF--GITLFSVSHRKSL 641
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
349-544 |
6.78e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 58.28 E-value: 6.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 349 SLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERIAWVPQRP--YLFAGTIAE 426
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 427 NVRLARPDADDGAVAAALRDAGAYDFVaelpdGAQTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETE 506
Cdd:PRK13652 99 DIAFGPINLGLDEETVAHRVSSALHML-----GLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2351811981 507 AGIVEAVRRLAQ--GRTVLLVVHRPALLP-LADRVVRLEPG 544
Cdd:PRK13652 174 KELIDFLNDLPEtyGMTVIFSTHQLDLVPeMADYIYVMDKG 214
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
464-545 |
8.68e-09 |
|
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: 56.18 E-value: 8.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 464 LGEDGAGLSAGQRQRLALARaFLADRP---LLLLDEPTASLDGETEAGIVEAVRRL-AQGRTVLLVVHRPALLPLADRVV 539
Cdd:cd03238 81 LGQKLSTLSGGELQRVKLAS-ELFSEPpgtLFILDEPSTGLHQQDINQLLEVIKGLiDLGNTVILIEHNLDVLSSADWII 159
|
....*.
gi 2351811981 540 RLEPGA 545
Cdd:cd03238 160 DFGPGS 165
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
941-1139 |
8.95e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 58.73 E-value: 8.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 941 VDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVdacVLEgDTVRGF--------VGLCAQDAHIFDS-S 1011
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGR---VLF-DAEKGIclppekrrIGYVFQDARLFPHyK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1012 IRENLRLARTGATDEELraaLDRARLLdwaealpaGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDL 1091
Cdd:PRK11144 93 VRGNLRYGMAKSMVAQF---DKIVALL--------GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 1092 ATADALTADL--LAATRGRTTVLITHRLQG-LEAVDEVVVLEAGRVVQRGP 1139
Cdd:PRK11144 162 PRKRELLPYLerLAREINIPILYVSHSLDEiLRLADRVVVLEQGKVKAFGP 212
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
333-539 |
1.07e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 57.63 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGG-----VDLATL--APER 405
Cdd:PRK11701 7 LSVRGLTKLYGPR--KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALseAERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 406 WRERIAW--VPQ------RPYLFAG-TIAEnvrlaRPDADDGAVAAALRDAgAYDFVAELpDGAQTLLGEDGAGLSAGQR 476
Cdd:PRK11701 85 RLLRTEWgfVHQhprdglRMQVSAGgNIGE-----RLMAVGARHYGDIRAT-AGDWLERV-EIDAARIDDLPTTFSGGMQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2351811981 477 QRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLA--QGRTVLLVVHRPALLP-LADRVV 539
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVreLGLAVVIVTHDLAVARlLAHRLL 223
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
350-527 |
1.08e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 58.17 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 350 LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDlatlaPerWRERIAwvpqrpylFAGTIA---- 425
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV-----P--FKRRKE--------FARRIGvvfg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 426 ------------ENVRLarpdaddgavaaaLR-----DAGAYD-FVAELPDgaqtLLGEDG------AGLSAGQRQRLAL 481
Cdd:COG4586 103 qrsqlwwdlpaiDSFRL-------------LKaiyriPDAEYKkRLDELVE----LLDLGElldtpvRQLSLGQRMRCEL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2351811981 482 ARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQ--GRTVLLVVH 527
Cdd:COG4586 166 AAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRerGTTILLTSH 213
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
916-1114 |
1.11e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 56.78 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 916 ASPFPLEVRGLSarYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACvlEGDTVR 995
Cdd:PRK13543 7 TAPPLLAAHALA--FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT--RGDRSR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 996 GFVGLCAQDAHIFDSSIRENLRLArtgatdeelrAALDRARlldwAEALPAGLDTLVGEHG------ARLSGGQRQRLAL 1069
Cdd:PRK13543 83 FMAYLGHLPGLKADLSTLENLHFL----------CGLHGRR----AKQMPGSALAIVGLAGyedtlvRQLSAGQKKRLAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2351811981 1070 ARAILADFPVLVLDEPAEHLDLATADALTADLLAATRGRTTVLIT 1114
Cdd:PRK13543 149 ARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGGGAALVT 193
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
921-1085 |
1.12e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 56.96 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGaeRDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVD---------Acvleg 991
Cdd:COG1137 4 LEAENLVKSYGK--RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDithlpmhkrA----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 992 dtvRGFVGLCAQDAHIF-DSSIRENLRLARtgatdeELRAaLDRARLLDWAEALpagLDTLVGEH-----GARLSGGQRQ 1065
Cdd:COG1137 77 ---RLGIGYLPQEASIFrKLTVEDNILAVL------ELRK-LSKKEREERLEEL---LEEFGITHlrkskAYSLSGGERR 143
|
170 180
....*....|....*....|
gi 2351811981 1066 RLALARAILADFPVLVLDEP 1085
Cdd:COG1137 144 RVEIARALATNPKFILLDEP 163
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
921-1157 |
1.34e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 58.65 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLlrfldarEGTYRIGGvdacvLEGDTVrgFVGL 1000
Cdd:NF040905 2 LEMRGITKTFPGVK--ALDDVNLSVREGEIHALCGENGAGKSTLMKVL-------SGVYPHGS-----YEGEIL--FDGE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDAHIFDS------------------SIRENLRL----ARTGATDeeLRAALDRAR-LLDwaealPAGL----DTLVG 1053
Cdd:NF040905 66 VCRFKDIRDSealgiviihqelalipylSIAENIFLgnerAKRGVID--WNETNRRAReLLA-----KVGLdespDTLVT 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1054 EHGArlsgGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTaDLLAATRGR--TTVLITHRLQGLEAV-DEVVVLE 1130
Cdd:NF040905 139 DIGV----GKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALL-DLLLELKAQgiTSIIISHKLNEIRRVaDSITVLR 213
|
250 260 270
....*....|....*....|....*....|...
gi 2351811981 1131 AGRVVQRgpyadLTAEEGPL------RRMLERE 1157
Cdd:NF040905 214 DGRTIET-----LDCRADEVtedriiRGMVGRD 241
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
937-1139 |
1.34e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 57.59 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 937 ALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGLCAQDAHIFDSSIRENL 1016
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVDWSFPVLVEDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1017 RLARTGATDEELRA-ALDRARLldwAEALpAGLDTLVGEHG--ARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLAT 1093
Cdd:PRK15056 102 MMGRYGHMGWLRRAkKRDRQIV---TAAL-ARVDMVEFRHRqiGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2351811981 1094 aDALTADLLAATR--GRTTVLITHRLQGLEAVDEVVVLEAGRVVQRGP 1139
Cdd:PRK15056 178 -EARIISLLRELRdeGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGP 224
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
348-505 |
1.53e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.81 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 348 PSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGvDLatlaperwreRIAWVPQR-PYLFAGT--- 423
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ-DL----------IVARLQQDpPRNVEGTvyd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 424 -IAENV---------------------------RLARPDADDGAVAAALRDAGAYDFVAELPDGAQTLLGEdgagLSAGQ 475
Cdd:PRK11147 86 fVAEGIeeqaeylkryhdishlvetdpseknlnELAKLQEQLDHHNLWQLENRINEVLAQLGLDPDAALSS----LSGGW 161
|
170 180 190
....*....|....*....|....*....|
gi 2351811981 476 RQRLALARAFLADRPLLLLDEPTASLDGET 505
Cdd:PRK11147 162 LRKAALGRALVSNPDVLLLDEPTNHLDIET 191
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
333-502 |
1.53e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 57.93 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGrGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPerwRER-IA 411
Cdd:PRK11650 4 LKLQAVRKSYDG-KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEP---ADRdIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 412 WVPQR----PYLfagTIAENVRLArpdaddgavaaaLRDAG-AYDFVAELPDGAQTLLGEDG------AGLSAGQRQRLA 480
Cdd:PRK11650 80 MVFQNyalyPHM---SVRENMAYG------------LKIRGmPKAEIEERVAEAARILELEPlldrkpRELSGGQRQRVA 144
|
170 180
....*....|....*....|..
gi 2351811981 481 LARAFLADRPLLLLDEPTASLD 502
Cdd:PRK11650 145 MGRAIVREPAVFLFDEPLSNLD 166
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
938-1115 |
1.71e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.81 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 938 LDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGvDACV--LEGD-------TVRGFV--GLCAQDAH 1006
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ-DLIVarLQQDpprnvegTVYDFVaeGIEEQAEY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1007 IfdssiRENLRLARTGATD---------EELRAALDRA-------RLLDWAEALPAGLDTLVGEhgarLSGGQRQRLALA 1070
Cdd:PRK11147 98 L-----KRYHDISHLVETDpseknlnelAKLQEQLDHHnlwqlenRINEVLAQLGLDPDAALSS----LSGGWLRKAALG 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2351811981 1071 RAILADFPVLVLDEPAEHLDLATADALtADLLAATRGrTTVLITH 1115
Cdd:PRK11147 169 RALVSNPDVLLLDEPTNHLDIETIEWL-EGFLKTFQG-SIIFISH 211
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
921-1138 |
1.84e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 58.71 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYA--GAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGV-------------D 985
Cdd:PRK10261 13 LAVENLNIAFMqeQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqvielsE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 986 ACVLEGDTVRGfvglcAQDAHIFDS-------------SIRENLRLARTGATDEELRAAldrARLLDWAEALPAglDTLV 1052
Cdd:PRK10261 93 QSAAQMRHVRG-----ADMAMIFQEpmtslnpvftvgeQIAESIRLHQGASREEAMVEA---KRMLDQVRIPEA--QTIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1053 GEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLaTADALTADLLAATRGRTT---VLITHRLQGL-EAVDEVVV 1128
Cdd:PRK10261 163 SRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDV-TIQAQILQLIKVLQKEMSmgvIFITHDMGVVaEIADRVLV 241
|
250
....*....|
gi 2351811981 1129 LEAGRVVQRG 1138
Cdd:PRK10261 242 MYQGEAVETG 251
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
333-553 |
2.13e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 56.68 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRV-----RVGGVDLATLaperwR 407
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqAITDDNFEKL-----R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 408 ERIAWVPQRP-YLFAGTIA--------ENvRLARPDADDGAVAAALRDAGAYDFVAELPDGaqtllgedgagLSAGQRQR 478
Cdd:PRK13648 83 KHIGIVFQNPdNQFVGSIVkydvafglEN-HAVPYDEMHRRVSEALKQVDMLERADYEPNA-----------LSGGQKQR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2351811981 479 LALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQGR--TVLLVVHRPALLPLADRVVRLEPGATLRPEKPE 553
Cdd:PRK13648 151 VAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPT 227
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
636-756 |
2.17e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 57.14 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 636 PVLYLMVAVTATRAFGLGRAVFRYAERLVSHDAVLKMLAELRVAVYRGLERIAPAGLRRSRRGDLLSRLVADVDALQDYW 715
Cdd:cd18564 49 PLALLLLAAAALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLL 128
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2351811981 716 LRWLLPAGTAVVVGAATAGFIGWLLPA-AGIVLATGLLLAGA 756
Cdd:cd18564 129 VSGVLPLLTNLLTLVGMLGVMFWLDWQlALIALAVAPLLLLA 170
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
332-527 |
2.18e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 56.53 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 332 RLELEGVTVrheGRGEPSLDHA-SLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERI 410
Cdd:PRK10253 7 RLRGEQLTL---GYGKYTVAENlTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 411 AWVPQRPYLFAG-TIAENVRLARPDADDGAVAAALRDAGAYDfVAELPDGAQTLLGEDGAGLSAGQRQRLALARAFLADR 489
Cdd:PRK10253 84 GLLAQNATTPGDiTVQELVARGRYPHQPLFTRWRKEDEEAVT-KAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQET 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2351811981 490 PLLLLDEPTASLDGETEAGIVEAVRRL--AQGRTVLLVVH 527
Cdd:PRK10253 163 AIMLLDEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLH 202
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
924-1139 |
2.37e-08 |
|
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: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 924 RGLSARYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTL----AQVLLRFLDAREGTYRIGGVDACVLEgDTVRGFVG 999
Cdd:TIGR00956 63 RKLKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLlktiASNTDGFHIGVEGVITYDGITPEEIK-KHYRGDVV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1000 LCAQ-DAHIFDSSIRENLRLA---RTGATDEELRAALDRARLLDWAEALPAGL----DTLVGEHGAR-LSGGQRQRLALA 1070
Cdd:TIGR00956 142 YNAEtDVHFPHLTVGETLDFAarcKTPQNRPDGVSREEYAKHIADVYMATYGLshtrNTKVGNDFVRgVSGGERKRVSIA 221
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 1071 RAILADFPVLVLDEPAEHLDLATA----DAL--TADLLaatrgRTTVLIThRLQ----GLEAVDEVVVLEAGRVVQRGP 1139
Cdd:TIGR00956 222 EASLGGAKIQCWDNATRGLDSATAlefiRALktSANIL-----DTTPLVA-IYQcsqdAYELFDKVIVLYEGYQIYFGP 294
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
320-545 |
2.61e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.87 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 320 RRGGTADVPESLRLELEGVTVRHEGRgepsLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLA 399
Cdd:PRK09700 253 MKENVSNLAHETVFEVRNVTSRDRKK----VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 400 TLAP-ERWRERIAWVPQ--RPYLFAG--TIAENVRLARpdaddgavaaALRDA---GAYDFVAE-----LPDGAQTLLG- 465
Cdd:PRK09700 329 PRSPlDAVKKGMAYITEsrRDNGFFPnfSIAQNMAISR----------SLKDGgykGAMGLFHEvdeqrTAENQRELLAl 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 466 ------EDGAGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLA-QGRTVLLVVHR-PALLPLADR 537
Cdd:PRK09700 399 kchsvnQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSElPEIITVCDR 478
|
....*...
