NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|648489723|ref|WP_026181474|]
View 

excinuclease ABC subunit UvrA [Thioalkalivibrio sp. ALJ7]

Protein Classification

excinuclease ABC subunit UvrA( domain architecture ID 11478512)

excinuclease ABC subunit UvrA is a DNA-binding ATPase that recognizes DNA adducts in the nucleotide excision repair process catalyzed by the UvrABC excinuclease repair system

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
uvrA PRK00349
excinuclease ABC subunit UvrA;
1-940 0e+00

excinuclease ABC subunit UvrA;


:

Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 1915.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723   1 MDSISIRGARTHNLKNVDLDLPRERLIVITGVSGSGKSSLAFDTLFAEGQRRYVESLSTYARQFLSMMEKPDVDQIEGLS 80
Cdd:PRK00349   3 MDKIIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  81 PAISIEQKSTSHNPRSTVGTITEIYDYLRLLFARAGEPRCPEHGETLAAQTISQMVDQVLALPEGDKVMLLAPVVRGRKG 160
Cdd:PRK00349  83 PAISIDQKTTSHNPRSTVGTVTEIYDYLRLLYARVGKPHCPNCGRPIEAQTVSQMVDRVLELPEGTRLQILAPVVRGRKG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 161 EHHKMLEAMRSQGYLRARINGEIHDLDALPALDPKRKHNIEIVIDRFRVREDLRQRLAESFETATELADGLALVAWMDEP 240
Cdd:PRK00349 163 EHKKLLENLRKQGFVRVRVDGEVYDLDEPPKLDKNKKHTIEVVVDRLVVKEDIRQRLADSIETALKLSDGLVVVEVMDDP 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 241 EREPMIFSARYACPVCGYALRELEPRLFSFNNPAGACPTCDGLGVRQYFDPERVVSQPALSLGGGAVRGWDRR-NAWYFS 319
Cdd:PRK00349 243 EAEELLFSEKFACPVCGFSIPELEPRLFSFNSPYGACPTCDGLGVKLEFDPDLVVPDPELSLAEGAIAPWSRSsSSYYFQ 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 320 LLTSLARHYGFDVETPWEELPAEVRAVVLHGSGTDKVKLSTPAANGRMRTDERVFEGVIPNLERRYRETDSSAVREELGR 399
Cdd:PRK00349 323 MLKSLAEHYGFDLDTPWKDLPEEVQDIILYGSGDEEIEFRYKNDRGRTRERKHPFEGVIPNLERRYRETESEYVREELEK 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 400 YLAEQPCPDCHGTRLNSAARHVFVNDMTLPEVTHMSVANAQAFFSDLQLPGRFAQIAEKIVREISSRLGFLNDVGLDYLT 479
Cdd:PRK00349 403 YMSERPCPSCKGKRLKPEALAVKVGGKNIGEVSELSIGEALEFFENLKLSEQEAKIAEPILKEIRERLKFLVDVGLDYLT 482
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 480 LDRSADTLSGGEAQRIRLASQIGSALVGVMYILDEPSIGLHQRDNARLLNTLSHLRDLGNTVIVVEHDEDAIRQADYVVD 559
Cdd:PRK00349 483 LSRSAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDEDTIRAADYIVD 562
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 560 IGPGAGRHGGQIVASGTPEAVTQHPDSLTGAYLRGTRCIPVPEHRIePDPDREIRVIGARGNNLKGGDFAFPTGLFTCVT 639
Cdd:PRK00349 563 IGPGAGVHGGEVVASGTPEEIMKNPNSLTGQYLSGKKKIEVPKERR-KGNGKFLKLKGARENNLKNVDVEIPLGKFTCVT 641
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 640 GVSGSGKSTLVNNTLYPAVATELHGGRHHIEEHERIDGLELIDKVVDIDQSPIGRTPRSNPATYTGLFTPIRELFAATAE 719
Cdd:PRK00349 642 GVSGSGKSTLINETLYKALARKLNGAKKVPGKHKEIEGLEHLDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAGTPE 721
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 720 ARSRGYKPGRFSFNVRGGRCEACQGDGVIKVEMHFLPDVFVPCDVCKGHRYNRETLEVRYKGKNVHEVLEMTVEEALDFF 799
Cdd:PRK00349 722 AKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEFF 801
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 800 QPVPVIHRKLEMLMEVGLSYIQLGQNATTLSGGEAQRIKLARELSKRDTGRTLYILDEPTTGLHFEDIAQLLRVLHRLRD 879
Cdd:PRK00349 802 EAIPKIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELSKRSTGKTLYILDEPTTGLHFEDIRKLLEVLHRLVD 881
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648489723 880 HGNTIVVIEHNLDVIKTADWLIDIGPEGGSGGGELLVAGTPEAVAGHPRSHTGRFLAPMLA 940
Cdd:PRK00349 882 KGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVATGTPEEVAKVEASYTGRYLKPVLE 942
 
Name Accession Description Interval E-value
uvrA PRK00349
excinuclease ABC subunit UvrA;
1-940 0e+00

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 1915.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723   1 MDSISIRGARTHNLKNVDLDLPRERLIVITGVSGSGKSSLAFDTLFAEGQRRYVESLSTYARQFLSMMEKPDVDQIEGLS 80
Cdd:PRK00349   3 MDKIIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  81 PAISIEQKSTSHNPRSTVGTITEIYDYLRLLFARAGEPRCPEHGETLAAQTISQMVDQVLALPEGDKVMLLAPVVRGRKG 160
Cdd:PRK00349  83 PAISIDQKTTSHNPRSTVGTVTEIYDYLRLLYARVGKPHCPNCGRPIEAQTVSQMVDRVLELPEGTRLQILAPVVRGRKG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 161 EHHKMLEAMRSQGYLRARINGEIHDLDALPALDPKRKHNIEIVIDRFRVREDLRQRLAESFETATELADGLALVAWMDEP 240
Cdd:PRK00349 163 EHKKLLENLRKQGFVRVRVDGEVYDLDEPPKLDKNKKHTIEVVVDRLVVKEDIRQRLADSIETALKLSDGLVVVEVMDDP 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 241 EREPMIFSARYACPVCGYALRELEPRLFSFNNPAGACPTCDGLGVRQYFDPERVVSQPALSLGGGAVRGWDRR-NAWYFS 319
Cdd:PRK00349 243 EAEELLFSEKFACPVCGFSIPELEPRLFSFNSPYGACPTCDGLGVKLEFDPDLVVPDPELSLAEGAIAPWSRSsSSYYFQ 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 320 LLTSLARHYGFDVETPWEELPAEVRAVVLHGSGTDKVKLSTPAANGRMRTDERVFEGVIPNLERRYRETDSSAVREELGR 399
Cdd:PRK00349 323 MLKSLAEHYGFDLDTPWKDLPEEVQDIILYGSGDEEIEFRYKNDRGRTRERKHPFEGVIPNLERRYRETESEYVREELEK 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 400 YLAEQPCPDCHGTRLNSAARHVFVNDMTLPEVTHMSVANAQAFFSDLQLPGRFAQIAEKIVREISSRLGFLNDVGLDYLT 479
Cdd:PRK00349 403 YMSERPCPSCKGKRLKPEALAVKVGGKNIGEVSELSIGEALEFFENLKLSEQEAKIAEPILKEIRERLKFLVDVGLDYLT 482
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 480 LDRSADTLSGGEAQRIRLASQIGSALVGVMYILDEPSIGLHQRDNARLLNTLSHLRDLGNTVIVVEHDEDAIRQADYVVD 559
Cdd:PRK00349 483 LSRSAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDEDTIRAADYIVD 562
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 560 IGPGAGRHGGQIVASGTPEAVTQHPDSLTGAYLRGTRCIPVPEHRIePDPDREIRVIGARGNNLKGGDFAFPTGLFTCVT 639
Cdd:PRK00349 563 IGPGAGVHGGEVVASGTPEEIMKNPNSLTGQYLSGKKKIEVPKERR-KGNGKFLKLKGARENNLKNVDVEIPLGKFTCVT 641
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 640 GVSGSGKSTLVNNTLYPAVATELHGGRHHIEEHERIDGLELIDKVVDIDQSPIGRTPRSNPATYTGLFTPIRELFAATAE 719
Cdd:PRK00349 642 GVSGSGKSTLINETLYKALARKLNGAKKVPGKHKEIEGLEHLDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAGTPE 721
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 720 ARSRGYKPGRFSFNVRGGRCEACQGDGVIKVEMHFLPDVFVPCDVCKGHRYNRETLEVRYKGKNVHEVLEMTVEEALDFF 799
Cdd:PRK00349 722 AKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEFF 801
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 800 QPVPVIHRKLEMLMEVGLSYIQLGQNATTLSGGEAQRIKLARELSKRDTGRTLYILDEPTTGLHFEDIAQLLRVLHRLRD 879
Cdd:PRK00349 802 EAIPKIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELSKRSTGKTLYILDEPTTGLHFEDIRKLLEVLHRLVD 881
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648489723 880 HGNTIVVIEHNLDVIKTADWLIDIGPEGGSGGGELLVAGTPEAVAGHPRSHTGRFLAPMLA 940
Cdd:PRK00349 882 KGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVATGTPEEVAKVEASYTGRYLKPVLE 942
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
1-941 0e+00

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 1877.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723   1 MDSISIRGARTHNLKNVDLDLPRERLIVITGVSGSGKSSLAFDTLFAEGQRRYVESLSTYARQFLSMMEKPDVDQIEGLS 80
Cdd:COG0178    3 MDKIRIRGAREHNLKNIDVDIPRNKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  81 PAISIEQKSTSHNPRSTVGTITEIYDYLRLLFARAGEPRCPEHGETLAAQTISQMVDQVLALPEGDKVMLLAPVVRGRKG 160
Cdd:COG0178   83 PAISIEQKTTSRNPRSTVGTVTEIYDYLRLLFARVGTPHCPICGRPVEKQTVDQIVDRILALPEGTRLQILAPVVRGRKG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 161 EHHKMLEAMRSQGYLRARINGEIHDLDALPALDPKRKHNIEIVIDRFRVREDLRQRLAESFETATELADGLALVAWMDEP 240
Cdd:COG0178  163 EHKELLEELRKQGFVRVRVDGEVYDLDEEPELDKNKKHTIEVVVDRLVVKEDIRSRLADSVETALKLGDGLVIVEVVDEG 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 241 ErePMIFSARYACPVCGYALRELEPRLFSFNNPAGACPTCDGLGVRQYFDPERVVSQPALSLGGGAVRGWDRR-NAWYFS 319
Cdd:COG0178  243 E--ELLFSEKFACPDCGISFEELEPRLFSFNSPYGACPTCDGLGRVLEFDPDLVIPDPSLSLAEGAIAPWSGPsSSYYFQ 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 320 LLTSLARHYGFDVETPWEELPAEVRAVVLHGSGtDKVKLSTPAaNGRMRTDERVFEGVIPNLERRYRETDSSAVREELGR 399
Cdd:COG0178  321 LLEALAKHYGFDLDTPWKDLPEEQRDLILYGSD-EKIKFRYKN-RGRRRTYEKPFEGVIPFLERRYRETYSEHVREELSR 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 400 YLAEQPCPDCHGTRLNSAARHVFVNDMTLPEVTHMSVANAQAFFSDLQLPGRFAQIAEKIVREISSRLGFLNDVGLDYLT 479
Cdd:COG0178  399 YMSETPCPACKGARLKPEALAVKIGGKNIAELTALSIDEALEFFENLELTEREAEIAERILKEIRSRLGFLVDVGLDYLT 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 480 LDRSADTLSGGEAQRIRLASQIGSALVGVMYILDEPSIGLHQRDNARLLNTLSHLRDLGNTVIVVEHDEDAIRQADYVVD 559
Cdd:COG0178  479 LDRSAGTLSGGEAQRIRLATQIGSGLVGVLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDTIRAADYIID 558
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 560 IGPGAGRHGGQIVASGTPEAVTQHPDSLTGAYLRGTRCIPVPEHRIEPDpDREIRVIGARGNNLKGGDFAFPTGLFTCVT 639
Cdd:COG0178  559 IGPGAGEHGGEVVAQGTPEEILKNPDSLTGQYLSGRKRIPVPKKRRKGN-GKFLTIKGARENNLKNVDVEIPLGVLTCVT 637
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 640 GVSGSGKSTLVNNTLYPAVATELHGGRHHIEEHERIDGLELIDKVVDIDQSPIGRTPRSNPATYTGLFTPIRELFAATAE 719
Cdd:COG0178  638 GVSGSGKSTLVNDILYPALARKLNGAKEKPGPHDSIEGLEHIDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAQTPE 717
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 720 ARSRGYKPGRFSFNVRGGRCEACQGDGVIKVEMHFLPDVFVPCDVCKGHRYNRETLEVRYKGKNVHEVLEMTVEEALDFF 799
Cdd:COG0178  718 AKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEFF 797
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 800 QPVPVIHRKLEMLMEVGLSYIQLGQNATTLSGGEAQRIKLARELSKRDTGRTLYILDEPTTGLHFEDIAQLLRVLHRLRD 879
Cdd:COG0178  798 ENIPKIARKLQTLQDVGLGYIKLGQPATTLSGGEAQRVKLASELSKRSTGKTLYILDEPTTGLHFHDIRKLLEVLHRLVD 877
                        890       900       910       920       930       940       950
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 648489723 880 HGNTIVVIEHNLDVIKTADWLIDigpeggsgggeL----------LVA-GTPEAVAGHPRSHTGRFLAPMLAA 941
Cdd:COG0178  878 KGNTVVVIEHNLDVIKTADWIID-----------LgpeggdgggeIVAeGTPEEVAKVKASYTGRYLKEYLEA 939
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
4-924 0e+00

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: 1569.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723    4 ISIRGARTHNLKNVDLDLPRERLIVITGVSGSGKSSLAFDTLFAEGQRRYVESLSTYARQFLSMMEKPDVDQIEGLSPAI 83
Cdd:TIGR00630   2 IIVRGAREHNLKNIDVEIPRDKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGVMDKPDVDSIEGLSPAI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723   84 SIEQKSTSHNPRSTVGTITEIYDYLRLLFARAGEPRCPEHGETLAAQTISQMVDQVLALPEGDKVMLLAPVVRGRKGEHH 163
Cdd:TIGR00630  82 SIDQKTTSHNPRSTVGTITEIYDYLRLLFARVGTPYCPTCGRPISRQTPSQIVDQILALPEGTRVILLAPIVRGRKGEFR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  164 KMLEAMRSQGYLRARINGEIHDLDALPALDPKRKHNIEIVIDRFRVREDLRQRLAESFETATELADGLALVAWMDE---P 240
Cdd:TIGR00630 162 KLLEKLRKQGFARVRVDGEVYPLEDPPKLEKNKKHTIDVVIDRLTVKNENRSRLAESVETALRLGDGLLEVEFDDDeevA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  241 EREPMIFSARYACPVCGYALRELEPRLFSFNNPAGACPTCDGLGVRQYFDPERVVSQPALSLGGGAVRGWD-RRNAWYFS 319
Cdd:TIGR00630 242 ESKEELFSEKFACPECGFSLPELEPRLFSFNSPYGACPECSGLGIKQEFDPELIIPDPLLSLNGGAIVPFKkSTTSYYRQ 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  320 LLTSLARHYGFDVETPWEELPAEVRAVVLHGSGTDKVKLSTPAANGRMRTDERVFEGVIPNLERRYRETDSSAVREELGR 399
Cdd:TIGR00630 322 MFASLAEHLGFDLDTPWKDLPEEAQKAILYGSGEEVIVVKYRNGGGETFRYHKPFEGVIPELERRYLETESESMREYLEK 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  400 YLAEQPCPDCHGTRLNSAARHVFVNDMTLPEVTHMSVANAQAFFSDLQLPGRFAQIAEKIVREISSRLGFLNDVGLDYLT 479
Cdd:TIGR00630 402 FMSERPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFNQLTLTPEEKKIAEEVLKEIRERLGFLIDVGLDYLS 481
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  480 LDRSADTLSGGEAQRIRLASQIGSALVGVMYILDEPSIGLHQRDNARLLNTLSHLRDLGNTVIVVEHDEDAIRQADYVVD 559
Cdd:TIGR00630 482 LSRAAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVID 561
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  560 IGPGAGRHGGQIVASGTPEAVTQHPDSLTGAYLRGTRCIPVPEHRIEPDPdREIRVIGARGNNLKGGDFAFPTGLFTCVT 639
Cdd:TIGR00630 562 IGPGAGEHGGEVVASGTPEEILANPDSLTGQYLSGRKKIEVPAERRPGNG-KFLTLKGARENNLKNITVSIPLGLFTCIT 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  640 GVSGSGKSTLVNNTLYPAVATELHGGRHHIEEHERIDGLELIDKVVDIDQSPIGRTPRSNPATYTGLFTPIRELFAATAE 719
Cdd:TIGR00630 641 GVSGSGKSTLINDTLYPALANRLNGAKTVPGRYTSIEGLEHLDKVIHIDQSPIGRTPRSNPATYTGVFDEIRELFAETPE 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  720 ARSRGYKPGRFSFNVRGGRCEACQGDGVIKVEMHFLPDVFVPCDVCKGHRYNRETLEVRYKGKNVHEVLEMTVEEALDFF 799
Cdd:TIGR00630 721 AKVRGYTPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEAYEFF 800
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  800 QPVPVIHRKLEMLMEVGLSYIQLGQNATTLSGGEAQRIKLARELSKRDTGRTLYILDEPTTGLHFEDIAQLLRVLHRLRD 879
Cdd:TIGR00630 801 EAVPSISRKLQTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKRSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVD 880
                         890       900       910       920
                  ....*....|....*....|....*....|....*....|....*
gi 648489723  880 HGNTIVVIEHNLDVIKTADWLIDIGPEGGSGGGELLVAGTPEAVA 924
Cdd:TIGR00630 881 KGNTVVVIEHNLDVIKTADYIIDLGPEGGDGGGTVVASGTPEEVA 925
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
613-920 1.98e-151