gi 2351811981 538 VVRLEPGA 545
Cdd:PRK09700 479 IAVFCEGR 486
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
350-527 |
3.40e-08 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 56.84 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 350 LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPD----EGRVRVGGVDLATLAPERWRE----RIAWVPQRP--YL 419
Cdd:COG4170 23 VDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLKLSPRERRKiigrEIAMIFQEPssCL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 420 F-AGTIAENVRLA------------RPDADDGAVAAALRDAGAYDFVA-------ELPDGaqtllgedgaglsAGQRQRL 479
Cdd:COG4170 103 DpSAKIGDQLIEAipswtfkgkwwqRFKWRKKRAIELLHRVGIKDHKDimnsyphELTEG-------------ECQKVMI 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 480 ALArafLADRP-LLLLDEPTASLDGETEAGIVEAVRRLAQ--GRTVLLVVH 527
Cdd:COG4170 170 AMA---IANQPrLLIADEPTNAMESTTQAQIFRLLARLNQlqGTSILLISH 217
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
360-531 |
3.82e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 57.93 E-value: 3.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 360 GETVALVGPSGVGKSTLLDVVLGFTAPD--EGRVRVGGVdlatlaPERwRERIAWVPQrpYLFAGTIAENVRLARPDADD 437
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGF------PKK-QETFARISG--YCEQNDIHSPQVTVRESLIY 976
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 438 GAVAAALRDAGAYD---FV------AELPDGAQTLLGEDG-AGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEA 507
Cdd:PLN03140 977 SAFLRLPKEVSKEEkmmFVdevmelVELDNLKDAIVGLPGvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAA 1056
|
170 180
....*....|....*....|....*
gi 2351811981 508 GIVEAVRR-LAQGRTVLLVVHRPAL 531
Cdd:PLN03140 1057 IVMRTVRNtVDTGRTVVCTIHQPSI 1081
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
921-1117 |
4.17e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 55.81 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAgaERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRfLDAREGTYRIGG----VDACVLEG----D 992
Cdd:PRK14258 8 IKVNNLSFYYD--TQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNR-MNELESEVRVEGrvefFNQNIYERrvnlN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 993 TVRGFVGLCAQDAHIFDSSIRENLR--LARTG-----ATDEELRAALDRARLldWAEalpagLDTLVGEHGARLSGGQRQ 1065
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAygVKIVGwrpklEIDDIVESALKDADL--WDE-----IKHKIHKSALDLSGGQQQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2351811981 1066 RLALARAILADFPVLVLDEPAEHLDLAtADALTADLLAATRGR---TTVLITHRL 1117
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPI-ASMKVESLIQSLRLRselTMVIVSHNL 211
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
350-542 |
4.30e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.49 E-value: 4.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 350 LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVggvdlatlaPERWRerIAWVPQRPYLFAGTIAENV- 428
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTF---------PGNWQ--LAWVNQETPALPQPALEYVi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 429 ---RLARPDADDGAVAAALRDAGAYDFV----------------AELPDG---AQTLLGEDGAGLSAGQRQRLALARAFL 486
Cdd:PRK10636 86 dgdREYRQLEAQLHDANERNDGHAIATIhgkldaidawtirsraASLLHGlgfSNEQLERPVSDFSGGWRMRLNLAQALI 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2351811981 487 ADRPLLLLDEPTASLDgeTEAGI-VEAVRRLAQGRTVLLVVHRPALLPLADRVVRLE 542
Cdd:PRK10636 166 CRSDLLLLDEPTNHLD--LDAVIwLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIE 220
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
930-1139 |
4.36e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.81 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 930 YAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDaregtyriGGVdacVLEGDTVRGF----------VG 999
Cdd:TIGR00956 771 IKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVT--------TGV---ITGGDRLVNGrpldssfqrsIG 839
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1000 LCAQ-DAHIFDSSIRENLRLA---RTGA--TDEELRAALDRA-RLL---DWAEAlpagldtLVGEHGARLSGGQRQRLAL 1069
Cdd:TIGR00956 840 YVQQqDLHLPTSTVRESLRFSaylRQPKsvSKSEKMEYVEEViKLLemeSYADA-------VVGVPGEGLNVEQRKRLTI 912
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2351811981 1070 ARAILADFPVLV-LDEPAEHLDLATAdALTADLL--AATRGRTTVLITHRLQG--LEAVDEVVVLE-AGRVVQRGP 1139
Cdd:TIGR00956 913 GVELVAKPKLLLfLDEPTSGLDSQTA-WSICKLMrkLADHGQAILCTIHQPSAilFEEFDRLLLLQkGGQTVYFGD 987
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
339-544 |
4.97e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 54.58 E-value: 4.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 339 TVRHEGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPD---EGRVRVGGVDLATlAPERWRERIAWVPQ 415
Cdd:cd03233 12 TTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKE-FAEKYPGEIIYVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 416 R----PYLfagTIAENVrlarpdaddgavaaalrdagayDFVAELpDGAQTLlgedgAGLSAGQRQRLALARAFLADRPL 491
Cdd:cd03233 91 EdvhfPTL---TVRETL----------------------DFALRC-KGNEFV-----RGISGGERKRVSIAEALVSRASV 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2351811981 492 LLLDEPTASLDGETEAGIVEAVRRLAQ--GRTVLLVVHRPA--LLPLADRVVRLEPG 544
Cdd:cd03233 140 LCWDNSTRGLDSSTALEILKCIRTMADvlKTTTFVSLYQASdeIYDLFDKVLVLYEG 196
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
906-1102 |
6.59e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.72 E-value: 6.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 906 REPDSpagtpaSPFPL-EVRGLSARYAgaERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTyrIGGV 984
Cdd:PRK10636 303 RAPES------LPNPLlKMEKVSAGYG--DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGE--IGLA 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 985 DACVLegdtvrgfvGLCAQDAHIF----DSSIRENLRLARTgATDEELRaaldrarllDWAEALPAGLDTlVGEHGARLS 1060
Cdd:PRK10636 373 KGIKL---------GYFAQHQLEFlradESPLQHLARLAPQ-ELEQKLR---------DYLGGFGFQGDK-VTEETRRFS 432
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2351811981 1061 GGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTADLL 1102
Cdd:PRK10636 433 GGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALI 474
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
950-1134 |
6.70e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.79 E-value: 6.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 950 RIAVVGPSGSGKTTLAQVLLRFLDAREGT-YRIGGVDACVLEGDTVRGfvglcaqdahiFDSSIRENLRLART--GATDE 1026
Cdd:PLN03073 537 RIAMVGPNGIGKSTILKLISGELQPSSGTvFRSAKVRMAVFSQHHVDG-----------LDLSSNPLLYMMRCfpGVPEQ 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1027 ELRAALDRARLldwaealpagLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTADLLAATR 1106
Cdd:PLN03073 606 KLRAHLGSFGV----------TGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQG 675
|
170 180 190
....*....|....*....|....*....|..
gi 2351811981 1107 GrttVLIT----HRLQGleAVDEVVVLEAGRV 1134
Cdd:PLN03073 676 G---VLMVshdeHLISG--SVDELWVVSEGKV 702
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
17-295 |
7.11e-08 |
|
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: 55.52 E-value: 7.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 17 FFLAAVVALGVVGAALVIAQ--AMLVADVVVGGFEDGLTVSGLrtpliLLAAVALGRALVSWLTELAAYRASAAVKSELR 94
Cdd:cd18542 1 YLLAILALLLATALNLLIPLliRRIIDSVIGGGLRELLWLLAL-----LILGVALLRGVFRYLQGYLAEKASQKVAYDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 95 GRLLDRAAELGPGLLSDRRTGSLVTLATRGVDALDDYFARYLPQLGLAVVVPVAVLARIVTEDWVSAAIIVVTLPLIPLF 174
Cdd:cd18542 76 NDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 175 MILIGwatqSRMDRQWRL----LSRLSGHFLDVVAGLPTLKVFGRAKAQAESIRAITSQYRRATLRTLRIAFLSSFALEL 250
Cdd:cd18542 156 SYVFF----KKVRPAFEEireqEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDF 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2351811981 251 LATLSVALVAVTIGMRLVHGELDL-----YTGLVVLILapeayLPIRQVG 295
Cdd:cd18542 232 LSGLQIVLVLWVGGYLVINGEITLgelvaFISYLWMLI-----WPVRQLG 276
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
921-1148 |
7.30e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.90 E-value: 7.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAgaERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAqvLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGL 1000
Cdd:NF000106 14 VEVRGLVKHFG--EVKAVDGVDLDVREGTVLGVLGP*GAA**RGA--LPAHV*GPDAGRRPWRF*TWCANRRALRRTIG* 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 --CAQDAHIFDSSIRENLRLArtgATDEELRAALDRARLLDWAEALpaGLDTLVGEHGARLSGGQRQRLALARAILADFP 1078
Cdd:NF000106 90 hrPVR*GRRESFSGRENLYMI---GR*LDLSRKDARARADELLERF--SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2351811981 1079 VLVLDEPAEHLDLATADALTADLLAATRGRTTVLITHRL--QGLEAVDEVVVLEAGRVVQRGPYADLTAEEG 1148
Cdd:NF000106 165 VLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYmeEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
909-1138 |
7.55e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 55.50 E-value: 7.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 909 DSPAGTPASPFPLEVRGLSARYAGAERD--ALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLdAREGtyRIGGvdA 986
Cdd:PRK09473 1 TVPLAQQQADALLDVKDLRVTFSTPDGDvtAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL-AANG--RIGG--S 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 987 CVLEGdtvRGFVGL---------CAQDAHIFD---SSIRENLRLArtgatdEELRAALDRARLLDWAEALPAGLDTL--V 1052
Cdd:PRK09473 76 ATFNG---REILNLpekelnklrAEQISMIFQdpmTSLNPYMRVG------EQLMEVLMLHKGMSKAEAFEESVRMLdaV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1053 GEHGAR---------LSGGQRQRLALARAILADFPVLVLDEPAEHLDLaTADALTADLLAATR---GRTTVLITHRLqGL 1120
Cdd:PRK09473 147 KMPEARkrmkmypheFSGGMRQRVMIAMALLCRPKLLIADEPTTALDV-TVQAQIMTLLNELKrefNTAIIMITHDL-GV 224
|
250 260
....*....|....*....|
gi 2351811981 1121 EA--VDEVVVLEAGRVVQRG 1138
Cdd:PRK09473 225 VAgiCDKVLVMYAGRTMEYG 244
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
337-544 |
7.70e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 56.64 E-value: 7.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 337 GVTVRHEGRGEPSLDHASLVVDEGETVALVGPSGVGKS-TLLDVVLGFTAPD----EGRVRVGGVDLATLAPERWR---- 407
Cdd:PRK15134 12 SVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRgvrg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 408 ERIAWVPQRP-------YLFAGTIAENVRLARPDAddgavaaalRDAGAYDFVAELP----DGAQTLLGEDGAGLSAGQR 476
Cdd:PRK15134 92 NKIAMIFQEPmvslnplHTLEKQLYEVLSLHRGMR---------REAARGEILNCLDrvgiRQAAKRLTDYPHQLSGGER 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 477 QRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQ--GRTVLLVVHRPALL-PLADRVVRLEPG 544
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVrKLADRVAVMQNG 233
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
356-545 |
8.34e-08 |
|
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: 54.68 E-value: 8.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 356 VVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGR-------------------------VRVGGVDlATLAPErwreri 410
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKfddppdwdeildefrgselqnyftkLLEGDVK-VIVKPQ------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 411 aWVPQRPYLFAGTIAENVRLARpdaddgavaaalrDAGAYDFVAELPDgAQTLLGEDGAGLSAGQRQRLALARAFLADRP 490
Cdd:cd03236 95 -YVDLIPKAVKGKVGELLKKKD-------------ERGKLDELVDQLE-LRHVLDRNIDQLSGGELQRVAIAAALARDAD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 491 LLLLDEPTASLDGETEAGIVEAVRRLAQ-GRTVLLVVHRPALLP-LADRVVRL--EPGA 545