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: 447.45  E-value: 1.98e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 613 IRVIGARGNNLKGGDFAFPTGLFTCVTGVSGSGKSTLVNNTLYPAVATELHGGRHHIEEHERIDGLELIDKVVDIDQSPI 692
Cdd:cd03271    1 LTLKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPALARRLHLKKEQPGNHDRIEGLEHIDKVIVIDQSPI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 693 GRTPRSNPATYTGLFTPIRELFaataearsrgykpgrfsfnvrggrceacqgdgvikvemhflpdvfvpCDVCKGHRYNR 772
Cdd:cd03271   81 GRTPRSNPATYTGVFDEIRELF-----------------------------------------------CEVCKGKRYNR 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 773 ETLEVRYKGKNVHEVLEMTVEEALDFFQPVPVIHRKLEMLMEVGLSYIQLGQNATTLSGGEAQRIKLARELSKRDTGRTL 852
Cdd:cd03271  114 ETLEVRYKGKSIADVLDMTVEEALEFFENIPKIARKLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRSTGKTL 193
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648489723 853 YILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHNLDVIKTADWLIDIGPEGGSGGGELLVAGTP 920
Cdd:cd03271  194 YILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLGPEGGDGGGQVVASGTP 261
UvrA_inter pfam17760
UvrA interaction domain; This domain found in UvrA proteins interacts with the UvrB protein.
130-238 1.54e-48

UvrA interaction domain; This domain found in UvrA proteins interacts with the UvrB protein.


Pssm-ID: 436020 [Multi-domain]  Cd Length: 109  Bit Score: 167.27  E-value: 1.54e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  130 QTISQMVDQVLALPEGDKVMLLAPVVRGRKGEHHKMLEAMRSQGYLRARINGEIHDLDALPALDPKRKHNIEIVIDRFRV 209
Cdd:pfam17760   1 QTVDQIVDRILALPEGTKIQILAPVVRGRKGEHKELLDDLRKQGFVRVRVDGEIYDLDDEPKLDKNKKHTIEVVVDRLVV 80
                          90       100
                  ....*....|....*....|....*....
gi 648489723  210 REDLRQRLAESFETATELADGLALVAWMD 238
Cdd:pfam17760  81 KEDNRSRLADSVETALKLGKGLVIVLVLD 109
GguA NF040905
sugar ABC transporter ATP-binding protein;
804-898 9.02e-07

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 52.48  E-value: 9.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 804 VIHRKLEMLMEVGLSyiqlgQNATTLSG----GEAQRIKLARELSKRdtgRTLYILDEPTTGLHFEDIAQLLRVLHRLRD 879
Cdd:NF040905 116 TNRRARELLAKVGLD-----ESPDTLVTdigvGKQQLVEIAKALSKD---VKLLILDEPTAALNEEDSAALLDLLLELKA 187
                         90       100
                 ....*....|....*....|
gi 648489723 880 HGNTIVVIEHNL-DVIKTAD 898
Cdd:NF040905 188 QGITSIIISHKLnEIRRVAD 207
 
Name Accession Description Interval E-value
uvrA PRK00349
excinuclease ABC subunit UvrA;
1-940 0e+00

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 1915.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723   1 MDSISIRGARTHNLKNVDLDLPRERLIVITGVSGSGKSSLAFDTLFAEGQRRYVESLSTYARQFLSMMEKPDVDQIEGLS 80
Cdd:PRK00349   3 MDKIIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  81 PAISIEQKSTSHNPRSTVGTITEIYDYLRLLFARAGEPRCPEHGETLAAQTISQMVDQVLALPEGDKVMLLAPVVRGRKG 160
Cdd:PRK00349  83 PAISIDQKTTSHNPRSTVGTVTEIYDYLRLLYARVGKPHCPNCGRPIEAQTVSQMVDRVLELPEGTRLQILAPVVRGRKG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 161 EHHKMLEAMRSQGYLRARINGEIHDLDALPALDPKRKHNIEIVIDRFRVREDLRQRLAESFETATELADGLALVAWMDEP 240
Cdd:PRK00349 163 EHKKLLENLRKQGFVRVRVDGEVYDLDEPPKLDKNKKHTIEVVVDRLVVKEDIRQRLADSIETALKLSDGLVVVEVMDDP 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 241 EREPMIFSARYACPVCGYALRELEPRLFSFNNPAGACPTCDGLGVRQYFDPERVVSQPALSLGGGAVRGWDRR-NAWYFS 319
Cdd:PRK00349 243 EAEELLFSEKFACPVCGFSIPELEPRLFSFNSPYGACPTCDGLGVKLEFDPDLVVPDPELSLAEGAIAPWSRSsSSYYFQ 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 320 LLTSLARHYGFDVETPWEELPAEVRAVVLHGSGTDKVKLSTPAANGRMRTDERVFEGVIPNLERRYRETDSSAVREELGR 399
Cdd:PRK00349 323 MLKSLAEHYGFDLDTPWKDLPEEVQDIILYGSGDEEIEFRYKNDRGRTRERKHPFEGVIPNLERRYRETESEYVREELEK 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 400 YLAEQPCPDCHGTRLNSAARHVFVNDMTLPEVTHMSVANAQAFFSDLQLPGRFAQIAEKIVREISSRLGFLNDVGLDYLT 479
Cdd:PRK00349 403 YMSERPCPSCKGKRLKPEALAVKVGGKNIGEVSELSIGEALEFFENLKLSEQEAKIAEPILKEIRERLKFLVDVGLDYLT 482
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 480 LDRSADTLSGGEAQRIRLASQIGSALVGVMYILDEPSIGLHQRDNARLLNTLSHLRDLGNTVIVVEHDEDAIRQADYVVD 559
Cdd:PRK00349 483 LSRSAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDEDTIRAADYIVD 562
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 560 IGPGAGRHGGQIVASGTPEAVTQHPDSLTGAYLRGTRCIPVPEHRIePDPDREIRVIGARGNNLKGGDFAFPTGLFTCVT 639
Cdd:PRK00349 563 IGPGAGVHGGEVVASGTPEEIMKNPNSLTGQYLSGKKKIEVPKERR-KGNGKFLKLKGARENNLKNVDVEIPLGKFTCVT 641
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 640 GVSGSGKSTLVNNTLYPAVATELHGGRHHIEEHERIDGLELIDKVVDIDQSPIGRTPRSNPATYTGLFTPIRELFAATAE 719
Cdd:PRK00349 642 GVSGSGKSTLINETLYKALARKLNGAKKVPGKHKEIEGLEHLDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAGTPE 721
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 720 ARSRGYKPGRFSFNVRGGRCEACQGDGVIKVEMHFLPDVFVPCDVCKGHRYNRETLEVRYKGKNVHEVLEMTVEEALDFF 799
Cdd:PRK00349 722 AKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEFF 801
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 800 QPVPVIHRKLEMLMEVGLSYIQLGQNATTLSGGEAQRIKLARELSKRDTGRTLYILDEPTTGLHFEDIAQLLRVLHRLRD 879
Cdd:PRK00349 802 EAIPKIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELSKRSTGKTLYILDEPTTGLHFEDIRKLLEVLHRLVD 881
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648489723 880 HGNTIVVIEHNLDVIKTADWLIDIGPEGGSGGGELLVAGTPEAVAGHPRSHTGRFLAPMLA 940
Cdd:PRK00349 882 KGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVATGTPEEVAKVEASYTGRYLKPVLE 942
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
1-941 0e+00

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 1877.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723   1 MDSISIRGARTHNLKNVDLDLPRERLIVITGVSGSGKSSLAFDTLFAEGQRRYVESLSTYARQFLSMMEKPDVDQIEGLS 80
Cdd:COG0178    3 MDKIRIRGAREHNLKNIDVDIPRNKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  81 PAISIEQKSTSHNPRSTVGTITEIYDYLRLLFARAGEPRCPEHGETLAAQTISQMVDQVLALPEGDKVMLLAPVVRGRKG 160
Cdd:COG0178   83 PAISIEQKTTSRNPRSTVGTVTEIYDYLRLLFARVGTPHCPICGRPVEKQTVDQIVDRILALPEGTRLQILAPVVRGRKG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 161 EHHKMLEAMRSQGYLRARINGEIHDLDALPALDPKRKHNIEIVIDRFRVREDLRQRLAESFETATELADGLALVAWMDEP 240
Cdd:COG0178  163 EHKELLEELRKQGFVRVRVDGEVYDLDEEPELDKNKKHTIEVVVDRLVVKEDIRSRLADSVETALKLGDGLVIVEVVDEG 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 241 ErePMIFSARYACPVCGYALRELEPRLFSFNNPAGACPTCDGLGVRQYFDPERVVSQPALSLGGGAVRGWDRR-NAWYFS 319
Cdd:COG0178  243 E--ELLFSEKFACPDCGISFEELEPRLFSFNSPYGACPTCDGLGRVLEFDPDLVIPDPSLSLAEGAIAPWSGPsSSYYFQ 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 320 LLTSLARHYGFDVETPWEELPAEVRAVVLHGSGtDKVKLSTPAaNGRMRTDERVFEGVIPNLERRYRETDSSAVREELGR 399
Cdd:COG0178  321 LLEALAKHYGFDLDTPWKDLPEEQRDLILYGSD-EKIKFRYKN-RGRRRTYEKPFEGVIPFLERRYRETYSEHVREELSR 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 400 YLAEQPCPDCHGTRLNSAARHVFVNDMTLPEVTHMSVANAQAFFSDLQLPGRFAQIAEKIVREISSRLGFLNDVGLDYLT 479
Cdd:COG0178  399 YMSETPCPACKGARLKPEALAVKIGGKNIAELTALSIDEALEFFENLELTEREAEIAERILKEIRSRLGFLVDVGLDYLT 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 480 LDRSADTLSGGEAQRIRLASQIGSALVGVMYILDEPSIGLHQRDNARLLNTLSHLRDLGNTVIVVEHDEDAIRQADYVVD 559
Cdd:COG0178  479 LDRSAGTLSGGEAQRIRLATQIGSGLVGVLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDTIRAADYIID 558
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 560 IGPGAGRHGGQIVASGTPEAVTQHPDSLTGAYLRGTRCIPVPEHRIEPDpDREIRVIGARGNNLKGGDFAFPTGLFTCVT 639
Cdd:COG0178  559 IGPGAGEHGGEVVAQGTPEEILKNPDSLTGQYLSGRKRIPVPKKRRKGN-GKFLTIKGARENNLKNVDVEIPLGVLTCVT 637
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 640 GVSGSGKSTLVNNTLYPAVATELHGGRHHIEEHERIDGLELIDKVVDIDQSPIGRTPRSNPATYTGLFTPIRELFAATAE 719
Cdd:COG0178  638 GVSGSGKSTLVNDILYPALARKLNGAKEKPGPHDSIEGLEHIDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAQTPE 717
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 720 ARSRGYKPGRFSFNVRGGRCEACQGDGVIKVEMHFLPDVFVPCDVCKGHRYNRETLEVRYKGKNVHEVLEMTVEEALDFF 799
Cdd:COG0178  718 AKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEFF 797
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 800 QPVPVIHRKLEMLMEVGLSYIQLGQNATTLSGGEAQRIKLARELSKRDTGRTLYILDEPTTGLHFEDIAQLLRVLHRLRD 879
Cdd:COG0178  798 ENIPKIARKLQTLQDVGLGYIKLGQPATTLSGGEAQRVKLASELSKRSTGKTLYILDEPTTGLHFHDIRKLLEVLHRLVD 877
                        890       900       910       920       930       940       950
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 648489723 880 HGNTIVVIEHNLDVIKTADWLIDigpeggsgggeL----------LVA-GTPEAVAGHPRSHTGRFLAPMLAA 941
Cdd:COG0178  878 KGNTVVVIEHNLDVIKTADWIID-----------LgpeggdgggeIVAeGTPEEVAKVKASYTGRYLKEYLEA 939
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
4-924 0e+00

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: 1569.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723    4 ISIRGARTHNLKNVDLDLPRERLIVITGVSGSGKSSLAFDTLFAEGQRRYVESLSTYARQFLSMMEKPDVDQIEGLSPAI 83
Cdd:TIGR00630   2 IIVRGAREHNLKNIDVEIPRDKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGVMDKPDVDSIEGLSPAI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723   84 SIEQKSTSHNPRSTVGTITEIYDYLRLLFARAGEPRCPEHGETLAAQTISQMVDQVLALPEGDKVMLLAPVVRGRKGEHH 163
Cdd:TIGR00630  82 SIDQKTTSHNPRSTVGTITEIYDYLRLLFARVGTPYCPTCGRPISRQTPSQIVDQILALPEGTRVILLAPIVRGRKGEFR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  164 KMLEAMRSQGYLRARINGEIHDLDALPALDPKRKHNIEIVIDRFRVREDLRQRLAESFETATELADGLALVAWMDE---P 240
Cdd:TIGR00630 162 KLLEKLRKQGFARVRVDGEVYPLEDPPKLEKNKKHTIDVVIDRLTVKNENRSRLAESVETALRLGDGLLEVEFDDDeevA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  241 EREPMIFSARYACPVCGYALRELEPRLFSFNNPAGACPTCDGLGVRQYFDPERVVSQPALSLGGGAVRGWD-RRNAWYFS 319
Cdd:TIGR00630 242 ESKEELFSEKFACPECGFSLPELEPRLFSFNSPYGACPECSGLGIKQEFDPELIIPDPLLSLNGGAIVPFKkSTTSYYRQ 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  320 LLTSLARHYGFDVETPWEELPAEVRAVVLHGSGTDKVKLSTPAANGRMRTDERVFEGVIPNLERRYRETDSSAVREELGR 399
Cdd:TIGR00630 322 MFASLAEHLGFDLDTPWKDLPEEAQKAILYGSGEEVIVVKYRNGGGETFRYHKPFEGVIPELERRYLETESESMREYLEK 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  400 YLAEQPCPDCHGTRLNSAARHVFVNDMTLPEVTHMSVANAQAFFSDLQLPGRFAQIAEKIVREISSRLGFLNDVGLDYLT 479
Cdd:TIGR00630 402 FMSERPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFNQLTLTPEEKKIAEEVLKEIRERLGFLIDVGLDYLS 481
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  480 LDRSADTLSGGEAQRIRLASQIGSALVGVMYILDEPSIGLHQRDNARLLNTLSHLRDLGNTVIVVEHDEDAIRQADYVVD 559
Cdd:TIGR00630 482 LSRAAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVID 561
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  560 IGPGAGRHGGQIVASGTPEAVTQHPDSLTGAYLRGTRCIPVPEHRIEPDPdREIRVIGARGNNLKGGDFAFPTGLFTCVT 639
Cdd:TIGR00630 562 IGPGAGEHGGEVVASGTPEEILANPDSLTGQYLSGRKKIEVPAERRPGNG-KFLTLKGARENNLKNITVSIPLGLFTCIT 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  640 GVSGSGKSTLVNNTLYPAVATELHGGRHHIEEHERIDGLELIDKVVDIDQSPIGRTPRSNPATYTGLFTPIRELFAATAE 719
Cdd:TIGR00630 641 GVSGSGKSTLINDTLYPALANRLNGAKTVPGRYTSIEGLEHLDKVIHIDQSPIGRTPRSNPATYTGVFDEIRELFAETPE 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  720 ARSRGYKPGRFSFNVRGGRCEACQGDGVIKVEMHFLPDVFVPCDVCKGHRYNRETLEVRYKGKNVHEVLEMTVEEALDFF 799
Cdd:TIGR00630 721 AKVRGYTPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEAYEFF 800
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  800 QPVPVIHRKLEMLMEVGLSYIQLGQNATTLSGGEAQRIKLARELSKRDTGRTLYILDEPTTGLHFEDIAQLLRVLHRLRD 879
Cdd:TIGR00630 801 EAVPSISRKLQTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKRSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVD 880
                         890       900       910       920
                  ....*....|....*....|....*....|....*....|....*
gi 648489723  880 HGNTIVVIEHNLDVIKTADWLIDIGPEGGSGGGELLVAGTPEAVA 924
Cdd:TIGR00630 881 KGNTVVVIEHNLDVIKTADYIIDLGPEGGDGGGTVVASGTPEEVA 925
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
1-942 0e+00