Cdd:cd03236 160 FYFFDEPSSYLDIKQRLNAARLIRELAEdDNYVLVVEHDLAVLDyLSDYIHCLygEPGA 218
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
356-545 |
1.06e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.95 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 356 VVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRvggvdlatlAPERWREriawVPQRpylFAGTI---------AE 426
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDYD---------EEPSWDE----VLKR---FRGTElqdyfkklaNG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 427 NVRLAR--------PDADDGAVAAALRDA---GAYDFVAELPdGAQTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLD 495
Cdd:COG1245 159 EIKVAHkpqyvdliPKVFKGTVRELLEKVderGKLDELAEKL-GLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 496 EPTASLDGETEAGIVEAVRRLAQ-GRTVLLVVHRPALLP-LADRVVRL--EPGA 545
Cdd:COG1245 238 EPSSYLDIYQRLNVARLIRELAEeGKYVLVVEHDLAILDyLADYVHILygEPGV 291
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
916-1136 |
1.20e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.69 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 916 ASPFpLEVRGLSARYAGAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDacVLEGDTVR 995
Cdd:PRK11288 1 SSPY-LSFDGIGKTFPGVK--ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE--MRFASTTA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 996 GF---VGLCAQDAHIF-DSSIRENLRL----ARTGATDEELRAALDRARLldwaEALpaGLDTLVGEHGARLSGGQRQRL 1067
Cdd:PRK11288 76 ALaagVAIIYQELHLVpEMTVAENLYLgqlpHKGGIVNRRLLNYEAREQL----EHL--GVDIDPDTPLKYLSIGQRQMV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2351811981 1068 ALARAILADFPVLVLDEPAEHLDLATADALTAdLLAATR--GRTTVLITHRLQGLEAV-DEVVVLEAGRVVQ 1136
Cdd:PRK11288 150 EIAKALARNARVIAFDEPTSSLSAREIEQLFR-VIRELRaeGRVILYVSHRMEEIFALcDAITVFKDGRYVA 220
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
934-1153 |
1.30e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 54.71 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 934 ERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVR--GFV-G----Lcaqdah 1006
Cdd:COG4586 34 EVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARriGVVfGqrsqL------ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1007 IFDSSIRENLRLART--GATDEELRAALDR-ARLLDWAEALpaglDTLVgehgaR-LSGGQRQRLALARAILADFPVLVL 1082
Cdd:COG4586 108 WWDLPAIDSFRLLKAiyRIPDAEYKKRLDElVELLDLGELL----DTPV-----RqLSLGQRMRCELAAALLHRPKILFL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2351811981 1083 DEPAEHLDLATADALTaDLLA---ATRGRTTVLITHRLQGLEAV-DEVVVLEAGRVVQRGPYADLTAEEGPLRRM 1153
Cdd:COG4586 179 DEPTIGLDVVSKEAIR-EFLKeynRERGTTILLTSHDMDDIEALcDRVIVIDHGRIIYDGSLEELKERFGPYKTI 252
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
921-1138 |
1.51e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 54.85 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAeRDALDSVDLRLTAGRRIAVVGPSGSGKTTLaqvlLRFLDARE----GTYRIGGVDACVLE-GDtvR 995
Cdd:PRK11650 4 LKLQAVRKSYDGK-TQVIKGIDLDVADGEFIVLVGPSGCGKSTL----LRMVAGLEritsGEIWIGGRVVNELEpAD--R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 996 GFvglcaqdAHIFDS-------SIREN----LRLARTGATDEELRAAlDRARLLdwaealpaGLDTLVGEHGARLSGGQR 1064
Cdd:PRK11650 77 DI-------AMVFQNyalyphmSVRENmaygLKIRGMPKAEIEERVA-EAARIL--------ELEPLLDRKPRELSGGQR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1065 QRLALARAILADFPVLVLDEPAEHLDlatadaltADLLAATR----------GRTTVLITHrlQGLEAV---DEVVVLEA 1131
Cdd:PRK11650 141 QRVAMGRAIVREPAVFLFDEPLSNLD--------AKLRVQMRleiqrlhrrlKTTSLYVTH--DQVEAMtlaDRVVVMNG 210
|
....*..
gi 2351811981 1132 GRVVQRG 1138
Cdd:PRK11650 211 GVAEQIG 217
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
921-1090 |
1.53e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 53.74 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGaeRDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLE-GDTVRGFVG 999
Cdd:PRK10895 4 LTAKNLAKAYKG--RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1000 LCAQDAHIFDS-SIRENLRLARtgatdeELRAALDRARLLDWAEALPA--GLDTLVGEHGARLSGGQRQRLALARAILAD 1076
Cdd:PRK10895 82 YLPQEASIFRRlSVYDNLMAVL------QIRDDLSAEQREDRANELMEefHIEHLRDSMGQSLSGGERRRVEIARALAAN 155
|
170
....*....|....
gi 2351811981 1077 FPVLVLDEPAEHLD 1090
Cdd:PRK10895 156 PKFILLDEPFAGVD 169
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
925-1115 |
1.56e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 55.33 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 925 GLSARYAGaERDALDSVDLRLTAGRRIAVVGPSGSGKTTLaqvlLRFldaregtyrIGGVD------ACVLEGDTVrgfv 998
Cdd:TIGR03719 9 RVSKVVPP-KKEILKDISLSFFPGAKIGVLGLNGAGKSTL----LRI---------MAGVDkdfngeARPQPGIKV---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 999 GLCAQDAHIFDS-SIRENLRLARtgatdEELRAALDR----------------------ARLLD-------W-------- 1040
Cdd:TIGR03719 71 GYLPQEPQLDPTkTVRENVEEGV-----AEIKDALDRfneisakyaepdadfdklaaeqAELQEiidaadaWdldsqlei 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2351811981 1041 -AEAL--PAGlDTLVgehgARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTaDLLAATRGrTTVLITH 1115
Cdd:TIGR03719 146 aMDALrcPPW-DADV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLE-RHLQEYPG-TVVAVTH 216
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
332-544 |
1.90e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 55.36 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 332 RLELEGVTVRHEGRGEpSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERWRERIA 411
Cdd:PRK10522 322 TLELRNVTFAYQDNGF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 412 WVPQRPYLFAGTIAENVRLARPDADDG-AVAAALRDAgaydfvAELPDGAQTLLGedgagLSAGQRQRLALARAFLADRP 490
Cdd:PRK10522 401 AVFTDFHLFDQLLGPEGKPANPALVEKwLERLKMAHK------LELEDGRISNLK-----LSKGQKKRLALLLALAEERD 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 491 LLLLDEPTASLDGEteagiveaVRRL----------AQGRTVLLVVHRPALLPLADRVVRLEPG 544
Cdd:PRK10522 470 ILLLDEWAADQDPH--------FRREfyqvllpllqEMGKTIFAISHDDHYFIHADRLLEMRNG 525
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
17-311 |
2.24e-07 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 54.03 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 17 FFLAAVVALGVVGAALVIAQamLVADVVVGGFEDGlTVSGLRTPLILLAAVALGRALVSWLTELAAYRASAAVKSELRGR 96
Cdd:cd18543 1 LILALLAALLATLAGLAIPL--LTRRAIDGPIAHG-DRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 97 LLDRAAELGPGLLSDRRTGSLVTLATRGVDALDDYFArYLPQLGLAVVVPVAVLARIVTEDWVSAAIIVVTLPLIplfmI 176
Cdd:cd18543 78 LFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLA-FGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPL----V 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 177 LIGWATQSRMDRQ-WRLLSR---LSGHFLDVVAGLPTLKVFGRAKAQAESIRAITSQYRRATLRTLRIAFLSSFALELLA 252
Cdd:cd18543 153 LVARRFRRRYFPAsRRAQDQagdLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALP 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 253 TLSVALVAVTIGMRLVHGELDLYTglvvlILAPEAYL-----PIRQVGAQYHAAAEGLSAAEEI 311
Cdd:cd18543 233 ELGLAAVLALGGWLVANGSLTLGT-----LVAFSAYLtmlvwPVRMLGWLLAMAQRARAAAERV 291
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
921-1138 |
2.66e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 53.47 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGtyriggvdACVLEGDTV----RG 996
Cdd:PRK13638 2 LATSDLWFRYQDEP--VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKG--------AVLWQGKPLdyskRG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 997 FVGLCAQDAHIF------------DSSIRENLRlaRTGATDEELraaldrARLLDwaEALpagldTLVGEHGAR------ 1058
Cdd:PRK13638 72 LLALRQQVATVFqdpeqqifytdiDSDIAFSLR--NLGVPEAEI------TRRVD--EAL-----TLVDAQHFRhqpiqc 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1059 LSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTADL-LAATRGRTTVLITHRLQGL-EAVDEVVVLEAGRVVQ 1136
Cdd:PRK13638 137 LSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIrRIVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILT 216
|
..
gi 2351811981 1137 RG 1138
Cdd:PRK13638 217 HG 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
921-1123 |
2.72e-07 |
|
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: 55.40 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGvDACVLEGDTVRGFVGL 1000
Cdd:TIGR01257 1938 LRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAG-KSILTNISDVHQNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQdahiFDS-----SIRENLRL-AR-TGATDEELRaaldraRLLDWA-EALPAGL--DTLVGEHgarlSGGQRQRLALA 1070
Cdd:TIGR01257 2017 CPQ----FDAiddllTGREHLYLyARlRGVPAEEIE------KVANWSiQSLGLSLyaDRLAGTY----SGGNKRKLSTA 2082
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 1071 RAILADFPVLVLDEPAEHLDLATADALTADLLAATR-GRTTVLITHRLQGLEAV 1123
Cdd:TIGR01257 2083 IALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIReGRAVVLTSHSMEECEAL 2136
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
914-1143 |
2.76e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 53.25 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 914 TPASPFPLEVRGLSARYAGaeRDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVL---- 989
Cdd:PRK10575 5 TNHSDTTFALRNVSFRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWsska 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 990 ---------------EGDTVRGFVGLCAQDAHifdssirenLRLARTGATDeelRAALDRARLLdwaealpAGLDTLVGE 1054
Cdd:PRK10575 83 farkvaylpqqlpaaEGMTVRELVAIGRYPWH---------GALGRFGAAD---REKVEEAISL-------VGLKPLAHR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1055 HGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTADL--LAATRGRTTVLITHRLQ-GLEAVDEVVVLEA 1131
Cdd:PRK10575 144 LVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVhrLSQERGLTVIAVLHDINmAARYCDYLVALRG 223
|
250
....*....|..
gi 2351811981 1132 GRVVQRGPYADL 1143
Cdd:PRK10575 224 GEMIAQGTPAEL 235
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
324-544 |
3.17e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.48 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 324 TADVPESLRLELEGVTVR--HEGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGG------ 395
Cdd:PRK10261 4 SDELDARDVLAVENLNIAfmQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 396 ----VDLATLAPERWRE----RIAWVPQRP-------YLFAGTIAENVRLARpdadDGAVAAALRDAGAYDFVAELPDgA 460
Cdd:PRK10261 84 srqvIELSEQSAAQMRHvrgaDMAMIFQEPmtslnpvFTVGEQIAESIRLHQ----GASREEAMVEAKRMLDQVRIPE-A 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 461 QTLLGEDGAGLSAGQRQRLALARAfLADRPLLLL-DEPTASLDGETEAGIVEAVRRLAQGRT--VLLVVHRPALLP-LAD 536
Cdd:PRK10261 159 QTILSRYPHQLSGGMRQRVMIAMA-LSCRPAVLIaDEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAeIAD 237
|
....*...
gi 2351811981 537 RVVRLEPG 544
Cdd:PRK10261 238 RVLVMYQG 245
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
360-544 |
3.25e-07 |
|
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: 50.83 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 360 GETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVggvdlatLAPERWRERIAWVPQrpylfagtiaenvrlarpdaddga 439
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY-------IDGEDILEEVLDQLL------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 440 vaaalrdagaydfvaelpdgaQTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLA-- 517
Cdd:smart00382 51 ---------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLll 109
|
170 180 190
....*....|....*....|....*....|....*...