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 653.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723    1 MDSISIR--GARTHNLKNVDLD-LPRErLIVITGVSGSGKSSLAFDTLFAEGQRRYVESLSTYARQFLSMMEKPDVDQIE 77
Cdd:PRK00635    1 MPSLPVRlsGITVRNLKNISIEfCPRE-IVLLTGVSGSGKSSLAFDTIYAAGRKRYLSTLPSFFATTLDSLPDPSVEKIE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723   78 GLSPAISIEQKSTSHNPRSTVGTITEIYDYLRLLFARAGEPRCPEHGETLAAQTISQMVDQVLALPEGDKVMLLAPVVRG 157
Cdd:PRK00635   80 GLSPTIAVKQNHFSQHSHATVGSTTELNSHLALLFSLEGQARDPVTLHPLTLYSKEKILSTIAAIPDGTQITLLAPLPAK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  158 RKGEHHkmlEAMRsQGYLRARINGEIHDLDALPALDPKRKHNIEIVIDRFRVREDLRQRLAESFETATELADGLALVAWm 237
Cdd:PRK00635  160 DILAIR---ECLR-QGFTKVRIDGEISPIYKFLTSGIPEDVPVDIVVDTLIKNESNTARLKVSLFTALDIGHGECSLHF- 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  238 depEREPMIFSARYACPVCGYALRELEPRLFSFNNPAGACPTCDGLGVRQYFDPERVVsQPALSLgggavrgwdRRNA-- 315
Cdd:PRK00635  235 ---DNQKRTFSTQATIPETQQTYTPLTPQLFSPHSLEDRCPQCQGSGIFISIDDPSLI-QQNLSI---------EENCcp 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  316 --------WYFSLLTSLARHYGFDVETPWEELPAEVRAVVLHGsgtdKVKLSTP-----AANGRMRTDERVFEGVIPNLE 382
Cdd:PRK00635  302 fagncstyLYHTIYQSLADSLGFSLSTPWKDLSPEIQNIFLYG----KEGLVLPvrlfdGTLGKKTLTHKVWRGVLNEIG 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  383 RRYRETDSSAvreelgRYLAE----QPCPDCHGTRLNSAARHVFVNDMTLPEVTHMSVANAQAFFSdlQLPGRFAQIAEk 458
Cdd:PRK00635  378 EKVRYSNKPS------RYLPKgtsaTSCPRCQGTGLGDYANAATWHGKTFAEFQQMSLQELFIFLS--QLPSKSLSIEE- 448
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  459 IVREISSRLGFLNDVGLDYLTLDRSADTLSGGEAQRIRLASQIGSALVGVMYILDEPSIGLHQRDNARLLNTLSHLRDLG 538
Cdd:PRK00635  449 VLQGLKSRLSILIDLGLPYLTPERALATLSGGEQERTALAKHLGAELIGITYILDEPSIGLHPQDTHKLINVIKKLRDQG 528
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  539 NTVIVVEHDEDAIRQADYVVDIGPGAGRHGGQIVASGTPEAVTQHPDSLTGAYLRGTRCIPVPEHRiePDPDREIRVIGA 618
Cdd:PRK00635  529 NTVLLVEHDEQMISLADRIIDIGPGAGIFGGEVLFNGSPREFLAKSDSLTAKYLRQELTIPIPEKR--TNSLGTLTLSKA 606
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  619 RGNNLKGGDFAFPTGLFTCVTGVSGSGKSTLVNNTLYPAVATELHGGRhhiEEHERIDGLElIDKVVDIDQSPIGRTPRS 698
Cdd:PRK00635  607 TKHNLKDLTISLPLGRLTVVTGVSGSGKSSLINDTLVPAVEEFIEQGF---CSNLSIQWGA-ISRLVHITRDLPGRSQRS 682
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  699 NPATYTGLFTPIRELFAATAEARSRGYKPGRFSFNVRGGRCEACQGDGVIKVEMHFLPdvfVPCDVCKGHRYNRETLEVR 778
Cdd:PRK00635  683 IPLTYIKAFDDLRELFAEQPRSKRLGLTKSHFSFNTPLGACAECQGLGSITTTDNRTS---IPCPSCLGKRFLPQVLEVR 759
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  779 YKGKNVHEVLEMTVEEALDFFQPVPVIHRKLEMLMEVGLSYIQLGQNATTLSGGEAQRIKLARELSKRDTGRTLYILDEP 858
Cdd:PRK00635  760 YKGKNIADILEMTAYEAEKFFLDEPSIHEKIHALCSLGLDYLPLGRPLSSLSGGEIQRLKLAYELLAPSKKPTLYVLDEP 839
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  859 TTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHNLDVIKTADWLIDIGPEGGSGGGELLVAGTPEAVAgHPRSHTGRFLAPM 938
Cdd:PRK00635  840 TTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLELGPEGGNLGGYLLASCSPEELI-HLHTPTAKALRPY 918

                  ....
gi 648489723  939 LAAP 942
Cdd:PRK00635  919 LSSP 922
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
613-920 1.98e-151

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: 447.45  E-value: 1.98e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 613 IRVIGARGNNLKGGDFAFPTGLFTCVTGVSGSGKSTLVNNTLYPAVATELHGGRHHIEEHERIDGLELIDKVVDIDQSPI 692
Cdd:cd03271    1 LTLKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPALARRLHLKKEQPGNHDRIEGLEHIDKVIVIDQSPI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 693 GRTPRSNPATYTGLFTPIRELFaataearsrgykpgrfsfnvrggrceacqgdgvikvemhflpdvfvpCDVCKGHRYNR 772
Cdd:cd03271   81 GRTPRSNPATYTGVFDEIRELF-----------------------------------------------CEVCKGKRYNR 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 773 ETLEVRYKGKNVHEVLEMTVEEALDFFQPVPVIHRKLEMLMEVGLSYIQLGQNATTLSGGEAQRIKLARELSKRDTGRTL 852
Cdd:cd03271  114 ETLEVRYKGKSIADVLDMTVEEALEFFENIPKIARKLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRSTGKTL 193
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648489723 853 YILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHNLDVIKTADWLIDIGPEGGSGGGELLVAGTP 920
Cdd:cd03271  194 YILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLGPEGGDGGGQVVASGTP 261
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
4-929 1.45e-107

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 366.85  E-value: 1.45e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723    4 ISIRGARTHNLKNVDLDLPRERLIVITGVSGSGKSSLAFDTLFAEGQRRYVESLSTYARQ-FLSMMEKPDVDQIEGLSPA 82
Cdd:PRK00635  941 ITIKNAYQHNLKHIDLSLPRNALTAVTGPSASGKHSLVFDILYAAGNIAYAELFPPYIRQaLIKKTPLPSVDKVTGLSPV 1020
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723   83 ISIEQKSTSHNPRSTVGTITEIYDYLRLLFARAGEPRCPEHGETLAAQTISQMVDQVLALPEGDKVMLLAPVVRGRkgEH 162
Cdd:PRK00635 1021 IAIEKTSASKNSNHSVASALEISNGLEKLFARLGHPYSPLSGDALRKITPQTIAEELLTHYTKGYVTITSPIPKEE--DL 1098
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  163 HKMLEAMRSQGYLRARINGEIHDLDA-LPAL--DPKrkhnieIVIDRFRVREDLRQRLAESFETATELADGLALvawmdE 239
Cdd:PRK00635 1099 FIYLQEKLKEGFLKLYANEQFYDLDEpLPTSleNPA------IVIQHTKISEKNLSSLLSSLTLAFSLSSSICL-----H 1167
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  240 PEREPMIFSARYAC---PVCGYALRELEPRLFSFNNPAGACPTCDGLGVRQYFD----PERVVSQPALSLgggavrgwdr 312
Cdd:PRK00635 1168 IEYAGTSLSLTYRLgwqDSSGNLYPNITTPLLSRDHEEGLCPLCHGKGFILKCSllphKEKIAHYTPLSL---------- 1237
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  313 rnawyFSLLtsLARHYGFDVETPWEELpaevravvlhgsgtdKVKLSTPAANGRMRTDERVFEGVI--PNLERRYRETDS 390
Cdd:PRK00635 1238 -----FTLF--FPNQDPKPVYPLLKEL---------------GIPSIALFQELDTLSFESLCLGTQqhPGLNALLMEAML 1295
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  391 SAVREELGRYL-AEQPCPDCHGTRLNSAARHVFVNDMTLPEVTHMSVANAQAFFSDLQlpgrfAQIAEKIVREISSRLGF 469
Cdd:PRK00635 1296 MESEEPLPPPLiSKTPCNQCQGLGVYTYAHCVRIHNTSLSDIYQEDVTFLKKFLLTIH-----DDEEPSIIQDLLNRLTF 1370
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  470 LNDVGLDYLTLDRSADTLSGGEAQRIRLASQIGSALVGVMYILDEPSIGLHQRDNARLLNTLSHLRDLGNTVIVVEHDED 549
Cdd:PRK00635 1371 IDKVGLSYITLGQEQDTLSDGEHYRLHLAKKISSNLTDIIYLLEDPLSGLHPQDAPTLLQLIKELVTNNNTVIATDRSGS 1450
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  550 AIRQADYVVDIGPGAGRHGGqivasgtpeavtqhpdsltgaYLRGTRCIPVPE---HRI---EPDPDREIRVIGARGNNL 623
Cdd:PRK00635 1451 LAEHADHLIHLGPGSGPQGG---------------------YLLSTSALKQSQpdlHNTrssEETPTLSVSLSIHTIQNL 1509
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  624 KggdFAFPTGLFTCVTGVSGSGKSTLVNNTLYPAVATELHGGRHHIEEheridglelidkVVDIDQSPIGRTPRSNPATY 703
Cdd:PRK00635 1510 N---VSAPLHSLVAISGVSGSGKTSLLLEGFYKQACALIEKGPSVFSE------------IIFLDSHPQISSQRSDISTY 1574
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  704 TGLFTPIRELFAATAEARSRGYKPGRFSFNVRGGRCEACQGDGVIKVEMHFLPDVFVPCDVCKGHRYNRETLEVRYKGKN 783
Cdd:PRK00635 1575 FDIAPSLRNFYASLTQAKALNISASMFSTNTKQGQCSDCWGLGYQWIDRAFYALEKRPCPTCSGFRIQPLAQEVVYEGKH 1654
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  784 VHEVLEMTVEEALDFFQPVPVIHRKLEMLMEVGLSYIQLGQNATTLSGGEAQRIKLARELSKRDTGRTLYILDEPTTGLH 863
Cdd:PRK00635 1655 FGQLLQTPIEEVAETFPFLKKIQKPLQALIDNGLGYLPLGQNLSSLSLSEKIAIKIAKFLYLPPKHPTLFLLDEIATSLD 1734
                         890       900       910       920       930       940
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648489723  864 FEDIAQLLRVLHRLRDHGNTIVVIEHNLDVIKTADWLIDIGPEGGSGGGELLVAGTPEAVAGHPRS 929
Cdd:PRK00635 1735 NQQKSALLVQLRTLVSLGHSVIYIDHDPALLKQADYLIEMGPGSGKTGGKILFSGPPKDISASKDS 1800
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
4-116 3.55e-74

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: 243.32  E-value: 3.55e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723   4 ISIRGARTHNLKNVDLDLPRERLIVITGVSGSGKSSLAFDTLFAEGQRRYVESLSTYARQFLSMMEKPDVDQIEGLSPAI 83
Cdd:cd03270    1 IIVRGAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLSPAI 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 648489723  84 SIEQKSTSHNPRSTVGTITEIYDYLRLLFARAG 116
Cdd:cd03270   81 AIDQKTTSRNPRSTVGTVTEIYDYLRLLFARVG 113
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
463-575 2.51e-68

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: 227.14  E-value: 2.51e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 463 ISSRLGFLNDVGLDYLTLDRSADTLSGGEAQRIRLASQIGSALVGVMYILDEPSIGLHQRDNARLLNTLSHLRDLGNTVI 542
Cdd:cd03270  114 IRERLGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVL 193
                         90       100       110
                 ....*....|....*....|....*....|...
gi 648489723 543 VVEHDEDAIRQADYVVDIGPGAGRHGGQIVASG 575
Cdd:cd03270  194 VVEHDEDTIRAADHVIDIGPGAGVHGGEIVAQG 226
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
406-577 2.07e-49

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: 175.88  E-value: 2.07e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 406 CPDCHGTRLNSAARHVFVNDMTLPEVTHMSVANAQAFFSDlqlpgrFAQIAEKivreissrLGFLNDVGLDYLTLDRSAD 485
Cdd:cd03271  103 CEVCKGKRYNRETLEVRYKGKSIADVLDMTVEEALEFFEN------IPKIARK--------LQTLCDVGLGYIKLGQPAT 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 486 TLSGGEAQRIRLASQIGSALVG-VMYILDEPSIGLHQRDNARLLNTLSHLRDLGNTVIVVEHDEDAIRQADYVVDIGPGA 564
Cdd:cd03271  169 TLSGGEAQRIKLAKELSKRSTGkTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLGPEG 248
                        170
                 ....*....|...
gi 648489723 565 GRHGGQIVASGTP 577
Cdd:cd03271  249 GDGGGQVVASGTP 261
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
608-936 7.31e-49

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 187.93  E-value: 7.31e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 608 DPDREIRVIGARGNNLKGGDFAFPTGLFTCVTGVSGSGKSTLVNNTLYpAvatElhGGRHHIE----------------E 671
Cdd:COG0178    1 MMMDKIRIRGAREHNLKNIDVDIPRNKLVVITGLSGSGKSSLAFDTIY-A---E--GQRRYVEslsayarqflgqmdkpD 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 672 HERIDGLElidKVVDIDQSPIGRTPRSNPATYTG-------LF------------------TP------IRELFAAT--- 717
Cdd:COG0178   75 VDSIEGLS---PAISIEQKTTSRNPRSTVGTVTEiydylrlLFarvgtphcpicgrpvekqTVdqivdrILALPEGTrlq 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 718 -----------------AEARSRGY-----------------------------------KPG---R------------- 729
Cdd:COG0178  152 ilapvvrgrkgehkellEELRKQGFvrvrvdgevydldeepeldknkkhtievvvdrlvvKEDirsRladsvetalklgd 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 730 ------------------------------------FSFNVRGGRCEACQG---------------------DGVIKV-- 750
Cdd:COG0178  232 glvivevvdegeellfsekfacpdcgisfeeleprlFSFNSPYGACPTCDGlgrvlefdpdlvipdpslslaEGAIAPws 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 751 ----------------EMHF--------LPD------------------------------------------------- 757
Cdd:COG0178  312 gpsssyyfqllealakHYGFdldtpwkdLPEeqrdlilygsdekikfryknrgrrrtyekpfegvipflerryretyseh 391
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 758 ---------VFVPCDVCKGHRYNRETLEVRYKGKNVHEVLEMTVEEALDFFQPVPV--------------IHRKLEMLME 814
Cdd:COG0178  392 vreelsrymSETPCPACKGARLKPEALAVKIGGKNIAELTALSIDEALEFFENLELtereaeiaerilkeIRSRLGFLVD 471
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 815 VGLSYIQLGQNATTLSGGEAQRIKLARELSKRDTGrTLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHNLDVI 894
Cdd:COG0178  472 VGLDYLTLDRSAGTLSGGEAQRIRLATQIGSGLVG-VLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDTI 550
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|..
gi 648489723 895 KTADWLIDIGPEGGSGGGELLVAGTPEAVAGHPRSHTGRFLA 936
Cdd:COG0178  551 RAADYIIDIGPGAGEHGGEVVAQGTPEEILKNPDSLTGQYLS 592
UvrA_inter pfam17760
UvrA interaction domain; This domain found in UvrA proteins interacts with the UvrB protein.
130-238 1.54e-48

UvrA interaction domain; This domain found in UvrA proteins interacts with the UvrB protein.


Pssm-ID: 436020 [Multi-domain]  Cd Length: 109  Bit Score: 167.27  E-value: 1.54e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  130 QTISQMVDQVLALPEGDKVMLLAPVVRGRKGEHHKMLEAMRSQGYLRARINGEIHDLDALPALDPKRKHNIEIVIDRFRV 209
Cdd:pfam17760   1 QTVDQIVDRILALPEGTKIQILAPVVRGRKGEHKELLDDLRKQGFVRVRVDGEIYDLDDEPKLDKNKKHTIEVVVDRLVV 80
                          90       100
                  ....*....|....*....|....*....
gi 648489723  210 REDLRQRLAESFETATELADGLALVAWMD 238
Cdd:pfam17760  81 KEDNRSRLADSVETALKLGKGLVIVLVLD 109
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
465-575 1.17e-46

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: 164.80  E-value: 1.17e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 465 SRLGFLNDVGLDYLTLDRSADTLSGGEAQRIRLASQIGSALVGVMYILDEPSIGLHQRDNARLLNTLSHLRDLGNTVIVV 544
Cdd:cd03238   66 DQLQFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILI 145
                         90       100       110
                 ....*....|....*....|....*....|.
gi 648489723 545 EHDEDAIRQADYVVDIGPGAGRHGGQIVASG 575
Cdd:cd03238  146 EHNLDVLSSADWIIDFGPGSGKSGGKVVFSG 176
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
760-936 2.82e-45

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: 176.74  E-value: 2.82e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  760 VPCDVCKGHRYNRETLEVRYKGKNVHEVLEMTVEEALDFFQPV-----------PV---IHRKLEMLMEVGLSYIQLGQN 825
Cdd:TIGR00630 406 RPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFNQLtltpeekkiaeEVlkeIRERLGFLIDVGLDYLSLSRA 485
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  826 ATTLSGGEAQRIKLARELSKRDTGrTLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHNLDVIKTADWLIDIGP 905
Cdd:TIGR00630 486 AGTLSGGEAQRIRLATQIGSGLTG-VLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVIDIGP 564
                         170       180       190
                  ....*....|....*....|....*....|.
gi 648489723  906 EGGSGGGELLVAGTPEAVAGHPRSHTGRFLA 936
Cdd:TIGR00630 565 GAGEHGGEVVASGTPEEILANPDSLTGQYLS 595
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
613-903 4.58e-45

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: 162.04  E-value: 4.58e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 613 IRVIGARGNNLKGGDFAFPTGLFTCVTGVSGSGKSTLVNNTLYPAvatelhGGRHHIE----------------EHERID 676
Cdd:cd03270    1 IIVRGAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIYAE------GQRRYVEslsayarqflgqmdkpDVDSIE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 677 GLElidKVVDIDQSPIGRTPRSNPATYTGLFTPIRELFAataearsrgykpgrfsfnvRGGrceacqgdgvikvemhflp 756
Cdd:cd03270   75 GLS---PAIAIDQKTTSRNPRSTVGTVTEIYDYLRLLFA-------------------RVG------------------- 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 757 dvfvpcdvckghrynretlevrykgknvhevlemtveealdffqpvpvIHRKLEMLMEVGLSYIQLGQNATTLSGGEAQR 836
Cdd:cd03270  114 ------------------------------------------------IRERLGFLVDVGLGYLTLSRSAPTLSGGEAQR 145
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648489723 837 IKLARELSKRDTGrTLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHNLDVIKTADWLIDI 903
Cdd:cd03270  146 IRLATQIGSGLTG-VLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDI 211
UvrA_DNA-bind pfam17755
UvrA DNA-binding domain;
290-399 1.23e-44

UvrA DNA-binding domain;


Pssm-ID: 465484 [Multi-domain]  Cd Length: 110  Bit Score: 156.48  E-value: 1.23e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  290 DPERVVSQPALSLGGGAVRGWD-RRNAWYFSLLTSLARHYGFDVETPWEELPAEVRAVVLHGSGtDKVKLSTPAANGRMR 368
Cdd:pfam17755   1 DPDLVIPDPSLSLAEGAIAPWGkKRSSYYFQLLEALAKHYGFDLDTPFKDLPEEQQDIILYGSG-EEIIVFYYSRGGRTR 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 648489723  369 TDERVFEGVIPNLERRYRETDSSAVREELGR 399
Cdd:pfam17755  80 TYTKPFEGVIPNLERRYRETDSESVREELEK 110
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
405-901 8.83e-43

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 170.01  E-value: 8.83e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  405 PCPDCHGTRLNSAARHVFVNDMTLPEVTHMSVANAQAFFSDLqlpgrfAQIAEKIVReissrlgfLNDVGLDYLTLDRSA 484
Cdd:PRK00635  742 PCPSCLGKRFLPQVLEVRYKGKNIADILEMTAYEAEKFFLDE------PSIHEKIHA--------LCSLGLDYLPLGRPL 807
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  485 DTLSGGEAQRIRLASQIGSALVG-VMYILDEPSIGLHQRDNARLLNTLSHLRDLGNTVIVVEHDEDAIRQADYVVDIGPG 563
Cdd:PRK00635  808 SSLSGGEIQRLKLAYELLAPSKKpTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLELGPE 887
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  564 AGRHGGQIVASGTPEAVTqHPDSLTG----AYLRGTRCIP-VPEHRIEPDPDREIRVIGARGNNLKGGDFAFPTGLFTCV 638
Cdd:PRK00635  888 GGNLGGYLLASCSPEELI-HLHTPTAkalrPYLSSPQELPyLPDPSPKPPVPADITIKNAYQHNLKHIDLSLPRNALTAV 966
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  639 TGVSGSGKSTLVNNTLY-----------------------------------PAVATELHG----GRHHIEEHERI-DGL 678
Cdd:PRK00635  967 TGPSASGKHSLVFDILYaagniayaelfppyirqalikktplpsvdkvtglsPVIAIEKTSasknSNHSVASALEIsNGL 1046
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  679 ELIDKVVDIDQSPIGRTP--RSNP---------------ATYTGLFTPIRELFAATAEARSRGY---------------- 725
Cdd:PRK00635 1047 EKLFARLGHPYSPLSGDAlrKITPqtiaeellthytkgyVTITSPIPKEEDLFIYLQEKLKEGFlklyaneqfydldepl 1126
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  726 -----------------------------------------------------------KPGR---------FSFNVRGG 737
Cdd:PRK00635 1127 ptslenpaiviqhtkiseknlssllssltlafslsssiclhieyagtslsltyrlgwqdSSGNlypnittplLSRDHEEG 1206
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  738 RCEACQGDGVI----------KVEMH--------FLPDVFV--------------------------------------- 760
Cdd:PRK00635 1207 LCPLCHGKGFIlkcsllphkeKIAHYtplslftlFFPNQDPkpvypllkelgipsialfqeldtlsfeslclgtqqhpgl 1286
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  761 ------------------------PCDVCKGHRYNRETLEVRYKGKNVHEVLEMTVEEALDFF------QPVPVI---HR 807
Cdd:PRK00635 1287 nallmeamlmeseeplppplisktPCNQCQGLGVYTYAHCVRIHNTSLSDIYQEDVTFLKKFLltihddEEPSIIqdlLN 1366
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  808 KLEMLMEVGLSYIQLGQNATTLSGGEAQRIKLARELSkrdTGRT--LYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIV 885
Cdd:PRK00635 1367 RLTFIDKVGLSYITLGQEQDTLSDGEHYRLHLAKKIS---SNLTdiIYLLEDPLSGLHPQDAPTLLQLIKELVTNNNTVI 1443
                         730
                  ....*....|....*.
gi 648489723  886 VIEHNLDVIKTADWLI 901
Cdd:PRK00635 1444 ATDRSGSLAEHADHLI 1459
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
786-903 1.27e-38

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: 141.69  E-value: 1.27e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 786 EVLEMTVEEALDFFQPVPVIH-RKLEMLMEVGLSYIQLGQNATTLSGGEAQRIKLARELSKRdTGRTLYILDEPTTGLHF 864
Cdd:cd03238   44 ASGKARLISFLPKFSRNKLIFiDQLQFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSE-PPGTLFILDEPSTGLHQ 122
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 648489723 865 EDIAQLLRVLHRLRDHGNTIVVIEHNLDVIKTADWLIDI 903
Cdd:cd03238  123 QDINQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDF 161
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
759-945 6.66e-25

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 112.23  E-value: 6.66e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  759 FVPCDVCKGHRYNRETLEVRYKGKNVHEVLEMTVEEALDFFQPVP--------VIH---RKLEMLMEVGLSYIQLGQNAT 827
Cdd:PRK00635  396 ATSCPRCQGTGLGDYANAATWHGKTFAEFQQMSLQELFIFLSQLPskslsieeVLQglkSRLSILIDLGLPYLTPERALA 475
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  828 TLSGGEAQRIKLARELSKRDTGRTlYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHNLDVIKTADWLIDIGPEG 907
Cdd:PRK00635  476 TLSGGEQERTALAKHLGAELIGIT-YILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMISLADRIIDIGPGA 554
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 648489723  908 GSGGGELLVAGTPEAVAGHPRSHTGRFLAPMLAAPTRE 945
Cdd:PRK00635  555 GIFGGEVLFNGSPREFLAKSDSLTAKYLRQELTIPIPE 592
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
453-895 2.47e-21

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: 98.82  E-value: 2.47e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 453 AQIAEKIVREISSR-------LGFLNDVGLDYLtLDRSADTLSGGEAQRIRLASQIgsALVGVMYILDEPSIGLHQRDNA 525
Cdd:COG1123  103 DQIAEALENLGLSRaeararvLELLEAVGLERR-LDRYPHQLSGGQRQRVAIAMAL--ALDPDLLIADEPTTALDVTTQA 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 526 RLLNTLSHL-RDLGNTVIVVEHD-EDAIRQADYVVDIgpgagrHGGQIVASGTPEAVTQHPDSLTGAYLRGTRCIPVPEH 603
Cdd:COG1123  180 EILDLLRELqRERGTTVLLITHDlGVVAEIADRVVVM------DDGRIVEDGPPEEILAAPQALAAVPRLGAARGRAAPA 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 604 RIEPDPDREIR------VIGARGNN--LKGGDFAFPTGLFTCVTGVSGSGKSTLvnntlypavatelhgGRHhieeherI 675
Cdd:COG1123  254 AAAAEPLLEVRnlskryPVRGKGGVraVDDVSLTLRRGETLGLVGESGSGKSTL---------------ARL-------L 311
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 676 DGLELIDK-VVDIDQSPIGRTPRSNpatytglftpIRELfaataeARSRGY---KPGRfSFNVRggrceacqgdgvikve 751
Cdd:COG1123  312 LGLLRPTSgSILFDGKDLTKLSRRS----------LREL------RRRVQMvfqDPYS-SLNPR---------------- 358
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 752 mhflpdvfvpcdvckghrynretlevrykgknvhevleMTVEEALDFfqpVPVIHRKL----------EMLMEVGLSYIQ 821
Cdd:COG1123  359 --------------------------------------MTVGDIIAE---PLRLHGLLsraerrervaELLERVGLPPDL 397
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648489723 822 LGQNATTLSGGEAQRIKLARELSkrdTGRTLYILDEPTTGLhfeDI---AQLLRVLHRLRD-HGNTIVVIEHNLDVIK 895
Cdd:COG1123  398 ADRYPHELSGGQRQRVAIARALA---LEPKLLILDEPTSAL---DVsvqAQILNLLRDLQReLGLTYLFISHDLAVVR 469
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
4-143 4.42e-19

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: 88.06  E-value: 4.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723   4 ISIRGARTHNLKNVDLDLPRERLIVITGVSGSGKSSLAFDTLFAEGQRRYveslstyarqFLSMMEKPDVDQIEGL---S 80
Cdd:cd03271    1 LTLKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPALARRL----------HLKKEQPGNHDRIEGLehiD 70
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648489723  81 PAISIEQKSTSHNPRSTVGTITEIYDYLRLLFarageprCPE-HG-----ETLAAQTISQMVDQVLALP 143
Cdd:cd03271   71 KVIVIDQSPIGRTPRSNPATYTGVFDEIRELF-------CEVcKGkrynrETLEVRYKGKSIADVLDMT 132
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
4-80 7.74e-19

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: 85.07  E-value: 7.74e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648489723   4 ISIRGARTHNLKNVDLDLPRERLIVITGVSGSGKSSLAFDTLFAEGQRRYVESLSTYARQFLSMmekpdVDQIEGLS 80
Cdd:cd03238    1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKARLISFLPKFSRNKLIF-----IDQLQFLI 72
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
456-587 9.96e-18

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: 83.15  E-value: 9.96e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 456 AEKIVREIssrlgfLNDVGLDYLtLDRSADTLSGGEAQRIRLASqigsALVgvM----YILDEPSIGLHQRDNARLLNTL 531
Cdd:COG1122  111 IRERVEEA------LELVGLEHL-ADRPPHELSGGQKQRVAIAG----VLA--MepevLVLDEPTAGLDPRGRRELLELL 177
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 648489723 532 SHLRDLGNTVIVVEHD-EDAIRQADYVVDIgpgagrHGGQIVASGTPEAVTQHPDSL 587
Cdd:COG1122  178 KRLNKEGKTVIIVTHDlDLVAELADRVIVL------DDGRIVADGTPREVFSDYELL 228
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
829-903 1.32e-16

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: 78.06  E-value: 1.32e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648489723 829 LSGGEAQRIKLARELSKRdtgRTLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHNLDVIKTA-DWLIDI 903
Cdd:cd00267   81 LSGGQRQRVALARALLLN---PDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAaDRVIVL 153
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
815-903 1.56e-16

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: 77.79  E-value: 1.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 815 VGLSYIQLGQNATTLSGGEAQRIKLARELSKRDT-GRTLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHNLDV 893
Cdd:cd03227   64 VAAVSAELIFTRLQLSGGEKELSALALILALASLkPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPEL 143
                         90
                 ....*....|
gi 648489723 894 IKTADWLIDI 903
Cdd:cd03227  144 AELADKLIHI 153
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
473-562 1.61e-15

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: 75.09  E-value: 1.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 473 VGLDYLTLDRSADTLSGGEAQRIRLASQIGSALV--GVMYILDEPSIGLHQRDNARLLNTLSHLRDLGNTVIVVEHDEDA 550
Cdd:cd03227   64 VAAVSAELIFTRLQLSGGEKELSALALILALASLkpRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPEL 143
                         90
                 ....*....|..
gi 648489723 551 IRQADYVVDIGP 562
Cdd:cd03227  144 AELADKLIHIKK 155
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
401-594 1.69e-15

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 81.80  E-value: 1.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  401 LAEQPCPDCHGTRLNSAARHVFVNDMTLPEVTHMSVANAQAFFSDLQlpgrfaqiaekivrEISSRLGFLNDVGLDYLTL 480
Cdd:PRK00635 1628 LEKRPCPTCSGFRIQPLAQEVVYEGKHFGQLLQTPIEEVAETFPFLK--------------KIQKPLQALIDNGLGYLPL 1693
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  481 DRSADTLSGGEAQRIRLASQIGSA-LVGVMYILDEPSIGLHQRDNARLLNTLSHLRDLGNTVIVVEHDEDAIRQADYVVD 559
Cdd:PRK00635 1694 GQNLSSLSLSEKIAIKIAKFLYLPpKHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALLKQADYLIE 1773
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 648489723  560 IGPGAGRHGGQIVASGTPEAVTQHPDSLTGAYLRG 594
Cdd:PRK00635 1774 MGPGSGKTGGKILFSGPPKDISASKDSLLKTYMCN 1808
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
461-575 4.89e-15