gi 2351811981 518 -----QGRTVLLVVHRP------ALLPLADRVVRLEPG 544
Cdd:smart00382 110 llkseKNLTVILTTNDEkdlgpaLLRRRFDRRIVLLLI 147
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
935-1123 |
3.59e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.48 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 935 RDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVL-LRFLDAREGTYRIGGVDA-----------CVLEGDTVRGF----- 997
Cdd:PLN03073 190 RDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMaMHAIDGIPKNCQILHVEQevvgddttalqCVLNTDIERTQlleee 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 998 VGLCAQDAHIFDSSIRENLRLARTGATDEE-----LRAALDRARLLDW------AEALPAGLdTLVGEHGAR----LSGG 1062
Cdd:PLN03073 270 AQLVAQQRELEFETETGKGKGANKDGVDKDavsqrLEEIYKRLELIDAytaearAASILAGL-SFTPEMQVKatktFSGG 348
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 1063 QRQRLALARAILADFPVLVLDEPAEHLDLATADALTADLLAATrgRTTVLITHRLQGLEAV 1123
Cdd:PLN03073 349 WRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP--KTFIVVSHAREFLNTV 407
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
921-1147 |
3.81e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 52.57 E-value: 3.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAGAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLE-GDTVRGFVG 999
Cdd:PRK11614 6 LSFDKVSAHYGKIQ--ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQtAKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1000 LCAQDAHIFDS-SIRENLRLARTGATDEELRAALDRARLLdwaeaLPAGLDTLVGEHGArLSGGQRQRLALARAILADFP 1078
Cdd:PRK11614 84 IVPEGRRVFSRmTVEENLAMGGFFAERDQFQERIKWVYEL-----FPRLHERRIQRAGT-MSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2351811981 1079 VLVLDEPAehLDLATADALTA-DLLAATR--GRTTVLITHRL-QGLEAVDEVVVLEAGRVVQRGPYADLTAEE 1147
Cdd:PRK11614 158 LLLLDEPS--LGLAPIIIQQIfDTIEQLReqGMTIFLVEQNAnQALKLADRGYVLENGHVVLEDTGDALLANE 228
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
938-1116 |
3.83e-07 |
|
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: 51.00 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 938 LDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLlrfldarEGTYRIGgvdacvlegdtvRGFVGLCAQDAHIFdssirenlr 1017
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRAL-------AGLWPWG------------SGRIGMPEGEDLLF--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1018 LARTG-ATDEELRAALdrarLLDWAEALpagldtlvgehgarlSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADA 1096
Cdd:cd03223 69 LPQRPyLPLGTLREQL----IYPWDDVL---------------SGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR 129
|
170 180
....*....|....*....|
gi 2351811981 1097 LTAdlLAATRGRTTVLITHR 1116
Cdd:cd03223 130 LYQ--LLKELGITVISVGHR 147
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
305-505 |
4.10e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.97 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 305 LSAAEEIFSvlETEPRRGGTAD--VPESLRL-----ELEGVTvrhEGRGEPSL-DHASLVVDEGETVALVGPSGVGKSTL 376
Cdd:PRK11819 292 LARYEELLS--EEYQKRNETNEifIPPGPRLgdkviEAENLS---KSFGDRLLiDDLSFSLPPGGIVGIIGPNGAGKSTL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 377 LDVVLGFTAPDEGRVRVG-GVDLA-------TLAPER--WrERIA-----------WVPQRPYLfagtiaenvrlarpda 435
Cdd:PRK11819 367 FKMITGQEQPDSGTIKIGeTVKLAyvdqsrdALDPNKtvW-EEISggldiikvgnrEIPSRAYV---------------- 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2351811981 436 ddgavaaalrdaGAYDFvaelpDGA--QTLLGEdgagLSAGQRQRLALARAFLADRPLLLLDEPTASLDGET 505
Cdd:PRK11819 430 ------------GRFNF-----KGGdqQKKVGV----LSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVET 480
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
921-1143 |
5.02e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 53.21 E-value: 5.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYA--GAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLD----AREGTYRIGGVDACVLEGDTV 994
Cdd:PRK11022 4 LNVDKLSVHFGdeSAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 995 RGFVGlcAQDAHIFDS-------------SIRENLRLARTGATDEELRAALDRARLLdwaeALPAGLDTL-VGEHgaRLS 1060
Cdd:PRK11022 84 RNLVG--AEVAMIFQDpmtslnpcytvgfQIMEAIKVHQGGNKKTRRQRAIDLLNQV----GIPDPASRLdVYPH--QLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1061 GGQRQRLALARAILADFPVLVLDEPAEHLDLaTADALTADLLAATRGRTT---VLITHRLQGL-EAVDEVVVLEAGRVVQ 1136
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDV-TIQAQIIELLLELQQKENmalVLITHDLALVaEAAHKIIVMYAGQVVE 234
|
....*..
gi 2351811981 1137 RGPYADL 1143
Cdd:PRK11022 235 TGKAHDI 241
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
952-1127 |
5.24e-07 |
|
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: 51.45 E-value: 5.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 952 AVVGPSGSGKTTLaqvllrfldaregtyriggVDAC--VLEGDTVRGFVGLCAQDAHIFDSSIRENLRLARTGATDEELr 1029
Cdd:cd03240 26 LIVGQNGAGKTTI-------------------IEALkyALTGELPPNSKGGAHDPKLIREGEVRAQVKLAFENANGKKY- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1030 AALDRARLLDWAEALPAG-LDTLVGEHGARLSGGQRQ------RLALARAILADFPVLVLDEPAEHLDLATADALTADLL 1102
Cdd:cd03240 86 TITRSLAILENVIFCHQGeSNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLAEII 165
|
170 180
....*....|....*....|....*...
gi 2351811981 1103 AATRG---RTTVLITHRLQGLEAVDEVV 1127
Cdd:cd03240 166 EERKSqknFQLIVITHDEELVDAADHIY 193
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
921-1115 |
7.05e-07 |
|
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: 53.40 E-value: 7.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAgaERDALDSVDLRLTAGRRIAVVGPSGSGKTTLaqvlLRFLDARE----GTYRIGgvdacvlegDTVR- 995
Cdd:TIGR03719 323 IEAENLTKAFG--DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTL----FRMITGQEqpdsGTIEIG---------ETVKl 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 996 GFVGlcaQDAHIFDSS------IRENLRLARTGATDEELRAALDRARLldwaealpAGLD--TLVGEhgarLSGGQRQRL 1067
Cdd:TIGR03719 388 AYVD---QSRDALDPNktvweeISGGLDIIKLGKREIPSRAYVGRFNF--------KGSDqqKKVGQ----LSGGERNRV 452
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2351811981 1068 ALARAILADFPVLVLDEPAEHLDLATADALTADLLAAtrGRTTVLITH 1115
Cdd:TIGR03719 453 HLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVISH 498
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
948-1116 |
7.06e-07 |
|
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: 50.06 E-value: 7.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 948 GRRIAVVGPSGSGKTTLAQVLLRFLDAREGtyriggvdacvlegdtvrGFVGLCAQDAHIFDSSIRENlrlartgatdee 1027
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGG------------------GVIYIDGEDILEEVLDQLLL------------ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1028 lraaldrarlldwaealpagldTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTA-------D 1100
Cdd:smart00382 52 ----------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrllL 109
|
170
....*....|....*.
gi 2351811981 1101 LLAATRGRTTVLITHR 1116
Cdd:smart00382 110 LLKSEKNLTVILTTND 125
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
17-311 |
7.16e-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: 52.51 E-value: 7.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 17 FFLAAVVALGVVGAAL--------VIAQAMLVADVVVGGFEDGLTVSGLRTPLILLAA----VALGRALVSWLTELAAYR 84
Cdd:cd18564 1 LALALLALLLETALRLlepwplkvVIDDVLGDKPLPGLLGLAPLLGPDPLALLLLAAAalvgIALLRGLASYAGTYLTAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 85 ASAAVKSELRGRLLDRAAELGPGLLSDRRTGSLVTLATRGVDALDDYFARYLPQLGLAVVVPVAVLARIVTEDWVSAAII 164
Cdd:cd18564 81 VGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 165 VVTLPLIPLFMILIGWATQSRMDRQWRLLSRLSGHFLDVVAGLPTLKVFGRAKAQAESIRAITSQYRRATLRTLRIAFLS 244
Cdd:cd18564 161 LAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQALL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2351811981 245 SFALELLATLSVALVAVTIGMRLVHGELDLYTGLVVLILAPEAYLPIRQVGAQYHAAAEGLSAAEEI 311
Cdd:cd18564 241 SPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
940-1148 |
7.22e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 51.86 E-value: 7.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 940 SVDLRLT-------AGRRIAVVGPSGSGKTTLAQVLLRFLDArEGTYRIGGVDACVLEGDT---VRGFvgLCAQDAHIFD 1009
Cdd:PRK03695 7 AVSTRLGplsaevrAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAElarHRAY--LSQQQTPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1010 SSIRENLRLAR-TGATDEELRAALDRArlldwAEALpaGLDTLVGEHGARLSGGQRQRLALARAILADFP-------VLV 1081
Cdd:PRK03695 84 MPVFQYLTLHQpDKTRTEAVASALNEV-----AEAL--GLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPdinpagqLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 1082 LDEPAEHLDLATADALTADLLA-ATRGRTTVLITHRL-QGLEAVDEVVVLEAGRVVQRGPYADLTAEEG 1148
Cdd:PRK03695 157 LDEPMNSLDVAQQAALDRLLSElCQQGIAVVMSSHDLnHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
921-1152 |
7.45e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 52.07 E-value: 7.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSarYAGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGD---TVRGF 997
Cdd:PRK11831 8 VDMRGVS--FTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSrlyTVRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 998 VGLCAQDAHIF-DSSIRENLRLARTGATdeELRAALDRARLLDWAEALpaGLDTLVGEHGARLSGGQRQRLALARAILAD 1076
Cdd:PRK11831 86 MSMLFQSGALFtDMNVFDNVAYPLREHT--QLPAPLLHSTVMMKLEAV--GLRGAAKLMPSELSGGMARRAALARAIALE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 1077 FPVLVLDEPAEHLDLATADALTA--DLLAATRGRTTVLITHRL-QGLEAVDEVVVLEAGRVVQRGPYADLTAEEGPLRR 1152
Cdd:PRK11831 162 PDLIMFDEPFVGQDPITMGVLVKliSELNSALGVTCVVVSHDVpEVLSIADHAYIVADKKIVAHGSAQALQANPDPRVR 240
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
469-545 |
9.90e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 53.29 E-value: 9.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 469 AGLSAGQRQRLALARAFLADRP--LLLLDEPTASLDGETEAGIVEAVRRLA-QGRTVLLVVHRPALLPLADRVVRLEPGA 545
Cdd:PRK00635 475 ATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRdQGNTVLLVEHDEQMISLADRIIDIGPGA 554
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
333-544 |
1.02e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.97 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVrvggvdlatlapeRWRE--RI 410
Cdd:PRK15064 320 LEVENLTKGFDNG--PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-------------KWSEnaNI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 411 AWVPQRPylfagtiaenvrlarpdaddgavaaalrdagAYDFVAEL------------PDGAQT--------LLGEDGAG 470
Cdd:PRK15064 385 GYYAQDH-------------------------------AYDFENDLtlfdwmsqwrqeGDDEQAvrgtlgrlLFSQDDIK 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 471 -----LSAGQRQRLALARAFLADRPLLLLDEPTASLDGETeagiVEAVrRLA----QGrTVLLVVH-RPALLPLADRVVR 540
Cdd:PRK15064 434 ksvkvLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMES----IESL-NMAlekyEG-TLIFVSHdREFVSSLATRIIE 507
|
....
gi 2351811981 541 LEPG 544
Cdd:PRK15064 508 ITPD 511
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
333-506 |
1.15e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.62 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTvrHEGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGfTAPD---EGRVRVGGVDL-ATLAPERWRE 408
Cdd:PRK13549 6 LEMKNIT--KTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEELqASNIRDTERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 409 RIAWVPQR----PYLfagTIAENVRLARpdaddgavaaALRDAGAYDFvAELPDGAQTLLGEDGAG---------LSAGQ 475
Cdd:PRK13549 83 GIAIIHQElalvKEL---SVLENIFLGN----------EITPGGIMDY-DAMYLRAQKLLAQLKLDinpatpvgnLGLGQ 148
|
170 180 190
....*....|....*....|....*....|..