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: 74.01  E-value: 4.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 461 REISSRLGF----LNDVGLDYLtLDRSADTLSGGEAQRIRLAsqigSALVGV--MYILDEPSIGL---HQrdnARLLNTL 531
Cdd:cd03214   69 KELARKIAYvpqaLELLGLAHL-ADRPFNELSGGERQRVLLA----RALAQEppILLLDEPTSHLdiaHQ---IELLELL 140
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 648489723 532 SHL-RDLGNTVIVVEHDED-AIRQADYVVDIgpgagrHGGQIVASG 575
Cdd:cd03214  141 RRLaRERGKTVVMVLHDLNlAARYADRVILL------KDGRIVAQG 180
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
623-901 8.35e-15

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: 74.49  E-value: 8.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 623 LKGGDFAFPTGLFTCVTGVSGSGKSTLVnntlypavatelhggrhhieeheridglelidKVVdidqspigrtprsnpat 702
Cdd:cd03235   15 LEDVSFEVKPGEFLAIVGPNGAGKSTLL--------------------------------KAI----------------- 45
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 703 yTGLFTPIR---ELFAATAEARSR--GYKPGRFSFNVRggrceacqgdgvikvemhFLPDVFvpcDVCKGHRYNRETLEV 777
Cdd:cd03235   46 -LGLLKPTSgsiRVFGKPLEKERKriGYVPQRRSIDRD------------------FPISVR---DVVLMGLYGHKGLFR 103
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 778 RYKGKNVHEVlemtvEEALDFfqpvpvihrklemlmeVGLSYI---QLGQnattLSGGEAQRIKLARELSKRdtgRTLYI 854
Cdd:cd03235  104 RLSKADKAKV-----DEALER----------------VGLSELadrQIGE----LSGGQQQRVLLARALVQD---PDLLL 155
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 648489723 855 LDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHNLD-VIKTADWLI 901
Cdd:cd03235  156 LDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGlVLEYFDRVL 203
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
456-558 2.48e-14

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: 72.88  E-value: 2.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 456 AEKIVREIssrlgfLNDVGLDYLtLDRSADTLSGGEAQRIRLASQIgsalvgVM----YILDEPSIGLHQRDNARLLNTL 531
Cdd:cd03225  111 IEERVEEA------LELVGLEGL-RDRSPFTLSGGQKQRVAIAGVL------AMdpdiLLLDEPTAGLDPAGRRELLELL 177
                         90       100
                 ....*....|....*....|....*...
gi 648489723 532 SHLRDLGNTVIVVEHD-EDAIRQADYVV 558
Cdd:cd03225  178 KKLKAEGKTIIIVTHDlDLLLELADRVI 205
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
804-901 9.21e-14

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: 71.34  E-value: 9.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 804 VIHRKLEMLMEVGLSyIQLGQNATTLSGGEAQRIKLARELSkrdTGRTLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNT 883
Cdd:cd03225  111 IEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLA---MDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKT 186
                         90
                 ....*....|....*....
gi 648489723 884 IVVIEHNLDVIKT-ADWLI 901
Cdd:cd03225  187 IIIVTHDLDLLLElADRVI 205
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
784-901 1.21e-13

ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 71.66  E-value: 1.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 784 VHEVLEMTVEEALDFFQPVPVIHRK--LEMLMEVGLSYI---QLGQnattLSGGEAQRIKLAREL-SKRDtgrtLYILDE 857
Cdd:COG1121   94 VRDVVLMGRYGRRGLFRRPSRADREavDEALERVGLEDLadrPIGE----LSGGQQQRVLLARALaQDPD----LLLLDE 165
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 648489723 858 PTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHNLD-VIKTADWLI 901
Cdd:COG1121  166 PFAGVDAATEEALYELLRELRREGKTILVVTHDLGaVREYFDRVL 210
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
456-589 1.77e-13

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 71.97  E-value: 1.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 456 AEKIVREIssrlgfLNDVGLDYLTLDRSADTLSGGEAQRIrlasqigsALVGV------MYILDEPSIGLHQRDNARLLN 529
Cdd:PRK13634 121 AKQKAREM------IELVGLPEELLARSPFELSGGQMRRV--------AIAGVlamepeVLVLDEPTAGLDPKGRKEMME 186
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648489723 530 TLSHL-RDLGNTVIVVEHD-EDAIRQADYVVDIgpgagrHGGQIVASGTPEAVTQHPDSLTG 589
Cdd:PRK13634 187 MFYKLhKEKGLTTVLVTHSmEDAARYADQIVVM------HKGTVFLQGTPREIFADPDELEA 242
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
767-901 2.47e-13

ABC-type multidrug transport system, ATPase component [Defense mechanisms];


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 70.48  E-value: 2.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 767 GHRYNRETLEVRYK------GKNVHEvlEMTVEEALDFFQ-----PVPVIHRKLEMLME-VGLSyIQLGQNATTLSGGEA 834
Cdd:COG1131   61 GEDVARDPAEVRRRigyvpqEPALYP--DLTVRENLRFFArlyglPRKEARERIDELLElFGLT-DAADRKVGTLSGGMK 137
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648489723 835 QRIKLARELSKR-DtgrtLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHNLDVI-KTADWLI 901
Cdd:COG1131  138 QRLGLALALLHDpE----LLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAeRLCDRVA 202
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
789-895 4.24e-13

ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 69.07  E-value: 4.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 789 EMTVEEALDF----FQPVPVIHRKLEMLMEVGLSYIQLGQNATTLSGGEAQRIKLARELSkrdTGRTLYILDEPTTGL-- 862
Cdd:COG4619   87 GGTVRDNLPFpfqlRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALL---LQPDVLLLDEPTSALdp 163
                         90       100       110
                 ....*....|....*....|....*....|....
gi 648489723 863 -HFEDIAQLLRvlHRLRDHGNTIVVIEHNLDVIK 895
Cdd:COG4619  164 eNTRRVEELLR--EYLAEEGRAVLWVSHDPEQIE 195
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
821-903 5.61e-13

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: 72.48  E-value: 5.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 821 QLGQNATTLSGGEAQRIKLARELSKrdtGRTLYILDEPTTGLHFEDIAQLLRVLHRLRdHGNTIVVIEHNLDVIKTADWL 900
Cdd:COG4988  466 PLGEGGRGLSGGQAQRLALARALLR---DAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQADRI 541

                 ...
gi 648489723 901 IDI 903
Cdd:COG4988  542 LVL 544
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
487-563 7.64e-13

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: 67.27  E-value: 7.64e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648489723 487 LSGGEAQRIRLASQIGSAlvGVMYILDEPSIGLHQRDNARLLNTLSHLRDLGNTVIVVEHD-EDAIRQADYVVDIGPG 563
Cdd:cd00267   81 LSGGQRQRVALARALLLN--PDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDpELAELAADRVIVLKDG 156
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
442-585 1.41e-12

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: 68.23  E-value: 1.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 442 FFSDLQLPGRFAQIAEKiVREIssrlgfLNDVGLDYLtLDRSADTLSGGEAQRIrlasQIGSALVG--VMYILDEPSIGL 519
Cdd:cd03219  107 GLLLARARREEREARER-AEEL------LERVGLADL-ADRPAGELSYGQQRRL----EIARALATdpKLLLLDEPAAGL 174
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648489723 520 HQRDNARLLNTLSHLRDLGNTVIVVEHDEDAIRQ-ADYVVDIgpgagrHGGQIVASGTPEAVTQHPD 585
Cdd:cd03219  175 NPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVL------DQGRVIAEGTPDEVRNNPR 235
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
433-586 6.24e-12

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: 66.59  E-value: 6.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 433 HMSVANAQAFFSDLQLPGRfAQIAEKiVREISSRLGflndvgLDYLtLDRSADTLSGGEAQRIRLAsqigSALV--GVMY 510
Cdd:cd03299   85 HMTVYKNIAYGLKKRKVDK-KEIERK-VLEIAEMLG------IDHL-LNRKPETLSGGEQQRVAIA----RALVvnPKIL 151
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648489723 511 ILDEPSIGLHQRDNARLLNTLSHLRD-LGNTVIVVEHD-EDAIRQADYVVDIgpgagrHGGQIVASGTPEAVTQHPDS 586
Cdd:cd03299  152 LLDEPFSALDVRTKEKLREELKKIRKeFGVTVLHVTHDfEEAWALADKVAIM------LNGKLIQVGKPEEVFKKPKN 223
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
446-589 8.04e-12

Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 66.58  E-value: 8.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 446 LQLPGRFAQIAEKIVREIssrlgfLNDVGLDYLTlDRSADTLSGGEAQRIRLASQIGSALVGVMyiLDEPSIGL---HQr 522
Cdd:PRK11231 105 LSLWGRLSAEDNARVNQA------MEQTRINHLA-DRRLTDLSGGQRQRAFLAMVLAQDTPVVL--LDEPTTYLdinHQ- 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 523 dnARLLNTLSHLRDLGNTVIVVEHD-EDAIRQADYVVDIgpgagrHGGQIVASGTPEAVTQ--------------HPDSL 587
Cdd:PRK11231 175 --VELMRLMRELNTQGKTVVTVLHDlNQASRYCDHLVVL------ANGHVMAQGTPEEVMTpgllrtvfdveaeiHPEPV 246

                 ..
gi 648489723 588 TG 589
Cdd:PRK11231 247 SG 248
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
474-583 9.24e-12

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: 68.63  E-value: 9.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 474 GLDYLTLDRSAdTLSGGEAQRIRLA------SQIgsalvgvmYILDEPSIGLHQRDNARLLNTLSHLRDlGNTVIVVEHD 547
Cdd:COG4988  462 GLDTPLGEGGR-GLSGGQAQRLALArallrdAPL--------LLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHR 531
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 648489723 548 EDAIRQADYVVDIgpgagrHGGQIVASGTPEAVTQH 583
Cdd:COG4988  532 LALLAQADRILVL------DDGRIVEQGTHEELLAK 561
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
810-901 1.79e-11

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: 65.05  E-value: 1.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 810 EMLMEVGLSYIqLGQNATTLSGGEAQRIKLARELSkrdTGRTLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEH 889
Cdd:COG1122  117 EALELVGLEHL-ADRPPHELSGGQKQRVAIAGVLA---MEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTH 192
                         90
                 ....*....|...
gi 648489723 890 NLD-VIKTADWLI 901
Cdd:COG1122  193 DLDlVAELADRVI 205
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
814-892 5.11e-11

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: 62.45  E-value: 5.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 814 EVGLSYIqLGQNATTLSGGEAQRIKLARELSkRDTgrTLYILDEPTTGLhfeDIAQLLRVLHRLRD----HGNTIVVIEH 889
Cdd:cd03214   84 LLGLAHL-ADRPFNELSGGERQRVLLARALA-QEP--PILLLDEPTSHL---DIAHQIELLELLRRlareRGKTVVMVLH 156

                 ...
gi 648489723 890 NLD 892
Cdd:cd03214  157 DLN 159
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
829-898 5.43e-11

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: 62.06  E-value: 5.43e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648489723 829 LSGGEAQRIKLARELSkrdTGRTLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHNLD-VIKTAD 898
Cdd:cd03216   83 LSVGERQMVEIARALA---RNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDeVFEIAD 150
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
809-894 6.97e-11

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: 63.22  E-value: 6.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 809 LEMLMEVGLSYIqLGQNATTLSGGEAQRIKLARELSkrdTGRTLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIE 888
Cdd:cd03219  125 EELLERVGLADL-ADRPAGELSYGQQRRLEIARALA---TDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVE 200

                 ....*.
gi 648489723 889 HNLDVI 894
Cdd:cd03219  201 HDMDVV 206
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
829-901 7.11e-11

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: 61.63  E-value: 7.11e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648489723 829 LSGGEAQRIKLARELSKRdtgRTLYILDEPTTGLhfeDI---AQLLRVLHRLRDhGNTIVVIEHNLDVIKTADWLI 901
Cdd:cd03228   97 LSGGQRQRIAIARALLRD---PPILILDEATSAL---DPeteALILEALRALAK-GKTVIVIAHRLSTIRDADRII 165
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
807-895 9.48e-11

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: 62.91  E-value: 9.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 807 RKLEMLMEVGLSYIQLGQNATTLSGGEAQRIKLARELSKR-DtgrtLYILDEPTTGLhfeDI---AQLLRVLHRLRD-HG 881
Cdd:cd03257  124 AVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNpK----LLIADEPTSAL---DVsvqAQILDLLKKLQEeLG 196
                         90
                 ....*....|....
gi 648489723 882 NTIVVIEHNLDVIK 895
Cdd:cd03257  197 LTLLFITHDLGVVA 210
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
456-584 1.36e-10

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: 64.92  E-value: 1.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 456 AEKIVREIssrlgfLNDVGLDYLTLDRSADTLSGGEAQRIRLAsqigSALVG---VMyILDEPSIGLHQRDNARLLNTLS 532
Cdd:COG1123  380 RRERVAEL------LERVGLPPDLADRYPHELSGGQRQRVAIA----RALALepkLL-ILDEPTSALDVSVQAQILNLLR 448
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 648489723 533 HLRD-LGNTVIVVEHDEDAIRQ-ADYVVDIgpgagrHGGQIVASGTPEAVTQHP 584
Cdd:COG1123  449 DLQReLGLTYLFISHDLAVVRYiADRVAVM------YDGRIVEDGPTEEVFANP 496
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
445-604 1.59e-10

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 62.64  E-value: 1.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 445 DLQLP-GRFAQIAEKIVREISSRLGfLNDvgldylTLDRSADTLSGGEAQRIRLAS---QIGSAL--VGVMYILDEPSIG 518
Cdd:PRK03695  91 TLHQPdKTRTEAVASALNEVAEALG-LDD------KLGRSVNQLSGGEWQRVRLAAvvlQVWPDInpAGQLLLLDEPMNS 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 519 LHQRDNARLLNTLSHLRDLGNTVIVVEHD-EDAIRQADYVVDIgpgagrHGGQIVASGTPEAVTQhPDSLTGAYLRGTRC 597
Cdd:PRK03695 164 LDVAQQAALDRLLSELCQQGIAVVMSSHDlNHTLRHADRVWLL------KQGKLLASGRRDEVLT-PENLAQVFGVNFRR 236

                 ....*..
gi 648489723 598 IPVPEHR 604
Cdd:PRK03695 237 LDVEGHP 243
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
442-582 1.85e-10

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: 62.18  E-value: 1.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 442 FFSDLQlpGRFAQIAEKIVREISSRLGFLNDvgldyltLDRSADTLSGGEAQRIRLASqigsALVG---VmYILDEPSIG 518
Cdd:COG4555   97 YFAELY--GLFDEELKKRIEELIELLGLEEF-------LDRRVGELSTGMKKKVALAR----ALVHdpkV-LLLDEPTNG 162
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648489723 519 L---HQRDnarLLNTLSHLRDLGNTVIVVEHD-EDAIRQADYVVDIgpgagrHGGQIVASGTPEAVTQ 582
Cdd:COG4555  163 LdvmARRL---LREILRALKKEGKTVLFSSHImQEVEALCDRVVIL------HKGKVVAQGSLDELRE 221
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
446-563 2.11e-10

ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 61.37  E-value: 2.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 446 LQLPGRFAQiaEKIVREISSRLgfLNDVGLDYLTLDRSADTLSGGEAQRIRLASQIgsALVGVMYILDEPSIGLHQrDNA 525
Cdd:COG4619   94 LPFPFQLRE--RKFDRERALEL--LERLGLPPDILDKPVERLSGGERQRLALIRAL--LLQPDVLLLDEPTSALDP-ENT 166
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 648489723 526 RLLNTL--SHLRDLGNTVIVVEHDEDAIRQ-ADYVVDIGPG 563
Cdd:COG4619  167 RRVEELlrEYLAEEGRAVLWVSHDPEQIERvADRVLTLEAG 207
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
829-903 3.00e-10

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: 59.92  E-value: 3.00e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648489723 829 LSGGEAQRIKLARELSKRdtgRTLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHNLDVIKTADWLIDI 903
Cdd:cd03246   97 LSGGQRQRLGLARALYGN---PRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVL 168
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
473-591 3.69e-10

Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 61.73  E-value: 3.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 473 VGLDYLTlDRSADTLSGGEAQRIRLA---SQIGSALvgvmyILDEPSIGL---HQRDNARLLNTLSHLRDLgnTVIVVEH 546
Cdd:PRK10575 135 VGLKPLA-HRLVDSLSGGERQRAWIAmlvAQDSRCL-----LLDEPTSALdiaHQVDVLALVHRLSQERGL--TVIAVLH 206
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 648489723 547 DED-AIRQADYVVDIgpgagrHGGQIVASGTPEAVTQhPDSLTGAY 591
Cdd:PRK10575 207 DINmAARYCDYLVAL------RGGEMIAQGTPAELMR-GETLEQIY 245
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
458-894 3.89e-10

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 63.65  E-value: 3.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 458 KIVREISSRLGflndvgLDYLtLDRSADTLSGGEAQRIrlasQIGSALV--GVMYILDEPSIGL--HQRDN-ARLLNTLS 532
Cdd:COG1245  191 GKLDELAEKLG------LENI-LDRDISELSGGELQRV----AIAAALLrdADFYFFDEPSSYLdiYQRLNvARLIRELA 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 533 hlrDLGNTVIVVEHD---EDAIrqADYVVdigpgagrhggqiVASGTPEA--VTQHPDSL-TG--AYLRGTrcipVPEH- 603
Cdd:COG1245  260 ---EEGKYVLVVEHDlaiLDYL--ADYVH-------------ILYGEPGVygVVSKPKSVrVGinQYLDGY----LPEEn 317
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 604 -RIEPDPdreIRvigargnnlkggdfafptglFTCVTGVSGSGKSTLVNntlYPAVATEL-------HGGRHHIEEheri 675
Cdd:COG1245  318 vRIRDEP---IE--------------------FEVHAPRREKEEETLVE---YPDLTKSYggfslevEGGEIREGE---- 367
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 676 dglelidkVVDI-DQSPIGRTprsnpatytglfTPIReLFAataearsrgykpgrfsfnvrggrceacqgdGVIKvemhf 754
Cdd:COG1245  368 --------VLGIvGPNGIGKT------------TFAK-ILA------------------------------GVLK----- 391
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 755 lPDvfvpcdvcKGhrYNRETLEVRYKGKNVHEVLEMTVEEALD----------FFQPVPVIHRKLEMLMEvglsyiqlgQ 824
Cdd:COG1245  392 -PD--------EG--EVDEDLKISYKPQYISPDYDGTVEEFLRsantddfgssYYKTEIIKPLGLEKLLD---------K 451
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648489723 825 NATTLSGGEAQRIKLARELSKR-DtgrtLYILDEPTTGLHFEDIAQLLRVLHRL-RDHGNTIVVIEHNLDVI 894
Cdd:COG1245  452 NVKDLSGGELQRVAIAACLSRDaD----LYLLDEPSAHLDVEQRLAVAKAIRRFaENRGKTAMVVDHDIYLI 519
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
452-609 4.26e-10

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 62.18  E-value: 4.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 452 FAQIAEKIVREISSRLG--FLNDVGLDYLTLDRSADTLSGGEAQRIRLASQIgsALVGVMYILDEPSIGLHQRDNARLLN 529
Cdd:PRK13631 140 FGPVALGVKKSEAKKLAkfYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGIL--AIQPEILIFDEPTAGLDPKGEHEMMQ 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 530 TLSHLRDLGNTVIVVEHD-EDAIRQADYVVDIGPgagrhgGQIVASGTPEAVTQHPDSLTGAYLRGTRCIPVPEHRIEPD 608
Cdd:PRK13631 218 LILDAKANNKTVFVITHTmEHVLEVADEVIVMDK------GKILKTGTPYEIFTDQHIINSTSIQVPRVIQVINDLIKKD 291

                 .
gi 648489723 609 P 609
Cdd:PRK13631 292 P 292
cbiO PRK13637
energy-coupling factor transporter ATPase;
462-587 5.45e-10

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 61.60  E-value: 5.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 462 EISSRL-GFLNDVGLDYLTL-DRSADTLSGGEAQRIRLASQIgsALVGVMYILDEPSIGLHQRDNARLLNTLSHLRD-LG 538
Cdd:PRK13637 118 EIENRVkRAMNIVGLDYEDYkDKSPFELSGGQKRRVAIAGVV--AMEPKILILDEPTAGLDPKGRDEILNKIKELHKeYN 195
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 648489723 539 NTVIVVEHD-EDAIRQADYVVDIgpgagrHGGQIVASGTPEAVTQHPDSL 587
Cdd:PRK13637 196 MTIILVSHSmEDVAKLADRIIVM------NKGKCELQGTPREVFKEVETL 239
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
470-547 5.79e-10

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: 60.24  E-value: 5.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 470 LNDVGLDYLtLDRSADTLSGGEAQRIRLASqigsALVG--VMYILDEPSIGL---HQRDNARLLNtlsHLRDLGNTVIVV 544
Cdd:cd03235  117 LERVGLSEL-ADRQIGELSGGQQQRVLLAR----ALVQdpDLLLLDEPFAGVdpkTQEDIYELLR---ELRREGMTILVV 188

                 ...
gi 648489723 545 EHD 547
Cdd:cd03235  189 THD 191
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
480-582 6.04e-10

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: 60.14  E-value: 6.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 480 LDRSADTLSGGEAQriRLAsqIGSALVG--VMYILDEPSIGLHQRDNARLLNTLSHLRDLGNTVIVVEHDEDAIRQ-AD- 555
Cdd:cd03224  126 RKQLAGTLSGGEQQ--MLA--IARALMSrpKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEiADr 201
                         90       100
                 ....*....|....*....|....*...
gi 648489723 556 -YVVDigpgagrhGGQIVASGTPEAVTQ 582
Cdd:cd03224  202 aYVLE--------RGRVVLEGTAAELLA 221
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
470-591 7.39e-10

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 60.56  E-value: 7.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 470 LNDVGLDYLTlDRSADTLSGGEAQRIRLA---------SQIGSALvgvmyILDEPSIGL---HQRDNARLLNTLSHLRdl 537
Cdd:PRK13548 119 LAQVDLAHLA-GRDYPQLSGGEQQRVQLArvlaqlwepDGPPRWL-----LLDEPTSALdlaHQHHVLRLARQLAHER-- 190
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 648489723 538 GNTVIVVEHDED-AIRQADYVVDIgpgagrHGGQIVASGTPEAVTQhPDSLTGAY 591
Cdd:PRK13548 191 GLAVIVVLHDLNlAARYADRIVLL------HQGRLVADGTPAEVLT-PETLRRVY 238
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
776-889 7.82e-10

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: 59.80  E-value: 7.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 776 EVRYKGKNVHEVL------------------EMTVEEALDFFQ---PVPVIHRKLEMLME-VGLSYIqLGQNATTLSGGE 833
Cdd:COG4133   58 EVLWNGEPIRDARedyrrrlaylghadglkpELTVRENLRFWAalyGLRADREAIDEALEaVGLAGL-ADLPVRQLSAGQ 136
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 648489723 834 AQRIKLARELSkrdTGRTLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEH 889
Cdd:COG4133  137 KRRVALARLLL---SPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
790-898 9.49e-10

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: 60.26  E-value: 9.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 790 MTVEEALDFF---QPVPV--IHRKLEMLME-VGLSYIqLGQNATTLSGGEAQRIKLARELSKRdtgRTLYILDEPTTGLH 863
Cdd:COG4555   89 LTVRENIRYFaelYGLFDeeLKKRIEELIElLGLEEF-LDRRVGELSTGMKKKVALARALVHD---PKVLLLDEPTNGLD 164
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 648489723 864 FEDIAQLLRVLHRLRDHGNTIVVIEHNLDVI-KTAD 898
Cdd:COG4555  165 VMARRLLREILRALKKEGKTVLFSSHIMQEVeALCD 200
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
480-587 2.64e-09

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 59.26  E-value: 2.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 480 LDRSADTLSGGEAQRIRLASQIgsALVGVMYILDEPSIGLHQRDNARLLNTLSHLRDLGN-TVIVVEHDEDAIRQADYVV 558
Cdd:PRK13635 134 LNREPHRLSGGQKQRVAIAGVL--ALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQADRVI 211
                         90       100
                 ....*....|....*....|....*....
gi 648489723 559 DIgpgagrHGGQIVASGTPEAVTQHPDSL 587
Cdd:PRK13635 212 VM------NKGEILEEGTPEEIFKSGHML 234
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
823-891 2.90e-09

ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 58.97  E-value: 2.90e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648489723 823 GQNATTLSGGEAQRIKLAREL-----SKRDTGRTLyILDEPTTGLhfeDIA---QLLRVLHRLRDHGNTIVVIEHNL 891
Cdd:COG4559  128 GRSYQTLSGGEQQRVQLARVLaqlwePVDGGPRWL-FLDEPTSAL---DLAhqhAVLRLARQLARRGGGVVAVLHDL 200
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
441-587 3.40e-09

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: 58.28  E-value: 3.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 441 AFFSDL------QLPGR-FAQIAEKIVREISsrLGFLNDVGLDYlTLDRSADTLSGGEAQRIRLASQIgsALVGVMYILD 513
Cdd:cd03261   87 ALFDSLtvfenvAFPLReHTRLSEEEIREIV--LEKLEAVGLRG-AEDLYPAELSGGMKKRVALARAL--ALDPELLLYD 161
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648489723 514 EPSIGLHQRDNARLLNTLSHLRD-LGNTVIVVEHDEDAIRQ-ADYVVDIgpgagrHGGQIVASGTPEAVTQHPDSL 587
Cdd:cd03261  162 EPTAGLDPIASGVIDDLIRSLKKeLGLTSIMVTHDLDTAFAiADRIAVL------YDGKIVAEGTPEELRASDDPL 231
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
821-900 3.99e-09

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: 60.15  E-value: 3.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 821 QLGQNATTLSGGEAQRIKLArelskrdtgRTLY------ILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHNLDVI 894
Cdd:COG4618  460 RIGEGGARLSGGQRQRIGLA---------RALYgdprlvVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLL 530

                 ....*.
gi 648489723 895 KTADWL 900
Cdd:COG4618  531 AAVDKL 536
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
822-898 4.25e-09

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: 60.16  E-value: 4.25e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648489723 822 LGQNATTLSGGEAQRIKLARELSKRdtgRTLYILDEPTTGLhfeDIAQLLRVLHRLRDH--GNTIVVIEHNLDVIKTAD 898
Cdd:COG4987  465 LGEGGRRLSGGERRRLALARALLRD---APILLLDEPTEGL---DAATEQALLADLLEAlaGRTVLLITHRLAGLERMD 537
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
789-892 5.40e-09

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: 57.44  E-value: 5.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 789 EMTVEEALD---FFQPVPVIHRKLEM-------LMEvglsyiQLGQNATTLSGGEAQRIKLARELSKRdtgRTLYILDEP 858
Cdd:cd03224   89 ELTVEENLLlgaYARRRAKRKARLERvyelfprLKE------RRKQLAGTLSGGEQQMLAIARALMSR---PKLLLLDEP 159
                         90       100       110
                 ....*....|....*....|....*....|....
gi 648489723 859 TTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHNLD 892
Cdd:cd03224  160 SEGLAPKIVEEIFEAIRELRDEGVTILLVEQNAR 193
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
776-901 5.56e-09

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: 57.27  E-value: 5.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 776 EVRYKGKNVHEVLEmTVEEALDFFqpvpvihrKLEMLMEvglsyiqlgQNATTLSGGEAQRIKLARELSkrdTGRTLYIL 855
Cdd:cd03226   92 ELLLGLKELDAGNE-QAETVLKDL--------DLYALKE---------RHPLSLSGGQKQRLAIAAALL---SGKDLLIF 150
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 648489723 856 DEPTTGL---HFEDIAQLLRvlhRLRDHGNTIVVIEHNLDVI-KTADWLI 901
Cdd:cd03226  151 DEPTSGLdykNMERVGELIR---ELAAQGKAVIVITHDYEFLaKVCDRVL 197
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
829-901 5.99e-09

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: 56.25  E-value: 5.99e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648489723 829 LSGGEAQRIKLARELSKRdtgRTLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHNLDVI-KTADWLI 901
Cdd:cd03230   96 LSGGMKQRLALAQALLHD---PELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAeRLCDRVA 166
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
821-901 6.41e-09

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: 59.85  E-value: 6.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 821 QLGQNATTLSGGEAQRIKLARELSKRdtgRTLYILDEPTTGLHFEDIAQLLRVLHRLRdHGNTIVVIEHNLDVIKTADWL 900
Cdd:COG2274  604 VVGEGGSNLSGGQRQRLAIARALLRN---PRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIRLADRI 679

                 .
gi 648489723 901 I 901
Cdd:COG2274  680 I 680
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
458-894 6.57e-09

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 59.44  E-value: 6.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 458 KIVREISSRLGFLNdvgldylTLDRSADTLSGGEAQRIRLAsqigSALV--GVMYILDEPS----IGlhQRDN-ARLlnt 530
Cdd:PRK13409 191 GKLDEVVERLGLEN-------ILDRDISELSGGELQRVAIA----AALLrdADFYFFDEPTsyldIR--QRLNvARL--- 254
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 531 lshLRDL--GNTVIVVEHD---EDAIrqADYVVdigpgagrhggqiVASGTPEA--VTQHPDSL-TG--AYLRGTrcipV 600
Cdd:PRK13409 255 ---IRELaeGKYVLVVEHDlavLDYL--ADNVH-------------IAYGEPGAygVVSKPKGVrVGinEYLKGY----L 312
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 601 PEH--RIEPDPDR-EIRVigargnnlkggdfafPTglftcvtgvSGSGKSTLVNntlYPAVATELHGGRHHIEEHErIDG 677
Cdd:PRK13409 313 PEEnmRIRPEPIEfEERP---------------PR---------DESERETLVE---YPDLTKKLGDFSLEVEGGE-IYE 364
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 678 LELIDKVvdidqSP--IGRTprsnpatytglfTPIReLFAataearsrgykpgrfsfnvrggrceacqgdGVIKvemhfl 755
Cdd:PRK13409 365 GEVIGIV-----GPngIGKT------------TFAK-LLA------------------------------GVLK------ 390
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 756 PD---VFvpcdvckghrynrETLEVRYKGKNVHEVLEMTVEEALD---------FFQPvPVIHR-KLEMLMEvglsyiql 822
Cdd:PRK13409 391 PDegeVD-------------PELKISYKPQYIKPDYDGTVEDLLRsitddlgssYYKS-EIIKPlQLERLLD-------- 448
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648489723 823 gQNATTLSGGEAQRIKLARELSKR-DtgrtLYILDEPTTGLHFEDIAQLLRVLHRL-RDHGNTIVVIEHNLDVI 894
Cdd:PRK13409 449 -KNVKDLSGGELQRVAIAACLSRDaD----LYLLDEPSAHLDVEQRLAVAKAIRRIaEEREATALVVDHDIYMI 517
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
810-901 6.71e-09

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: 57.50  E-value: 6.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 810 EMLMEVGLSYIQ-LGQNATTLSGGEAQRIKLARELSKRDtgrTLYILDEPTTGLHFEDIAQLLRVLHRLRDhGNTIVVIE 888
Cdd:cd03252  119 DFISELPEGYDTiVGEQGAGLSGGQRQRIAIARALIHNP---RILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIA 194
                         90
                 ....*....|...
gi 648489723 889 HNLDVIKTADWLI 901
Cdd:cd03252  195 HRLSTVKNADRII 207
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
807-898 6.73e-09

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: 57.11  E-value: 6.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 807 RKLEMLMEVGLSYIqLGQNATTLSGGEAQRIKLARELSKRdtgRTLYILDEPTTGL---HFEDIAQLLRVLHrlRDHGNT 883
Cdd:cd03255  120 RAEELLERVGLGDR-LNHYPSELSGGQQQRVAIARALAND---PKIILADEPTGNLdseTGKEVMELLRELN--KEAGTT 193
                         90
                 ....*....|....*
gi 648489723 884 IVVIEHNLDVIKTAD 898
Cdd:cd03255  194 IVVVTHDPELAEYAD 208
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
787-895 8.17e-09

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 59.17  E-value: 8.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 787 VLEMTVEEALdFF--QPVP--------VIHRKLEMLMEVGLSyIQLGQNATTLSGGEAQRIKLARELSKRdtgRTLYILD 856
Cdd:PRK13549  94 VKELSVLENI-FLgnEITPggimdydaMYLRAQKLLAQLKLD-INPATPVGNLGLGQQQLVEIAKALNKQ---ARLLILD 168
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 648489723 857 EPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHNLDVIK 895
Cdd:PRK13549 169 EPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVK 207
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
810-895 1.12e-08

Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 56.60  E-value: 1.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 810 EMLMEVGLSYiQLGQNATTLSGGEAQRIKLARELSKRDtgrTLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEH 889
Cdd:COG2884  120 EVLDLVGLSD-KAKALPHELSGGEQQRVAIARALVNRP---ELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATH 195