gi 2351811981 476 RQRLALARAFLADRPLLLLDEPTASL-DGETE 506
Cdd:PRK13549 149 QQLVEIAKALNKQARLLILDEPTASLtESETA 180
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
332-526 |
1.28e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.32 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 332 RLELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLG------------FtapdeGRVRVGGVDLa 399
Cdd:PRK10938 260 RIVLNNGVVSYNDR--PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltlF-----GRRRGSGETI- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 400 tlaperW--RERIAWVPQRPYL--FAGTIAENVRLArpdaddgavaAALRDAGAYDFVAE----LPDGAQTLLGEDGA-- 469
Cdd:PRK10938 332 ------WdiKKHIGYVSSSLHLdyRVSTSVRNVILS----------GFFDSIGIYQAVSDrqqkLAQQWLDILGIDKRta 395
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2351811981 470 -----GLSAGQrQRLAL-ARAFLADRPLLLLDEPTASLDGETEagivEAVRR-----LAQGRTVLLVV 526
Cdd:PRK10938 396 dapfhSLSWGQ-QRLALiVRALVKHPTLLILDEPLQGLDPLNR----QLVRRfvdvlISEGETQLLFV 458
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
948-1115 |
1.62e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.26 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 948 GRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGgvdaCVLEgdtVRGFvglcaqDAHifdssiRENLRLART------ 1021
Cdd:PRK11147 345 GDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG----TKLE---VAYF------DQH------RAELDPEKTvmdnla 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1022 -GATDEELRAaldRARlldwaEALPAGLDTLVGEHGAR-----LSGGQRQRLALARAILADFPVLVLDEPAEHLDLATAD 1095
Cdd:PRK11147 406 eGKQEVMVNG---RPR-----HVLGYLQDFLFHPKRAMtpvkaLSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLE 477
|
170 180
....*....|....*....|
gi 2351811981 1096 aLTADLLAATRGrTTVLITH 1115
Cdd:PRK11147 478 -LLEELLDSYQG-TVLLVSH 495
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
332-545 |
1.64e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.22 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 332 RLELEGVtvrhEGRG--EPsldhASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLA---------- 399
Cdd:PRK11288 257 RLRLDGL----KGPGlrEP----ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDirsprdaira 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 400 --TLAPE-RWRERIawVPQRpylfagTIAENVRL-ARPDADDGAVAAALR--DAGAYDFVAEL----PDGAQTLLGedga 469
Cdd:PRK11288 329 giMLCPEdRKAEGI--IPVH------SVADNINIsARRHHLRAGCLINNRweAENADRFIRSLniktPSREQLIMN---- 396
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2351811981 470 gLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLA-QGRTVLLVVHR-PALLPLADRVVRLEPGA 545
Cdd:PRK11288 397 -LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAaQGVAVLFVSSDlPEVLGVADRIVVMREGR 473
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
942-1146 |
1.71e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.94 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 942 DLRLTAGRRIAVVGPSGSGKTTLAQVLlrfldAREGTyriggvdacVLEGDTVRGF-----VGLCAQDAHIFDSSIRENL 1016
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARAL-----AGELP---------LLSGERQSQFshitrLSFEQLQKLVSDEWQRNNT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1017 RLARTGATDEELRAA-------LDRARLLDWAEALpaGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHL 1089
Cdd:PRK10938 89 DMLSPGEDDTGRTTAeiiqdevKDPARCEQLAQQF--GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1090 DLATADALtADLLA--ATRGRTTVLITHRLQGL-EAVDEVVVLEAGRVVQRGPYADLTAE 1146
Cdd:PRK10938 167 DVASRQQL-AELLAslHQSGITLVLVLNRFDEIpDFVQFAGVLADCTLAETGEREEILQQ 225
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
349-559 |
2.01e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 51.34 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 349 SLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPD----EGRVRVGGVDLATLAPerwRER-------IAWVPQRP 417
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNwrvtADRMRFDDIDLLRLSP---RERrklvghnVSMIFQEP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 418 --------------------YLFAGTIAENVRLARPDADDGAVAAALRDAgaYDFVAELPdgaqtllgedgAGLSAGQRQ 477
Cdd:PRK15093 99 qscldpservgrqlmqnipgWTYKGRWWQRFGWRKRRAIELLHRVGIKDH--KDAMRSFP-----------YELTEGECQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 478 RLALARAfLADRP-LLLLDEPTASLDGETEAGIVEAVRRLAQ--GRTVLLVVHRPALLP-LADRVVRLEPGATLRPEKPE 553
Cdd:PRK15093 166 KVMIAIA-LANQPrLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLSqWADKINVLYCGQTVETAPSK 244
|
....*.
gi 2351811981 554 GSVAVP 559
Cdd:PRK15093 245 ELVTTP 250
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
360-527 |
3.03e-06 |
|
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: 51.47 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 360 GETVALVGPSGVGKSTLLDVVLGFTAPDEGRvrvggvdlATLAPERwreRIAWVPQRPYLFAG-TIAENV---------- 428
Cdd:TIGR03719 31 GAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE--------ARPQPGI---KVGYLPQEPQLDPTkTVRENVeegvaeikda 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 429 ---------RLARPDA---DDGAVAAALRD----AGAYDFVAELPDGAQTLLGEDG----AGLSAGQRQRLALARAFLAD 488
Cdd:TIGR03719 100 ldrfneisaKYAEPDAdfdKLAAEQAELQEiidaADAWDLDSQLEIAMDALRCPPWdadvTKLSGGERRRVALCRLLLSK 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 2351811981 489 RPLLLLDEPTASLDGETEAGIVEAVRRLAQgrTVLLVVH 527
Cdd:TIGR03719 180 PDMLLLDEPTNHLDAESVAWLERHLQEYPG--TVVAVTH 216
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
894-1085 |
4.09e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 51.28 E-value: 4.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 894 RVYEVLDAPPPvrePDSPAGTPAspfpLEVRGLSARYAgaerD--ALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRF 971
Cdd:NF033858 247 RGHQPVVIPPR---PADDDDEPA----IEARGLTMRFG----DftAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGL 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 972 LDAREGTYRIGG--VDACVLEgdtVRGFVGLCAQDahiF----DSSIRENL----RLARTGATDEELR--AALDRARLLD 1039
Cdd:NF033858 316 LPASEGEAWLFGqpVDAGDIA---TRRRVGYMSQA---FslygELTVRQNLelhaRLFHLPAAEIAARvaEMLERFDLAD 389
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2351811981 1040 WAEALPAgldtlvgehgaRLSGGQRQRLALARAILADFPVLVLDEP 1085
Cdd:NF033858 390 VADALPD-----------SLPLGIRQRLSLAVAVIHKPELLILDEP 424
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
951-1115 |
4.71e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.58 E-value: 4.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 951 IAVVGPSGSGKTTLAQVLLRFLDAREGTyriggVDACV--------LEGD---TVRGFVGLCAQDahiFDSSIRENlrla 1019
Cdd:PRK13409 368 IGIVGPNGIGKTTFAKLLAGVLKPDEGE-----VDPELkisykpqyIKPDydgTVEDLLRSITDD---LGSSYYKS---- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1020 rtgatdeELRAALDRARLLDwaealpagldTLVGEhgarLSGGQRQRLALARAILADFPVLVLDEPAEHLD----LATAD 1095
Cdd:PRK13409 436 -------EIIKPLQLERLLD----------KNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrLAVAK 494
|
170 180
....*....|....*....|
gi 2351811981 1096 ALTAdlLAATRGRTTVLITH 1115
Cdd:PRK13409 495 AIRR--IAEEREATALVVDH 512
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
948-1129 |
5.45e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.58 E-value: 5.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 948 GRRIAVVGPSGSGKTTLAQVLlrfldAREGTYRIGGVDACVLEGDTVRGFVGLCAQD--AHIFDSSIR--------ENLR 1017
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKIL-----SGELIPNLGDYEEEPSWDEVLKRFRGTELQNyfKKLYNGEIKvvhkpqyvDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1018 LARTGATDEELRAALDRARLLDWAEALpaGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLD----LAT 1093
Cdd:PRK13409 174 KVFKGKVRELLKKVDERGKLDEVVERL--GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDirqrLNV 251
|
170 180 190
....*....|....*....|....*....|....*..
gi 2351811981 1094 ADALtADLlaaTRGRTTVLITHRLQGLEAV-DEVVVL 1129
Cdd:PRK13409 252 ARLI-REL---AEGKYVLVVEHDLAVLDYLaDNVHIA 284
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
932-1090 |
6.27e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.50 E-value: 6.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 932 GAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLaqvlLRFldaregtyrIGGVDAcVLEGDTVR--GF-VGLCAQDAHIF 1008
Cdd:PRK11819 17 PPKKQILKDISLSFFPGAKIGVLGLNGAGKSTL----LRI---------MAGVDK-EFEGEARPapGIkVGYLPQEPQLD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1009 DS-SIRENLRLARTgatdeELRAALDR----------------------ARLLD-------W---------AEAL--PAG 1047
Cdd:PRK11819 83 PEkTVRENVEEGVA-----EVKAALDRfneiyaayaepdadfdalaaeqGELQEiidaadaWdldsqleiaMDALrcPPW 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2351811981 1048 lDTLVGehgaRLSGGQRQRLALARAILADFPVLVLDEPAEHLD 1090
Cdd:PRK11819 158 -DAKVT----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
951-1130 |
7.36e-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: 50.17 E-value: 7.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 951 IAVVGPSGSGKTTLAQVLLRFLDAREGTyriggVDACV--------LEGDtvrgfvglcaqdahiFDSSIRENLRLARTG 1022
Cdd:COG1245 369 LGIVGPNGIGKTTFAKILAGVLKPDEGE-----VDEDLkisykpqyISPD---------------YDGTVEEFLRSANTD 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1023 ATD-----EELRAALDRARLLDwaealpagldTLVGEhgarLSGGQRQRLALARAILADFPVLVLDEPAEHLD----LAT 1093
Cdd:COG1245 429 DFGssyykTEIIKPLGLEKLLD----------KNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrLAV 494
|
170 180 190
....*....|....*....|....*....|....*...
gi 2351811981 1094 ADALTAdlLAATRGRTTVLITHRLQGLEAV-DEVVVLE 1130
Cdd:COG1245 495 AKAIRR--FAENRGKTAMVVDHDIYLIDYIsDRLMVFE 530
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
21-279 |
7.92e-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: 350020 [Multi-domain] Cd Length: 289 Bit Score: 49.02 E-value: 7.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 21 AVVALGVVGAAlviaqaMLVADVVVGGFEDGLTVSGLRTPL----ILLAAVALGRALVSWLTELAAYRASAAVKSELRGR 96
Cdd:cd18576 1 GLILLLLSSAI------GLVFPLLAGQLIDAALGGGDTASLnqiaLLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 97 LLDRAAELGPGLLSDRRTGSLVTLATRGVDALDDYFARYLPQLGLAVVVPVAVLARIVTEDWVSAAIIVVTLPLIPLFMI 176
Cdd:cd18576 75 LYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 177 LIGWATQsRMDRQWR-LLSRLSGHFLDVVAGLPTLKVFGRAKAQAESIRAITSQYRRATLRTLRI-AFLSSFaLELLATL 254
Cdd:cd18576 155 LFGRRIR-KLSKKVQdELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIrALFSSF-IIFLLFG 232
|
250 260 270
....*....|....*....|....*....|....
gi 2351811981 255 SVALVaVTIGMRLV-HGELD--------LYTGLV 279
Cdd:cd18576 233 AIVAV-LWYGGRLVlAGELTagdlvaflLYTLFI 265
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
951-1090 |
8.13e-06 |
|
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: 48.56 E-value: 8.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 951 IAVVGPSGSGKTTLAQVLLRFLDAREGtyriggvdacvlEGDTVRGFVGLCAQDAHI-FDSSIRENLRlartGATDEELR 1029
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEG------------DIEIELDTVSYKPQYIKAdYEGTVRDLLS----SITKDFYT 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 1030 AALDRARLLDwaealPAGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLD 1090
Cdd:cd03237 92 HPYFKTEIAK-----PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
310-544 |
8.25e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 49.82 E-value: 8.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 310 EIFSVLETEPRRGGtaDVPeslrLELEGVTVRH-EGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLG-FTAPD 387
Cdd:TIGR02633 241 EITSLYPHEPHEIG--DVI----LEARNLTCWDvINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGaYPGKF 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 388 EGRVRVGGVDLATLAPERW-RERIAWVPQR-------PYLFAGtiaENVRLArpDADDGAVAAALRDAGAYDFVAElpdG 459
Cdd:TIGR02633 315 EGNVFINGKPVDIRNPAQAiRAGIAMVPEDrkrhgivPILGVG---KNITLS--VLKSFCFKMRIDAAAELQIIGS---A 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 460 AQTLLGEDG------AGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQGRTVLLVVHR--PAL 531
Cdd:TIGR02633 387 IQRLKVKTAspflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSelAEV 466
|
250
....*....|...
gi 2351811981 532 LPLADRVVRLEPG 544
Cdd:TIGR02633 467 LGLSDRVLVIGEG 479
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
346-501 |
9.02e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.73 E-value: 9.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 346 GEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGG--VDLATlAPERWRERIAWVPQRPYLFAG- 422
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeIDFKS-SKEALENGISMVHQELNLVLQr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 423 TIAENVRLAR-PDADDGAVAAAL-RDAGAydFVAELpdGAQTLLGEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTAS 500
Cdd:PRK10982 89 SVMDNMWLGRyPTKGMFVDQDKMyRDTKA--IFDEL--DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
.