                 ....*.
gi 648489723 890 NLDVIK 895
Cdd:COG2884  196 DLELVD 201
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
433-587 1.14e-08

ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 58.19  E-value: 1.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 433 HMSVANAQAFFsdLQLPGRFAQIAEKIVREIssrlgfLNDVGLDYLtLDRSADTLSGGEAQRIRLAsqigSALV---GVM 509
Cdd:COG3842   91 HLTVAENVAFG--LRMRGVPKAEIRARVAEL------LELVGLEGL-ADRYPHQLSGGQQQRVALA----RALApepRVL 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 510 yILDEPsiglhqrdnarllntLSHL----------------RDLGNTVIVVEHD-EDAIRQADYVVDIgpgagrHGGQIV 572
Cdd:COG3842  158 -LLDEP---------------LSALdaklreemreelrrlqRELGITFIYVTHDqEEALALADRIAVM------NDGRIE 215
                        170
                 ....*....|....*
gi 648489723 573 ASGTPEAVTQHPDSL 587
Cdd:COG3842  216 QVGTPEEIYERPATR 230
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
808-903 1.27e-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: 56.99  E-value: 1.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 808 KLEMLMEV-GLSYIqLGQNATTLSGGEAQRIKLARELSkRDTgrTLYILDEPTTGLhfeDIAQLL---RVLHRLRDHGNT 883
Cdd:cd03236  119 KLDELVDQlELRHV-LDRNIDQLSGGELQRVAIAAALA-RDA--DFYFFDEPSSYL---DIKQRLnaaRLIRELAEDDNY 191
                         90       100
                 ....*....|....*....|
gi 648489723 884 IVVIEHNLDVIktaDWLIDI 903
Cdd:cd03236  192 VLVVEHDLAVL---DYLSDY 208
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
433-575 1.40e-08

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: 55.99  E-value: 1.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 433 HMSVANAQAFFSDLQLPGRfAQIAEKiVREISSRLGFLNDvgldyltLDRSADTLSGGEAQRIRLAsqigSALV---GVM 509
Cdd:cd03259   86 HLTVAENIAFGLKLRGVPK-AEIRAR-VRELLELVGLEGL-------LNRYPHELSGGQQQRVALA----RALArepSLL 152
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648489723 510 yILDEPSIGLHQRDNARLLNTLSHL-RDLGNTVIVVEHD-EDAIRQADYVVDIgpgagrHGGQIVASG 575
Cdd:cd03259  153 -LLDEPLSALDAKLREELREELKELqRELGITTIYVTHDqEEALALADRIAVM------NEGRIVQVG 213
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
821-903 1.69e-08

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: 58.07  E-value: 1.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  821 QLGQNATTLSGGEAQRIKLARELSKrdtGRTLYILDEPTTGLHFEDIAQLLRVLHRLRDhGNTIVVIEHNLDVIKTADWL 900
Cdd:TIGR02857 451 PIGEGGAGLSGGQAQRLALARAFLR---DAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAALADRI 526

                  ...
gi 648489723  901 IDI 903
Cdd:TIGR02857 527 VVL 529
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
779-903 1.75e-08

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 58.28  E-value: 1.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 779 YKGKnVHEVLEMTVEE-ALDffqpvpvihrklEMLMEVGLSYIqLGQNATTLSGGEAQRIKLARELSkRDTgrTLYILDE 857
Cdd:PRK13409 176 FKGK-VRELLKKVDERgKLD------------EVVERLGLENI-LDRDISELSGGELQRVAIAAALL-RDA--DFYFFDE 238
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 648489723 858 PTTGLhfeDIAQLLRVLHRLRD--HGNTIVVIEHNLDVIktaDWLIDI 903
Cdd:PRK13409 239 PTSYL---DIRQRLNVARLIRElaEGKYVLVVEHDLAVL---DYLADN 280
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
433-590 1.99e-08

ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 57.08  E-value: 1.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 433 HMSVANAQAFFSDLQLPGRfAQIAEKiVREissrlgFLNDVGLDYLTlDRSADTLSGGEAQRIRLAsqigSALV---GVM 509
Cdd:COG1118   89 HMTVAENIAFGLRVRPPSK-AEIRAR-VEE------LLELVQLEGLA-DRYPSQLSGGQRQRVALA----RALAvepEVL 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 510 yILDEPSIGL--HQRDNARLLntLSHL-RDLGNTVIVVEHD-EDAIRQADYVVDIgpgagrHGGQIVASGTPEAVTQHPD 585
Cdd:COG1118  156 -LLDEPFGALdaKVRKELRRW--LRRLhDELGGTTVFVTHDqEEALELADRVVVM------NQGRIEQVGTPDEVYDRPA 226

                 ....*
gi 648489723 586 SLTGA 590
Cdd:COG1118  227 TPFVA 231
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
807-892 2.17e-08

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 56.13  E-value: 2.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 807 RKLEMLMEVGLSYIQLGQNATTLSGGEAQRIKLARELSKRDTgrtLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVV 886
Cdd:PRK10619 131 RAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPE---VLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVV 207

                 ....*.
gi 648489723 887 IEHNLD 892
Cdd:PRK10619 208 VTHEMG 213
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
487-606 2.58e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 56.24  E-value: 2.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 487 LSGGEAQRIRLASQIgsALVGVMYILDEPSIGLHQRDNARLLNTLSHLRDLGNTVIVVEHDEDAI-RQADYVVDIGpgag 565
Cdd:PRK13639 138 LSGGQKKRVAIAGIL--AMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVpVYADKVYVMS---- 211
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 648489723 566 rhGGQIVASGTPEAVTQHPDSLTGAYLRgtrcIPVPEHRIE 606
Cdd:PRK13639 212 --DGKIIKEGTPKEVFSDIETIRKANLR----LPRVAHLIE 246
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
441-606 3.13e-08

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: 55.48  E-value: 3.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 441 AFFSDLQLPGRFAQIAEKIVREIssrlgfLNDVGLDYLtLDRSADTLSGGEAQRIrlasQIGSALVG--VMYILDEPSIG 518
Cdd:COG1119  104 GFFDSIGLYREPTDEQRERAREL------LELLGLAHL-ADRPFGTLSQGEQRRV----LIARALVKdpELLILDEPTAG 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 519 L--HQRdnARLLNTLSHLRDLGNTVIV-VEHdedairqadYVVDIGPGAGRH----GGQIVASGTPEAVtqhpdsLTGAY 591
Cdd:COG1119  173 LdlGAR--ELLLALLDKLAAEGAPTLVlVTH---------HVEEIPPGITHVlllkDGRVVAAGPKEEV------LTSEN 235
                        170
                 ....*....|....*
gi 648489723 592 LRGTRCIPVPEHRIE 606
Cdd:COG1119  236 LSEAFGLPVEVERRD 250
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
777-938 3.19e-08

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: 55.49  E-value: 3.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 777 VRYKGKNVHEVLEMTVEEAL---------------DFFQPVpvihrKLEMLMEvglsyiqlgQNATTLSGGEAQRIKLAR 841
Cdd:cd03237   63 VSYKPQYIKADYEGTVRDLLssitkdfythpyfktEIAKPL-----QIEQILD---------REVPELSGGELQRVAIAA 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 842 ELSKrDTgrTLYILDEPTTGLHFEDIAQLLRVLHRLRDHGN-TIVVIEHnlDVIkTADWLIDIGPEGGSGGGELLVAGTP 920
Cdd:cd03237  129 CLSK-DA--DIYLLDEPSAYLDVEQRLMASKVIRRFAENNEkTAFVVEH--DII-MIDYLADRLIVFEGEPSVNGVANPP 202
                        170
                 ....*....|....*...
gi 648489723 921 EAVaghpRSHTGRFLAPM 938
Cdd:cd03237  203 QSL----RSGMNRFLKNL 216
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
821-901 3.98e-08

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: 55.24  E-value: 3.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 821 QLGQNATTLSGGEAQRIKLARELSKRDtgrTLYILDEPTTGLHFEDIAQLLRVLHRLRDhGNTIVVIEHNLDVIKTADWL 900
Cdd:cd03249  132 LVGERGSQLSGGQKQRIAIARALLRNP---KILLLDEATSALDAESEKLVQEALDRAMK-GRTTIVIAHRLSTIRNADLI 207

                 .
gi 648489723 901 I 901
Cdd:cd03249  208 A 208
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
474-583 4.13e-08

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: 57.15  E-value: 4.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 474 GLDYLTLDRSAdTLSGGEAQRIRLAsqigSALVG--VMYILDEPSIGLHQRDNARLLNTLSHLRDlGNTVIVVEHDEDAI 551
Cdd:COG2274  600 GYDTVVGEGGS-NLSGGQRQRLAIA----RALLRnpRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTI 673
                         90       100       110
                 ....*....|....*....|....*....|..
gi 648489723 552 RQADYVVDIgpgagrHGGQIVASGTPEAVTQH 583
Cdd:COG2274  674 RLADRIIVL------DKGRIVEDGTHEELLAR 699
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
433-587 4.67e-08

ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 56.23  E-value: 4.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 433 HMSVANAQAFfsDLQLPGRFAQIAEKIVREISSRLGflndvgLDYLtLDRSADTLSGGEAQRIrlAsqIGSALV---GVm 509
Cdd:COG3839   89 HMTVYENIAF--PLKLRKVPKAEIDRRVREAAELLG------LEDL-LDRKPKQLSGGQRQRV--A--LGRALVrepKV- 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 510 YILDEPsiglhqrdnarllntLSHL----------------RDLGNTVIVVEHD-EDAIRQADYVVDIgpgagrHGGQIV 572
Cdd:COG3839  155 FLLDEP---------------LSNLdaklrvemraeikrlhRRLGTTTIYVTHDqVEAMTLADRIAVM------NDGRIQ 213
                        170
                 ....*....|....*
gi 648489723 573 ASGTPEAVTQHPDSL 587
Cdd:COG3839  214 QVGTPEELYDRPANL 228
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
481-618 4.73e-08

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 56.39  E-value: 4.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 481 DRSADTLSGGEAQRIRLASQIGSAlvGVMYILDEPSIGLHQRDNARLLNTLSHLRDLGNTVIVVEHDED-AIRQADYVVD 559
Cdd:PRK09536 134 DRPVTSLSGGERQRVLLARALAQA--TPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVL 211
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648489723 560 IGpgagrhGGQIVASGTPEAVTQhPDSLTGAY----LRGTRCI-------PVP-EHRIEPDPDREIRVIGA 618
Cdd:PRK09536 212 LA------DGRVRAAGPPADVLT-ADTLRAAFdartAVGTDPAtgaptvtPLPdPDRTEAAADTRVHVVGG 275
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
433-586 5.03e-08

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: 55.04  E-value: 5.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 433 HMSVANAQAFfsDLQLPGRFAQIAEKIVREISSRLgfLNDVGLDYLTlDRSADTLSGGEAQRIRLASQIgsALVGVMYIL 512
Cdd:cd03296   88 HMTVFDNVAF--GLRVKPRSERPPEAEIRAKVHEL--LKLVQLDWLA-DRYPAQLSGGQRQRVALARAL--AVEPKVLLL 160
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648489723 513 DEPSIGLHQRDNARLLNTLSHLRD-LGNTVIVVEHD-EDAIRQADYVVDIgpgagrHGGQIVASGTPEAVTQHPDS 586
Cdd:cd03296  161 DEPFGALDAKVRKELRRWLRRLHDeLHVTTVFVTHDqEEALEVADRVVVM------NKGRIEQVGTPDEVYDHPAS 230
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
810-891 5.23e-08

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 55.16  E-value: 5.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 810 EMLMEVGLSyiQLGQNA-TTLSGGEAQRIKLAR---ELSKRDTGRTLYILDEPTTGLhfeDIAQ---LLRVLHRL-RDHG 881
Cdd:PRK13548 117 AALAQVDLA--HLAGRDyPQLSGGEQQRVQLARvlaQLWEPDGPPRWLLLDEPTSAL---DLAHqhhVLRLARQLaHERG 191
                         90
                 ....*....|
gi 648489723 882 NTIVVIEHNL 891
Cdd:PRK13548 192 LAVIVVLHDL 201
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
829-887 5.79e-08

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: 53.59  E-value: 5.79e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 648489723 829 LSGGEAQRIKLARELSkrdTGRTLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVI 887
Cdd:cd03215  105 LSGGNQQKVVLARWLA---RDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLI 160
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
789-892 6.61e-08

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 56.18  E-value: 6.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 789 EMTVEEALdFF--QPV--PVIHRK------LEMLMEVGLSyIQLGQNATTLSGGEAQRIKLARELSKRdtGRTLyILDEP 858
Cdd:COG1129   93 NLSVAENI-FLgrEPRrgGLIDWRamrrraRELLARLGLD-IDPDTPVGDLSVAQQQLVEIARALSRD--ARVL-ILDEP 167
                         90       100       110
                 ....*....|....*....|....*....|....
gi 648489723 859 TTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHNLD 892
Cdd:COG1129  168 TASLTEREVERLFRIIRRLKAQGVAIIYISHRLD 201
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
778-902 8.36e-08

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: 8.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 778 RYKGKnVHEVLEMTVEEAldffqpvpvihrKLEMLME-VGLSYIqLGQNATTLSGGEAQRIKLARELSkRDTgrTLYILD 856
Cdd:COG1245  175 VFKGT-VRELLEKVDERG------------KLDELAEkLGLENI-LDRDISELSGGELQRVAIAAALL-RDA--DFYFFD 237
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 648489723 857 EPTTGLhfeDIAQLL---RVLHRLRDHGNTIVVIEHNLDVIktaDWLID 902
Cdd:COG1245  238 EPSSYL---DIYQRLnvaRLIRELAEEGKYVLVVEHDLAIL---DYLAD 280
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
486-580 8.75e-08

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: 55.91  E-value: 8.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 486 TLSGGEAQRIRLAsqigSALVG--VMYILDEPSIGLHQRDNARLLNTLSHLRDLGNTVIVVEHDEDAIRQADYVVDIgpg 563
Cdd:COG4618  467 RLSGGQRQRIGLA----RALYGdpRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAVDKLLVL--- 539
                         90
                 ....*....|....*..
gi 648489723 564 agrHGGQIVASGTPEAV 580
Cdd:COG4618  540 ---RDGRVQAFGPRDEV 553
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
467-566 1.08e-07

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 53.56  E-value: 1.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 467 LGFLNDVGLDYLTLDRSADTLSGGEAQRIRLASQIgSALVGVMyILDEPSIGLHQrDNARLLNTLSH--LRDLGNTVIVV 544
Cdd:PRK10247 118 LDDLERFALPDTILTKNIAELSGGEKQRISLIRNL-QFMPKVL-LLDEITSALDE-SNKHNVNEIIHryVREQNIAVLWV 194
                         90       100
                 ....*....|....*....|..
gi 648489723 545 EHDEDAIRQADYVVDIGPGAGR 566
Cdd:PRK10247 195 THDKDEINHADKVITLQPHAGE 216
cbiO PRK13643
energy-coupling factor transporter ATPase;
456-587 1.45e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 53.97  E-value: 1.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 456 AEKIVREIssrlgfLNDVGLDYLTLDRSADTLSGGEAQRIRLASQIgsALVGVMYILDEPSIGLHQRDNARLLNTLSHLR 535
Cdd:PRK13643 120 AEKIAAEK------LEMVGLADEFWEKSPFELSGGQMRRVAIAGIL--AMEPEVLVLDEPTAGLDPKARIEMMQLFESIH 191
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 648489723 536 DLGNTVIVVEH-DEDAIRQADYVVDIgpgagrHGGQIVASGTPEAVTQHPDSL 587
Cdd:PRK13643 192 QSGQTVVLVTHlMDDVADYADYVYLL------EKGHIISCGTPSDVFQEVDFL 238
cbiO PRK13649
energy-coupling factor transporter ATPase;
456-587 1.47e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 53.98  E-value: 1.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 456 AEKIVREIssrlgfLNDVGLDYLTLDRSADTLSGGEAQRIRLASQIgsALVGVMYILDEPSIGLHQRDNARLLNTLSHLR 535
Cdd:PRK13649 121 AEALAREK------LALVGISESLFEKNPFELSGGQMRRVAIAGIL--AMEPKILVLDEPTAGLDPKGRKELMTLFKKLH 192
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 648489723 536 DLGNTVIVVEH-DEDAIRQADYVVDIgpgagrHGGQIVASGTPEAVTQHPDSL 587
Cdd:PRK13649 193 QSGMTIVLVTHlMDDVANYADFVYVL------EKGKLVLSGKPKDIFQDVDFL 239
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
487-588 1.68e-07