gi 2351811981 501 L 501
Cdd:PRK10982 165 L 165
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
921-1134 |
9.63e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 49.82 E-value: 9.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYA-GAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLL---------------RFLDAREGTYRIGGV 984
Cdd:TIGR02633 258 LEARNLTCWDViNPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFgaypgkfegnvfingKPVDIRNPAQAIRAG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 985 DACVLEGDTVRGFVGLCAQDAHIFDSSIRENLRLARTGATDEE--LRAALDRARLLDWAEALPAGldtlvgehgaRLSGG 1062
Cdd:TIGR02633 338 IAMVPEDRKRHGIVPILGVGKNITLSVLKSFCFKMRIDAAAELqiIGSAIQRLKVKTASPFLPIG----------RLSGG 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 1063 QRQRLALARAILADFPVLVLDEPAEHLDL-ATADALTADLLAATRGRTTVLITHRL-QGLEAVDEVVVLEAGRV 1134
Cdd:TIGR02633 408 NQQKAVLAKMLLTNPRVLILDEPTRGVDVgAKYEIYKLINQLAQEGVAIIVVSSELaEVLGLSDRVLVIGEGKL 481
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
59-312 |
1.68e-05 |
|
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: 48.25 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 59 TPLILLAAVALGRALVSWLTELAAYRASAAVKSELRGRLLDRAAELGPGLLSDRRTGSLVTLATRGVDALDDYFARYLPQ 138
Cdd:cd18585 36 TPAAGVRGFAITRTAGRYGERLVSHDATFRLLSNLRVWFYRKLEPLAPARLQKYRSGDLLNRIVADIDTLDNLYLRVLSP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 139 LGLAVVVPVAVLARIVTEDWVSAAIIVVTLPLIPLFMILIGWATQSRMDRQWRLL-SRLSGHFLDVVAGLPTLKVFGRAK 217
Cdd:cd18585 116 PVVALLVILATILFLAFFSPALALILLAGLLLAGVVIPLLFYRLGKKIGQQLVQLrAELRTELVDGLQGMAELLIFGALE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 218 AQAESIRAITSQYRRATLRTLRIAFLSSFALELLATLSVALVAVtIGMRLVH-GELD--LYTGLVVLILAP-EAYLPIRQ 293
Cdd:cd18585 196 RQRQQLEQLSDALIKEQRRLARLSGLSQALMILLSGLTVWLVLW-LGAPLVQnGALDgaLLAMLVFAVLASfEAVAPLPL 274
|
250
....*....|....*....
gi 2351811981 294 VgaqYHAAAEGLSAAEEIF 312
Cdd:cd18585 275 A---FQYLGETRAAARRLF 290
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
354-502 |
1.77e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 47.86 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 354 SLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLaTLAPERWR-ERIAWVPQRPylfagTIAENVR--- 429
Cdd:PRK15112 33 SFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYSYRsQRIRMIFQDP-----STSLNPRqri 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 430 ---LARPDADDGAVAAALRDAGAYDF---VAELPDGAQTLlgedGAGLSAGQRQRLALARAFLADRPLLLLDEPTASLD 502
Cdd:PRK15112 107 sqiLDFPLRLNTDLEPEQREKQIIETlrqVGLLPDHASYY----PHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
921-1138 |
1.98e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 47.33 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAgaERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLlrfldAREGTYRIggvdacvLEGDTVrgFVGL 1000
Cdd:CHL00131 8 LEIKNLHASVN--ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVI-----AGHPAYKI-------LEGDIL--FKGE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDahiFDSSIRENLR--LAR------TGATDEE-LRAALDRARL---------LDWAEALPAGLDtLVGEHGARL--- 1059
Cdd:CHL00131 72 SILD---LEPEERAHLGifLAFqypieiPGVSNADfLRLAYNSKRKfqglpeldpLEFLEIINEKLK-LVGMDPSFLsrn 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1060 -----SGGQRQRLALARAILADFPVLVLDEPAEHLDLataDAL-----TADLLaATRGRTTVLITHRLQGLEAV--DEVV 1127
Cdd:CHL00131 148 vnegfSGGEKKRNEILQMALLDSELAILDETDSGLDI---DALkiiaeGINKL-MTSENSIILITHYQRLLDYIkpDYVH 223
|
250
....*....|.
gi 2351811981 1128 VLEAGRVVQRG 1138
Cdd:CHL00131 224 VMQNGKIIKTG 234
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
623-790 |
2.27e-05 |
|
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: 47.55 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 623 VSGWLISRASEQPPVLYLMVAVTATRAFGLGRAVFRYAERLVSHDAVLKMLAELRVAVYRGLERIAPAGLRRSRRGDLLS 702
Cdd:cd07346 21 LTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 703 RLVADVDALQ----DYWLRWLLPAGTAVVVGAATAgFIGWLLpaAGIVLATGLLLAGAGVplVSGACSRHAERQLAPARA 778
Cdd:cd07346 101 RLTSDVDAVQnlvsSGLLQLLSDVLTLIGALVILF-YLNWKL--TLVALLLLPLYVLILR--YFRRRIRKASREVRESLA 175
|
170
....*....|..
gi 2351811981 779 DLATRITDLLGG 790
Cdd:cd07346 176 ELSAFLQESLSG 187
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
349-392 |
2.57e-05 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 48.01 E-value: 2.57e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2351811981 349 SLDHASL-----VVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVR 392
Cdd:PRK01889 179 ALDGEGLdvlaaWLSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAVR 227
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
18-295 |
2.60e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 47.56 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 18 FLAAVVALgVVGAALVIAQAMLVA---DVVVGG-------FEDGLTVSGLRTPLILLA----AVALGRALVSWLTELAAY 83
Cdd:cd18565 1 LVLGLLAS-ILNRLFDLAPPLLIGvaiDAVFNGeasflplVPASLGPADPRGQLWLLGgltvAAFLLESLFQYLSGVLWR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 84 RASAAVKSELRGRLLDRAAELGPGLLSDRRTGSLVTLATRGVDALDDYFARYLPQLGLAVVVPVAVLARIVTEDWVSAAI 163
Cdd:cd18565 80 RFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 164 IVVTLPLIPLFMILIGWATQSRMDRQWRLLSRLSGHFLDVVAGLPTLKVFGRAKAQAESIRAITSQYRRATLRTLRIAFL 243
Cdd:cd18565 160 ALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2351811981 244 SSFALELLATLSVALVAVTIGMRLVHGELDLYTGLVV------LILAPEAYLPIRQVG 295
Cdd:cd18565 240 FFPVIRLVAGAGFVATFVVGGYWVLDGPPLFTGTLTVgtlvtfLFYTQRLLWPLTRLG 297
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
931-1132 |
2.67e-05 |
|
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: 46.47 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 931 AGAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDA--REGTYRIGGvdacVLEGDTVRGFVGLCAQ-DAHI 1007
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILING----RPLDKNFQRSTGYVEQqDVHS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1008 FDSSIRENLRLartgatdeelrAALDRArlldwaealpagldtlvgehgarLSGGQRQRLALARAILADFPVLVLDEPAE 1087
Cdd:cd03232 92 PNLTVREALRF-----------SALLRG-----------------------LSVEQRKRLTIGVELAAKPSILFLDEPTS 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2351811981 1088 HLDlATADALTADLLA--ATRGRTTVLITHRLQG--LEAVDEVVVLEAG 1132
Cdd:cd03232 138 GLD-SQAAYNIVRFLKklADSGQAILCTIHQPSAsiFEKFDRLLLLKRG 185
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
333-518 |
3.07e-05 |
|
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: 47.90 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGrgEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGF--TAPDEGRVRVGGVDL-ATLAPERWRER 409
Cdd:TIGR02633 2 LEMKGIVKTFGG--VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLkASNIRDTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 410 IAWVPQRPYLFAG-TIAENV----RLARPDADDGAVAAALRdagAYDFVAE--LPDGAQTLLGEDgagLSAGQRQRLALA 482
Cdd:TIGR02633 80 IVIIHQELTLVPElSVAENIflgnEITLPGGRMAYNAMYLR---AKNLLRElqLDADNVTRPVGD---YGGGQQQLVEIA 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 2351811981 483 RAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQ 518
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKA 189
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
355-532 |
3.67e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 46.56 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 355 LVVDEGETVALVGPSGVGKSTLLDVVLGFTAPD--EGRVRVGGVDLATLAPE-RWRERIAWVPQRPYLFAG-TIAENVRL 430
Cdd:CHL00131 28 LSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILDLEPEeRAHLGIFLAFQYPIEIPGvSNADFLRL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 431 ARPDADDGAVAAALRDAGAYDFVAE---LPDGAQTLLGED-GAGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETE 506
Cdd:CHL00131 108 AYNSKRKFQGLPELDPLEFLEIINEklkLVGMDPSFLSRNvNEGFSGGEKKRNEILQMALLDSELAILDETDSGLDIDAL 187
|
170 180
....*....|....*....|....*..
gi 2351811981 507 AGIVEAVRRLA-QGRTVLLVVHRPALL 532
Cdd:CHL00131 188 KIIAEGINKLMtSENSIILITHYQRLL 214
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
922-1085 |
4.55e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.81 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 922 EVRGLSARYAGAErdALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLlrfldarEGTYRI--GGVDacVLEGD--TVRGF 997
Cdd:NF033858 3 RLEGVSHRYGKTV--ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLI-------AGARKIqqGRVE--VLGGDmaDARHR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 998 VGLCAQDAHI---------FDSSIRENL----RLARTGATDEELRAaldrARLLDwAEALPAGLDTLVGehgaRLSGGQR 1064
Cdd:NF033858 72 RAVCPRIAYMpqglgknlyPTLSVFENLdffgRLFGQDAAERRRRI----DELLR-ATGLAPFADRPAG----KLSGGMK 142
|
170 180
....*....|....*....|.
gi 2351811981 1065 QRLALARAILADFPVLVLDEP 1085
Cdd:NF033858 143 QKLGLCCALIHDPDLLILDEP 163
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
341-395 |
5.30e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.19 E-value: 5.30e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2351811981 341 RHEGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGG 395
Cdd:PRK13545 31 SKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG 85
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
623-712 |
5.36e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 46.38 E-value: 5.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 623 VSGWLISRASEQP-------PVLYLMVAVTatrafgLGRAVFRYAERLVSHDAVLKMLAELRVAVYRGLERIAPAGLRRS 695
Cdd:cd18778 21 LIRELVDLVTIGSkslglllGLALLLLGAY------LLRALLNFLRIYLNHVAEQKVVADLRSDLYDKLQRLSLRYFDDR 94
|
90
....*....|....*..
gi 2351811981 696 RRGDLLSRLVADVDALQ 712
Cdd:cd18778 95 QTGDLMSRVINDVANVE 111
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
471-542 |
7.42e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 7.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 471 LSAGQRQ------RLALArAFLADR-PLLLLDEPTASLDGETEAGIVEAV----RRLAQgrtVLLVVHRPALLPLADRVV 539
Cdd:PRK03918 789 LSGGERIalglafRLALS-LYLAGNiPLLILDEPTPFLDEERRRKLVDIMerylRKIPQ---VIIVSHDEELKDAADYVI 864
|
...
gi 2351811981 540 RLE 542
Cdd:PRK03918 865 RVS 867
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
654-758 |
8.34e-05 |
|
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: 45.94 E-value: 8.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 654 RAVFRYAERLVSHDAVLKMLAELRVAVYRGLERIAPAGLRRSRRGDLLSRLVADVDALQDY---WLRWLLPAGTAVVVGA 730
Cdd:cd18576 49 QAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTlttTLAEFLRQILTLIGGV 128
|
90 100
....*....|....*....|....*...
gi 2351811981 731 ATAGFIGWLLpaAGIVLATGLLLAGAGV 758
Cdd:cd18576 129 VLLFFISWKL--TLLMLATVPVVVLVAV 154
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
471-545 |
8.84e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 45.33 E-value: 8.84e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2351811981 471 LSAGQRQRLALARAFLADRP--LLLLDEPTASLDGETEAGIVEAVRRL-AQGRTVLLVVHRPALLPLADRVVRLEPGA 545
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLrDLGNTVLVVEHDEDTIRAADHVIDIGPGA 215
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
464-545 |
1.03e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.75 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 464 LGEDGAGLSAGQRQRLALARaFLADRP----LLLLDEPTASLDGETEAGIVEAVRRL-AQGRTVLLVVHRPALLPLADRV 538
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAK-FLYLPPkhptLFLLDEIATSLDNQQKSALLVQLRTLvSLGHSVIYIDHDPALLKQADYL 1771
|
....*..
gi 2351811981 539 VRLEPGA 545
Cdd:PRK00635 1772 IEMGPGS 1778
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
464-543 |
1.19e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.75 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 464 LGEDGAGLSAGQRQRLALARAFLADRP---LLLLDEPTASLDGETEAGIVEAVRRLA-QGRTVLLVVHRPALLPLADRVV 539
Cdd:PRK00635 803 LGRPLSSLSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKALIYVLQSLThQGHTVVIIEHNMHVVKVADYVL 882
|
....
gi 2351811981 540 RLEP 543
Cdd:PRK00635 883 ELGP 886
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
449-545 |
1.46e-04 |
|
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: 44.91 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 449 AYDFVAELPDGAQTL------------LGEDGAGLSAGQRQRLALARAFL---ADRPLLLLDEPTASLDGETEAGIVEAV 513
Cdd:cd03271 136 ALEFFENIPKIARKLqtlcdvglgyikLGQPATTLSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLHFHDVKKLLEVL 215
|
90 100 110
....*....|....*....|....*....|...
gi 2351811981 514 RRL-AQGRTVLLVVHRPALLPLADRVVRLEPGA 545
Cdd:cd03271 216 QRLvDKGNTVVVIEHNLDVIKCADWIIDLGPEG 248
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
989-1145 |
1.48e-04 |
|
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: 46.16 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 989 LEGDTVRGFVGLCAQDAHIFDSSIRENLRLARtgATDEELRAALDRARLLdwaeaLPAGLDTLVGEHGAR-LSGGQRQRL 1067
Cdd:TIGR00630 425 VGGKSIADVSELSIREAHEFFNQLTLTPEEKK--IAEEVLKEIRERLGFL-----IDVGLDYLSLSRAAGtLSGGEAQRI 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1068 ALARAILADFP-VL-VLDEPAehLDLATADalTADLLAATR-----GRTTVLITHRLQGLEAVDEVVVL------EAGRV 1134
Cdd:TIGR00630 498 RLATQIGSGLTgVLyVLDEPS--IGLHQRD--NRRLINTLKrlrdlGNTLIVVEHDEDTIRAADYVIDIgpgageHGGEV 573
|
170
....*....|.
gi 2351811981 1135 VQRGPYADLTA 1145
Cdd:TIGR00630 574 VASGTPEEILA 584
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
350-546 |
1.93e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.55 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 350 LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGF--TAPDEGRVRVGGvdlatlAPERWR-----ER--IAWVPQR---- 416
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVypHGSYEGEILFDG------EVCRFKdirdsEAlgIVIIHQElali 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 417 PYLfagTIAENVRLARPDA---------DDGAVAAALRDAGaydfvaeLPDGAQTLLGEDGAGlsagQRQRLALARAFLA 487
Cdd:NF040905 91 PYL---SIAENIFLGNERAkrgvidwneTNRRARELLAKVG-------LDESPDTLVTDIGVG----KQQLVEIAKALSK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 488 DRPLLLLDEPTASLDGETEAGIVEAVRRL-AQGRTVLLVVHR-PALLPLADRVVRLEPGAT 546
Cdd:NF040905 157 DVKLLILDEPTAALNEEDSAALLDLLLELkAQGITSIIISHKlNEIRRVADSITVLRDGRT 217
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
935-1143 |
1.96e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 44.82 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 935 RDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTV-----------RGFVGLCAQ 1003
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGARVTGDVTLNGEPLaaidaprlarlRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1004 DAHIFdsSIRENLRLAR------TGATDEELRAALDRARLLdwaealpAGLDTLVGEHGARLSGGQRQRLALARAILADF 1077
Cdd:PRK13547 94 PAFAF--SAREIVLLGRypharrAGALTHRDGEIAWQALAL-------AGATALVGRDVTTLSGGELARVQFARVLAQLW 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 1078 P---------VLVLDEPAEHLDLATADALTADLLAATR----GRTTVLITHRLQGLEAvDEVVVLEAGRVVQRGPYADL 1143
Cdd:PRK13547 165 PphdaaqpprYLLLDEPTAALDLAHQHRLLDTVRRLARdwnlGVLAIVHDPNLAARHA-DRIAMLADGAIVAHGAPADV 242
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
948-1129 |
2.19e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 45.55 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 948 GRRIAVVGPSGSGKTTLAQVLlrfldAREGTYRIGGVDACVLEGDTVRGFVGLCAQD--AHIFDSSIR--------ENLR 1017
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKIL-----SGELKPNLGDYDEEPSWDEVLKRFRGTELQDyfKKLANGEIKvahkpqyvDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1018 LARTGATDEELRAALDRARLLDWAEALpaGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLD----LAT 1093
Cdd:COG1245 174 KVFKGTVRELLEKVDERGKLDELAEKL--GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqrLNV 251
|
170 180 190
....*....|....*....|....*....|....*..
gi 2351811981 1094 ADALTaDLlaATRGRTTVLITHRLQGLEAV-DEVVVL 1129
Cdd:COG1245 252 ARLIR-EL--AEEGKYVLVVEHDLAILDYLaDYVHIL 285
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
921-1103 |
2.57e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.11 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 921 LEVRGLSARYAgaERDALDSVDLRLTAGRRIAVVGPSGSGKTTLaqvlLRFLDARE----GTYRIGgvdacvlegDTVR- 995
Cdd:PRK11819 325 IEAENLSKSFG--DRLLIDDLSFSLPPGGIVGIIGPNGAGKSTL----FKMITGQEqpdsGTIKIG---------ETVKl 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 996 GFVglcaqdahifDSSirenlrlartgatdeelRAALDRARLLdWaEALPAGLDTL-VG--EHGAR-------------- 1058
Cdd:PRK11819 390 AYV----------DQS-----------------RDALDPNKTV-W-EEISGGLDIIkVGnrEIPSRayvgrfnfkggdqq 440
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1059 -----LSGGQRQRLALARAILADFPVLVLDEPAEHLDLATADALTADLLA 1103
Cdd:PRK11819 441 kkvgvLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLE 490
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
922-1147 |
2.75e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 44.78 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 922 EVRGLSARYAGAERDaldsVDLRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVL-EGDTVR---GF 997
Cdd:PRK09700 267 EVRNVTSRDRKKVRD----ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRsPLDAVKkgmAY 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 998 VGLCAQDAHIFDS-SIRENLRLART-------GA-----TDEELRAALDRARLLdwaeALP-AGLDTLVGEhgarLSGGQ 1063
Cdd:PRK09700 343 ITESRRDNGFFPNfSIAQNMAISRSlkdggykGAmglfhEVDEQRTAENQRELL----ALKcHSVNQNITE----LSGGN 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1064 RQRLALARAILADFPVLVLDEPAEHLDL-ATADALTADLLAATRGRTTVLITHRLQGLEAV-DEVVVLEAGRVVQR-GPY 1140
Cdd:PRK09700 415 QQKVLISKWLCCCPEVIIFDEPTRGIDVgAKAEIYKVMRQLADDGKVILMVSSELPEIITVcDRIAVFCEGRLTQIlTNR 494
|
....*..
gi 2351811981 1141 ADLTAEE 1147
Cdd:PRK09700 495 DDMSEEE 501
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
464-545 |
2.78e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.39 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 464 LGEDGAGLSAGQRQRLALARAFLADRP--LLLLDEPTASLDGETEAGIVEAVRRLA-QGRTVLLVVHRPALLPLADRVVR 540
Cdd:TIGR00630 482 LSRAAGTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRLRdLGNTLIVVEHDEDTIRAADYVID 561
|
....*
gi 2351811981 541 LEPGA 545
Cdd:TIGR00630 562 IGPGA 566
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
449-543 |
2.82e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.39 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 449 AYDFVAELPDGAQTL------------LGEDGAGLSAGQRQRLALARAFLAD---RPLLLLDEPTASLDGETEAGIVEAV 513
Cdd:TIGR00630 796 AYEFFEAVPSISRKLqtlcdvglgyirLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVL 875
|
90 100 110
....*....|....*....|....*....|.
gi 2351811981 514 RRL-AQGRTVLLVVHRPALLPLADRVVRLEP 543
Cdd:TIGR00630 876 QRLvDKGNTVVVIEHNLDVIKTADYIIDLGP 906
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
948-1117 |
3.69e-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: 43.51 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 948 GRRIAVVGPSGSGKTTLAQVLlrfldAREGTYRIGGVDACVLEGDTVRGFVGLCAQDahIFDSSIRENLRLAR------- 1020
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKIL-----AGKLKPNLGKFDDPPDWDEILDEFRGSELQN--YFTKLLEGDVKVIVkpqyvdl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1021 -----TGATDEELRAALDRARLLDWAEALpaGLDTLVGEHGARLSGGQRQRLALARAILADFPVLVLDEPAEHLDLA--- 1092
Cdd:cd03236 99 ipkavKGKVGELLKKKDERGKLDELVDQL--ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKqrl 176
|
170 180
....*....|....*....|....*
gi 2351811981 1093 TADALTADLlaATRGRTTVLITHRL 1117
Cdd:cd03236 177 NAARLIREL--AEDDNYVLVVEHDL 199
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
360-510 |
3.70e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.85 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 360 GETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGGVDLATLAPERW---RERIAWVPQRPY-------LFAGTIAENVR 429
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLqalRRDIQFIFQDPYasldprqTVGDSIMEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 430 LARpdaDDGAVAAALRDAGAYDFVAELPDGAQTLLGEdgagLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEAGI 509
Cdd:PRK10261 430 VHG---LLPGKAAAARVAWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQI 502
|
.
gi 2351811981 510 V 510
Cdd:PRK10261 503 I 503
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
328-513 |
6.31e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.01 E-value: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 328 PESLR---LELEGVTVrheGRGEPS-LDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVG-GVDLATLA 402
Cdd:PRK10636 305 PESLPnplLKMEKVSA---GYGDRIiLDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGIKLGYFA 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 403 PErwreriawvpQRPYLFA--GTIAENVRLArpdadDGAVAAALRD-AGAYDFvaelpDGAQtlLGEDGAGLSAGQRQRL 479
Cdd:PRK10636 382 QH----------QLEFLRAdeSPLQHLARLA-----PQELEQKLRDyLGGFGF-----QGDK--VTEETRRFSGGEKARL 439
|
170 180 190
....*....|....*....|....*....|....*
gi 2351811981 480 ALArAFLADRP-LLLLDEPTASLDGETEAGIVEAV 513
Cdd:PRK10636 440 VLA-LIVWQRPnLLLLDEPTNHLDLDMRQALTEAL 473
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
471-505 |
8.52e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.57 E-value: 8.52e-04
10 20 30
....*....|....*....|....*....|....*
gi 2351811981 471 LSAGQRQRLALARAFLADRPLLLLDEPTASLDGET 505
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
359-377 |
1.00e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 42.00 E-value: 1.00e-03
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
333-527 |
1.47e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 41.70 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 333 LELEGVTVRHEGRgePSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFT--APDEGRVRVGGVDLATLAPE-RWRER 409
Cdd:PRK09580 2 LSIKDLHVSVEDK--AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEdRAGEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 410 IAWVPQRP--------YLFAGTIAENVRLARpdaddgaVAAALRDAGAYDFVAE---LPDGAQTLLGED-GAGLSAGQRQ 477
Cdd:PRK09580 80 IFMAFQYPveipgvsnQFFLQTALNAVRSYR-------GQEPLDRFDFQDLMEEkiaLLKMPEDLLTRSvNVGFSGGEKK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2351811981 478 RLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQG-RTVLLVVH 527
Cdd:PRK09580 153 RNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTH 203
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
19-282 |
1.49e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 42.08 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 19 LAAVVALGVVGAALVIAQAMLVADVVVGGF--EDGLTVSGLrtpLILLAAVALGRALVSWLTELAAYRASAAVKSELRGR 96
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDALpqGDLGLLVLL---ALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 97 LLDRAAELGPGLLSDRRTGSLVTLATRGVDALDDYFARYLPQLGLAVVVPVAVLARIVTEDWVSAAIIVVTLPLIPLFMI 176
Cdd:cd18550 78 LYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 177 LIGWATQSRMDRQWRLLSRLSGH---FLDVvAGLPTLKVFGRAKAQAESIRAITSQYRRATLRTLRIAFLSSFALELLAT 253
Cdd:cd18550 158 RVGRRRRKLTREQQEKLAELNSImqeTLSV-SGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTA 236
|
250 260
....*....|....*....|....*....
gi 2351811981 254 LSVALVAVTIGMRLVHGELDLYTgLVVLI 282
Cdd:cd18550 237 IGPALVYWVGGLLVIGGGLTIGT-LVAFT 264
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
153-272 |
1.61e-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: 42.00 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 153 IVTEDWVSAAIIVVTLPLIPLFMILIGWATQSRMDRQWRLLSRLSGHFLDVVAGLPTLKVFGRAKAQAESIRAITSQYRR 232
Cdd:cd18548 134 AFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTD 213
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2351811981 233 ATLRTLRIAFLSSFALELLATLSVALVAVTIGMRLVHGEL 272
Cdd:cd18548 214 TSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSL 253
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
157-303 |
1.64e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 41.70 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 157 DWVSAAIIVVTLPliplFMILIGWATQSRMDRQWRLL----SRLSGHFLDVVAGLPTLKVFGRAKAQAESIRAITSQYRR 232
Cdd:cd18540 141 NWKLALIVLAVVP----VLAVVSIYFQKKILKAYRKVrkinSRITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRR 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 233 ATLRTLRIAFLSSFALELLATLSVALVAVTIGMRLVHGELDLYTgLVVLI-LAPEAYLPIRQ--------VGAQyhAAAE 303
Cdd:cd18540 217 ASVRAARLSALFLPIVLFLGSIATALVLWYGGILVLAGAITIGT-LVAFIsYATQFFEPIQQlarvlaelQSAQ--ASAE 293
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
649-784 |
1.84e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 41.70 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 649 AFGLGRAVFRYAERLVSHDAVLKMLAELRVAVYRGLERIAPAGLRRSRRGDLLSRLVADVDALQDyWLRWLLPAGTAVVV 728
Cdd:cd18543 47 ALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQR-FLAFGPFLLGNLLT 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2351811981 729 GAATAGFIGWLLPAAGIVlatglllAGAGVPLVSGACSRhAERQLAPA-------RADLATRI 784
Cdd:cd18543 126 LVVGLVVMLVLSPPLALV-------ALASLPPLVLVARR-FRRRYFPAsrraqdqAGDLATVV 180
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
1047-1129 |
1.95e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1047 GLDTL-VGEHGARLSGGQRQRLALARAILADFP---VLVLDEPAEHLDLATADALTADLLAAT-RGRTTVLITHRLQGLE 1121
Cdd:PRK00635 797 GLDYLpLGRPLSSLSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKALIYVLQSLThQGHTVVIIEHNMHVVK 876
|
....*...
gi 2351811981 1122 AVDEVVVL 1129
Cdd:PRK00635 877 VADYVLEL 884
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
465-527 |
2.10e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 41.64 E-value: 2.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 465 GEDGAGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLAQ-GRTVLLVVH 527
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRdGATVLLTTQ 202
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1029-1090 |
2.20e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.92 E-value: 2.20e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2351811981 1029 RAALDRARLL--DWAEALpaGLDTLVGEHGAR-LSGGQrQRLAL-ARAILADFPVLVLDEPAEHLD 1090
Cdd:PRK10938 371 QAVSDRQQKLaqQWLDIL--GIDKRTADAPFHsLSWGQ-QRLALiVRALVKHPTLLILDEPLQGLD 433
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
932-1141 |
2.37e-03 |
|
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: 40.70 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 932 GAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLAQVLL------RFLD-----AREgtyRIGgvdacVLEGDTVRGFVGL 1000
Cdd:cd03270 5 GAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIyaegqrRYVEslsayARQ---FLG-----QMDKPDVDSIEGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1001 CAQDAhIFDSSIRENLRlaRTGATDEELraaLDRARLLdWAEA---------LPAGLDTLVGEHGAR-LSGGQRQRLALA 1070
Cdd:cd03270 77 SPAIA-IDQKTTSRNPR--STVGTVTEI---YDYLRLL-FARVgirerlgflVDVGLGYLTLSRSAPtLSGGEAQRIRLA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 1071 RAILAD-FPVL-VLDEPAEHLDLATADALTADLLA-ATRGRTTVLITHrlqgleavDEVVVLEAGRVVQRGPYA 1141
Cdd:cd03270 150 TQIGSGlTGVLyVLDEPSIGLHPRDNDRLIETLKRlRDLGNTVLVVEH--------DEDTIRAADHVIDIGPGA 215
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
949-976 |
2.46e-03 |
|
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440337 [Multi-domain] Cd Length: 206 Bit Score: 40.59 E-value: 2.46e-03
10 20
....*....|....*....|....*...
gi 2351811981 949 RRIAVVGPSGSGKTTLAQVLLRFLDARE 976
Cdd:COG0572 8 RIIGIAGPSGSGKTTFARRLAEQLGADK 35
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
935-1113 |
2.68e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 39.79 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 935 RDALDSVdlRLTAGRRIAVVGPSGSGKTTLAQVLLRFLDAREGTYRIGGVDACVLEGDTVRGFVGLcaqdaHIFDSSIRE 1014
Cdd:pfam13191 13 LDALDRV--RSGRPPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDENLPYSPLLEALTRE-----GLLRQLLDE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1015 nlrlartgatDEELRAALDRARLLDWAEALPAgldtLVGEHGARLSGGQRQRLALARAiLADFPVLVLDEpAEHLDLATA 1094
Cdd:pfam13191 86 ----------LESSLLEAWRAALLEALAPVPE----LPGDLAERLLDLLLRLLDLLAR-GERPLVLVLDD-LQWADEASL 149
|
170
....*....|....*....
gi 2351811981 1095 DALtaDLLAATRGRTTVLI 1113
Cdd:pfam13191 150 QLL--AALLRLLESLPLLV 166
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
349-532 |
4.00e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 40.88 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 349 SLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTA-PdeGRV-----RVGGVDLATLAPERWRE----RIAWVPQRP- 417
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyP--GRVmaeklEFNGQDLQRISEKERRNlvgaEVAMIFQDPm 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 418 ------YLFAGTIAENVRLARPDADDGavaaalRDAGAYDFVAE--LPDGAqTLLGEDGAGLSAGQRQRLALARAFLADR 489
Cdd:PRK11022 100 tslnpcYTVGFQIMEAIKVHQGGNKKT------RRQRAIDLLNQvgIPDPA-SRLDVYPHQLSGGMSQRVMIAMAIACRP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2351811981 490 PLLLLDEPTASLDGETEAGIVEAVRRLAQGR--TVLLVVHRPALL 532
Cdd:PRK11022 173 KLLIADEPTTALDVTIQAQIIELLLELQQKEnmALVLITHDLALV 217
|
|
| MobB |
COG1763 |
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; ... |
951-982 |
4.07e-03 |
|
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 441369 [Multi-domain] Cd Length: 162 Bit Score: 39.39 E-value: 4.07e-03
10 20 30
....*....|....*....|....*....|..
gi 2351811981 951 IAVVGPSGSGKTTLAQVLLRFLDAREgtYRIG 982
Cdd:COG1763 4 LGIVGYSGSGKTTLLEKLIPELKARG--LRVG 33
|
|
| RsgA |
COG1162 |
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis]; |
359-377 |
4.13e-03 |
|
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440776 [Multi-domain] Cd Length: 300 Bit Score: 40.48 E-value: 4.13e-03
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
951-1094 |
4.71e-03 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 41.09 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 951 IAVVGPSGSGKTTLAQVLLRFldaregtYRIGGVDACVLegDTVRGFVGLC-AQDAHIFDSSIRENLRLA--RTGATDEE 1027
Cdd:COG3451 207 TLILGPSGSGKSFLLKLLLLQ-------LLRYGARIVIF--DPGGSYEILVrALGGTYIDLSPGSPTGLNpfDLEDTEEK 277
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2351811981 1028 lraaldRARLLDWaealpagLDTLVGEHGARLSGGQRQRLALA------------RAILADFpVLVLDEPAEHLDLATA 1094
Cdd:COG3451 278 ------RDFLLEL-------LELLLGREGEPLTPEERAAIDRAvralyrradpeeRTTLSDL-YELLKEQPEAKDLAAR 342
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
469-538 |
4.86e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 41.07 E-value: 4.86e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2351811981 469 AGLSAGQRQRLALARAFLADRPLLLLDEPTASLDGETEAGIVEAVRRLA-QGRTVLLVVHR-PALLPLADRV 538
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVqQGVAIIVISSElPEVLGLSDRV 475
|
|
| clpX |
PRK05342 |
ATP-dependent Clp protease ATP-binding subunit ClpX; |
951-973 |
5.60e-03 |
|
ATP-dependent Clp protease ATP-binding subunit ClpX;
Pssm-ID: 235422 [Multi-domain] Cd Length: 412 Bit Score: 40.53 E-value: 5.60e-03
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1060-1130 |
5.89e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.92 E-value: 5.89e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2351811981 1060 SGGQRQRLALARAILADFPVLVLDEPAEHLDLataDALT--ADLLAATRGrTTVLITHRLQGLEA-VDEVVVLE 1130
Cdd:PRK10636 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLDL---DAVIwlEKWLKSYQG-TLILISHDRDFLDPiVDKIIHIE 220
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
932-1127 |
6.21e-03 |
|
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: 38.88 E-value: 6.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 932 GAERDALDSVDLRLTAGRRIAVVGPSGSGKTTLA-QVLLRFLDAREGTYRIGGVDAcvleGDTVrgfvglCAQDAHifds 1010
Cdd:cd03227 5 GRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILdAIGLALGGAQSATRRRSGVKA----GCIV------AAVSAE---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 1011 sirenLRLARTGatdeelraaldrarlldwaealpagldtlvgehgarLSGGQRQRLALARAI-LADF---PVLVLDEPA 1086
Cdd:cd03227 71 -----LIFTRLQ------------------------------------LSGGEKELSALALILaLASLkprPLYILDEID 109
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2351811981 1087 EHLDLATADALtADLLAATR--GRTTVLITHRLQGLEAVDEVV 1127
Cdd:cd03227 110 RGLDPRDGQAL-AEAILEHLvkGAQVIVITHLPELAELADKLI 151
|
|
| RecA-like_ClpX |
cd19497 |
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ... |
951-973 |
6.32e-03 |
|
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent protease ClpXP. In ClpXP, ClpX ATPase serves to specifically recognize, unfold, and translocate protein substrates into the chamber of ClpP protease for degradation. This RecA-like_ClpX domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410905 [Multi-domain] Cd Length: 251 Bit Score: 39.89 E-value: 6.32e-03
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
472-502 |
6.46e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 6.46e-03
10 20 30
....*....|....*....|....*....|.
gi 2351811981 472 SAGQRQRLALARAFLADRPLLLLDEPTASLD 502
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
459-537 |
6.57e-03 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to 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 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: 213208 [Multi-domain] Cd Length: 276 Bit Score: 39.88 E-value: 6.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 459 GAQTLLGEDGAGL----SAGQRQRLALA-RAFLADR---PLLLLDEPTASLDGETEAGIVEAVRRLAQGRTVLLVVHRPA 530
Cdd:cd03241 155 LFSTNPGEPLKPLakiaSGGELSRLMLAlKAILARKdavPTLIFDEIDTGISGEVAQAVGKKLKELSRSHQVLCITHLPQ 234
|
....*..
gi 2351811981 531 LLPLADR 537
Cdd:cd03241 235 VAAMADN 241
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
359-382 |
6.90e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 38.68 E-value: 6.90e-03
|
| ClpX |
COG1219 |
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ... |
951-973 |
7.47e-03 |
|
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440832 [Multi-domain] Cd Length: 409 Bit Score: 40.03 E-value: 7.47e-03
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
472-542 |
7.60e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.80 E-value: 7.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2351811981 472 SAGQRQ------RLALARAFLADRPLLLLDEPTASLDGETEAG----IVEAVRRLAQGRTVLLVV--HRPALLPLADRVV 539
Cdd:TIGR00606 1201 SAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIESlahaLVEIIKSRSQQRNFQLLVitHDEDFVELLGRSE 1280
|
...
gi 2351811981 540 RLE 542
Cdd:TIGR00606 1281 YVE 1283
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
341-395 |
8.43e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.41 E-value: 8.43e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2351811981 341 RHEGRGEPSLDHASLVVDEGETVALVGPSGVGKSTLLDVVLGFTAPDEGRVRVGG 395
Cdd:PRK13546 31 KHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG 85
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1057-1090 |
9.24e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 39.91 E-value: 9.24e-03
10 20 30
....*....|....*....|....*....|....
gi 2351811981 1057 ARLSGGQRQRLALARAILADFPVLVLDEPAEHLD 1090
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| AAA_24 |
pfam13479 |
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins. |
947-985 |
9.59e-03 |
|
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
Pssm-ID: 433243 Cd Length: 199 Bit Score: 38.85 E-value: 9.59e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2351811981 947 AGRRIAVVGPSGSGKTTLAQVLLR--FLDAREGTYRIGGVD 985
Cdd:pfam13479 1 KKLKILIYGPSGIGKTTFAKTLPKplFLDTEKGSKALDGDR 41
|
|
| |