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 55.12  E-value: 1.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 487 LSGGEAQRIRLASqigsALV--GVMYILDEPSIGLHQRDNARLLNTLSHLRDLGNTVIVVEHDEDAIRQADYVVDIgpga 564
Cdd:PRK10535 145 LSGGQQQRVSIAR----ALMngGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEI---- 216
                         90       100
                 ....*....|....*....|....*..
gi 648489723 565 grHGGQIVASGTPE---AVTQHPDSLT 588
Cdd:PRK10535 217 --RDGEIVRNPPAQekvNVAGGTEPVV 241
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
821-901 1.79e-07

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: 53.10  E-value: 1.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 821 QLGQNATTLSGGEAQRIKLARELSKRDTgrtLYILDEPTTGL--HFEDIAQLLRVLHRLRDHGNTIVVIEHNLDVIKTAD 898
Cdd:cd03290  133 EIGERGINLSGGQRQRICVARALYQNTN---IVFLDDPFSALdiHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPHAD 209

                 ...
gi 648489723 899 WLI 901
Cdd:cd03290  210 WII 212
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
470-584 2.02e-07

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: 53.07  E-value: 2.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 470 LNDVGLDYLTL-DRSADTLSGGEAQRIRLASQIgsALVGVMYILDEPSIGLHQRDNARLLNTLSHL-RDLGNTVIVVEHD 547
Cdd:cd03295  118 LALVGLDPAEFaDRYPHELSGGQQQRVGVARAL--AADPPLLLMDEPFGALDPITRDQLQEEFKRLqQELGKTIVFVTHD 195
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 648489723 548 -EDAIRQADYVVDIgpgagrHGGQIVASGTPEAVTQHP 584
Cdd:cd03295  196 iDEAFRLADRIAIM------KNGEIVQVGTPDEILRSP 227
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
821-901 2.07e-07

ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 54.79  E-value: 2.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 821 QLGQNATTLSGGEAQRIKLARELSKRdtgRTLYILDEPTTGLHFEDIAQLLRVLHRLRdHGNTIVVIEHNLDVIKTADWL 900
Cdd:COG1132  469 VVGERGVNLSGGQRQRIAIARALLKD---PPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLSTIRNADRI 544

                 .
gi 648489723 901 I 901
Cdd:COG1132  545 L 545
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
448-571 2.19e-07

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: 52.49  E-value: 2.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 448 LPGRFAQIAEKIVREISSRLgfLNDVGLDYLtLDRSADTLSGGEAQRIRLASqigsALVG-VMYIL-DEPSIGLHQRDNA 525
Cdd:cd03255  105 LPLLLAGVPKKERRERAEEL--LERVGLGDR-LNHYPSELSGGQQQRVAIAR----ALANdPKIILaDEPTGNLDSETGK 177
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 648489723 526 RLLNTLSHL-RDLGNTVIVVEHDEDAIRQADYVVDIgpgagrHGGQI 571
Cdd:cd03255  178 EVMELLRELnKEAGTTIVVVTHDPELAEYADRIIEL------RDGKI 218
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
789-898 2.21e-07

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: 52.60  E-value: 2.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 789 EMTVEEALDFFQPVPVIHRKL--EMLMEVGLSYIQlGQNATTLSGGEAQRIKLARE-LSKRDtgrtLYILDEPTTGLHFE 865
Cdd:cd03268   86 NLTARENLRLLARLLGIRKKRidEVLDVVGLKDSA-KKKVKGFSLGMKQRLGIALAlLGNPD----LLILDEPTNGLDPD 160
                         90       100       110
                 ....*....|....*....|....*....|....
gi 648489723 866 DIAQLLRVLHRLRDHGNTIVVIEHNL-DVIKTAD 898
Cdd:cd03268  161 GIKELRELILSLRDQGITVLISSHLLsEIQKVAD 194
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
473-549 2.28e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 53.55  E-value: 2.28e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648489723 473 VGLDYLTLDRSADTLSGGEAQRIRLASQIgsALVGVMYILDEPSIGLHQRDNARLLNTLSHLRDLGNTVIVVEHDED 549
Cdd:PRK13651 152 VGLDESYLQRSPFELSGGQKRRVALAGIL--AMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLD 226
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
769-898 2.39e-07

high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 52.96  E-value: 2.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 769 RYNRETLEVRYKGKNVHEvlEMTVEEAL---DFFQPVPVIHRKLEMLMEVGLS-YIQLGQNATTLSGGEAQRIKLARELS 844
Cdd:PRK11614  76 KIMREAVAIVPEGRRVFS--RMTVEENLamgGFFAERDQFQERIKWVYELFPRlHERRIQRAGTMSGGEQQMLAIGRALM 153
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 648489723 845 KRDTgrtLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHNLD-VIKTAD 898
Cdd:PRK11614 154 SQPR---LLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANqALKLAD 205
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
807-903 3.01e-07

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 54.34  E-value: 3.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 807 RKLEMLMEVGLS---YIQLGQnattLSGGEAQRIKLARELSkrdTGRTLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNT 883
Cdd:PRK10535 124 RAQELLQRLGLEdrvEYQPSQ----LSGGQQQRVSIARALM---NGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHT 196
                         90       100
                 ....*....|....*....|
gi 648489723 884 IVVIEHNLDVIKTADWLIDI 903
Cdd:PRK10535 197 VIIVTHDPQVAAQAERVIEI 216
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
433-587 4.57e-07

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: 51.85  E-value: 4.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 433 HMSVANAQAFfsdlqlPGRFAQIAEKIVREISSRLgfLNDVGLDYLtLDRSADTLSGGEAQRIRLAsqigSALV---GVM 509
Cdd:cd03300   86 HLTVFENIAF------GLRLKKLPKAEIKERVAEA--LDLVQLEGY-ANRKPSQLSGGQQQRVAIA----RALVnepKVL 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 510 yILDEPSIGLHQRDNARLLNTLSHL-RDLGNTVIVVEHD-EDAIRQADYVVDIgpgagrHGGQIVASGTPEAVTQHPDSL 587
Cdd:cd03300  153 -LLDEPLGALDLKLRKDMQLELKRLqKELGITFVFVTHDqEEALTMSDRIAVM------NKGKIQQIGTPEEIYEEPANR 225
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
790-898 4.96e-07

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: 52.75  E-value: 4.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 790 MTV----EEALDFFQPVP---VIHRKLEMLMEVGLSYIQ--LGQNATTLSGGEAQRIKLARELSkrdTGRTLYILDEPTT 860
Cdd:COG0444  103 MTVgdqiAEPLRIHGGLSkaeARERAIELLERVGLPDPErrLDRYPHELSGGMRQRVMIARALA---LEPKLLIADEPTT 179
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 648489723 861 GLhfeDI---AQLLRVLHRL-RDHGNTIVVIEHNLDVIK-TAD 898
Cdd:COG0444  180 AL---DVtiqAQILNLLKDLqRELGLAILFITHDLGVVAeIAD 219
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
805-894 5.10e-07

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: 52.01  E-value: 5.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 805 IHRKLEMLMEVGLSYIqLGQNATTLSGGEAQRIKLARELSKRDTgrtLYILDEPTTGLHFEDIAQLLRVLHRLRDHGN-T 883
Cdd:COG1119  120 RERARELLELLGLAHL-ADRPFGTLSQGEQRRVLIARALVKDPE---LLILDEPTAGLDLGARELLLALLDKLAAEGApT 195
                         90
                 ....*....|.
gi 648489723 884 IVVIEHNLDVI 894
Cdd:COG1119  196 LVLVTHHVEEI 206
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
822-923 5.25e-07

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 51.86  E-value: 5.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 822 LGQNATTLSGGEAQRIKLA-------RELSKRdtGRTLyILDEPTTGLhfeDIAQ---LLRVLHRLRDHGNTIVVIEHNL 891
Cdd:PRK03695 120 LGRSVNQLSGGEWQRVRLAavvlqvwPDINPA--GQLL-LLDEPMNSL---DVAQqaaLDRLLSELCQQGIAVVMSSHDL 193
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 648489723 892 D-VIKTAD--WLIdigpeggsGGGELLVAGTPEAV 923
Cdd:PRK03695 194 NhTLRHADrvWLL--------KQGKLLASGRRDEV 220
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
480-560 5.69e-07

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: 51.98  E-value: 5.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 480 LDRSADTLSGGEAQRIRLASQIgsALVGVMYILDEPS--IGLHQRDN-ARLLNTLShlrDLGNTVIVVEHDEDAIrqaDY 556
Cdd:cd03236  133 LDRNIDQLSGGELQRVAIAAAL--ARDADFYFFDEPSsyLDIKQRLNaARLIRELA---EDDNYVLVVEHDLAVL---DY 204

                 ....
gi 648489723 557 VVDI 560
Cdd:cd03236  205 LSDY 208
cbiO PRK13644
energy-coupling factor transporter ATPase;
791-927 6.81e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 51.91  E-value: 6.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 791 TVEEALDF------FQPVPVIHRKLEMLMEVGLSYIQLgQNATTLSGGEAQRIKLARELSKRDTgrtLYILDEPTTGLHF 864
Cdd:PRK13644  94 TVEEDLAFgpenlcLPPIEIRKRVDRALAEIGLEKYRH-RSPKTLSGGQGQCVALAGILTMEPE---CLIFDEVTSMLDP 169
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 648489723 865 EDIAQLLRVLHRLRDHGNTIVVIEHNLDVIKTADWLIdigpegGSGGGELLVAGTPEAVAGHP 927
Cdd:PRK13644 170 DSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRII------VMDRGKIVLEGEPENVLSDV 226
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
813-898 6.90e-07

lipid A ABC transporter ATP-binding protein/permease MsbA;


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 53.10  E-value: 6.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 813 MEVGLSYIqLGQNATTLSGGEAQRIKLARELsKRDTgrTLYILDEPTTGLHFED---IAQLLRVLHRLRdhgnTIVVIEH 889
Cdd:PRK11176 466 MDNGLDTV-IGENGVLLSGGQRQRIAIARAL-LRDS--PILILDEATSALDTESeraIQAALDELQKNR----TSLVIAH 537

                 ....*....
gi 648489723 890 NLDVIKTAD 898
Cdd:PRK11176 538 RLSTIEKAD 546
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
809-889 7.05e-07

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 51.63  E-value: 7.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 809 LEMLMEVGLSYiQLGQNATTLSGGEAQRIKLARELSKRDTgrtLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIE 888
Cdd:PRK09493 118 RELLAKVGLAE-RAHHYPSELSGGQQQRVAIARALAVKPK---LMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVT 193

                 .
gi 648489723 889 H 889
Cdd:PRK09493 194 H 194
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
807-895 7.27e-07

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: 51.43  E-value: 7.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 807 RKLEMLMEVGLS-----YIqlgqnaTTLSGGEAQRIKLARELSkrdTGRTLYILDEPTTGLHFEDIAQLLRVLHRL-RDH 880
Cdd:cd03258  120 RVLELLELVGLEdkadaYP------AQLSGGQKQRVGIARALA---NNPKVLLCDEATSALDPETTQSILALLRDInREL 190
                         90
                 ....*....|....*
gi 648489723 881 GNTIVVIEHNLDVIK 895
Cdd:cd03258  191 GLTIVLITHEMEVVK 205
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
776-860 7.34e-07

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: 49.57  E-value: 7.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  776 EVRYKGKNVHEVLEMTVEEALDFFQPVPVIHRK---------LEMLMEVGLSYIQLGQNATTLSGGEAQRIKLARELSKR 846
Cdd:pfam00005  60 EIGYVFQDPQLFPRLTVRENLRLGLLLKGLSKRekdaraeeaLEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTK 139
                          90
                  ....*....|....
gi 648489723  847 dtgRTLYILDEPTT 860
Cdd:pfam00005 140 ---PKLLLLDEPTA 150
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
827-892 7.94e-07

Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 51.55  E-value: 7.94e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648489723 827 TTLSGGEAQRIKLARELSKrDTgrTLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHNLD 892
Cdd:PRK11231 137 TDLSGGQRQRAFLAMVLAQ-DT--PVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLN 199
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
807-892 8.25e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 52.01  E-value: 8.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 807 RKLEMLMEVGL--SYIQlgQNATTLSGGEAQRIKLARELSKRDTgrtLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTI 884
Cdd:PRK13651 144 RAAKYIELVGLdeSYLQ--RSPFELSGGQKRRVALAGILAMEPD---FLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTI 218

                 ....*...
gi 648489723 885 VVIEHNLD 892
Cdd:PRK13651 219 ILVTHDLD 226
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
487-561 8.85e-07

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: 50.07  E-value: 8.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 487 LSGGEAQRIRLA------SQIgsalvgvmYILDEPSIGLHQRDNARLLNTLSHLRDlGNTVIVVEHDEDAIRQAD--YVV 558
Cdd:cd03228   97 LSGGQRQRIAIArallrdPPI--------LILDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIRDADriIVL 167

                 ...
gi 648489723 559 DIG 561
Cdd:cd03228  168 DDG 170
GguA NF040905
sugar ABC transporter ATP-binding protein;
804-898 9.02e-07

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 52.48  E-value: 9.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 804 VIHRKLEMLMEVGLSyiqlgQNATTLSG----GEAQRIKLARELSKRdtgRTLYILDEPTTGLHFEDIAQLLRVLHRLRD 879
Cdd:NF040905 116 TNRRARELLAKVGLD-----ESPDTLVTdigvGKQQLVEIAKALSKD---VKLLILDEPTAALNEEDSAALLDLLLELKA 187
                         90       100
                 ....*....|....*....|
gi 648489723 880 HGNTIVVIEHNL-DVIKTAD 898
Cdd:NF040905 188 QGITSIIISHKLnEIRRVAD 207
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
473-580 9.07e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 51.53  E-value: 9.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 473 VGLDYLtLDRSADTLSGGEAQRIRLASQIgsALVGVMYILDEPSIGLHQRDNARLLNTLSHLRDLGN-TVIVVEHDEDAI 551
Cdd:PRK13632 130 VGMEDY-LDKEPQNLSGGQKQRVAIASVL--ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEA 206
                         90       100
                 ....*....|....*....|....*....
gi 648489723 552 RQADYVVDIGpgagrhGGQIVASGTPEAV 580
Cdd:PRK13632 207 ILADKVIVFS------EGKLIAQGKPKEI 229
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
816-902 9.21e-07

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 52.54  E-value: 9.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 816 GLSYiQLGQNATTLSGGEAQRIKLARELSKrdTGRtLYILDEPTTGL--HFEDiaQLLRVLHRLRdHGNTIVVIEHNLDV 893
Cdd:PRK11174 474 GLDT-PIGDQAAGLSVGQAQRLALARALLQ--PCQ-LLLLDEPTASLdaHSEQ--LVMQALNAAS-RRQTTLMVTHQLED 546
                         90
                 ....*....|.
gi 648489723 894 IKTAD--WLID 902
Cdd:PRK11174 547 LAQWDqiWVMQ 557
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
804-895 9.52e-07

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: 52.52  E-value: 9.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  804 VIHRKLEMLMEVGLSYIQLGQNATTLSGGEAQRIKLARELSKRdtgRTLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNT 883
Cdd:TIGR02633 117 MYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQ---ARLLILDEPSSSLTEKETEILLDIIRDLKAHGVA 193
                          90
                  ....*....|..
gi 648489723  884 IVVIEHNLDVIK 895
Cdd:TIGR02633 194 CVYISHKLNEVK 205
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
447-560 1.07e-06

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: 52.29  E-value: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  447 QLPGRFAQ-IAEKI-----------VREISSRLG---FLNDVGLDYLT-LDRSADTLSGGEAQRIRLAsqigSALVGV-- 508
Cdd:TIGR02857 403 QHPFLFAGtIAENIrlarpdasdaeIREALERAGldeFVAALPQGLDTpIGEGGAGLSGGQAQRLALA----RAFLRDap 478
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 648489723  509 MYILDEPSIGLHQRDNARLLNTLSHLRDlGNTVIVVEHDEDAIRQADYVVDI 560
Cdd:TIGR02857 479 LLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAALADRIVVL 529
cbiO PRK13641
energy-coupling factor transporter ATPase;
467-592 1.09e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 51.37  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 467 LGFLNDVGLDYLTLDRSADTLSGGEAQRIrlasqigsALVGVMYI------LDEPSIGLHQRDNARLLNTLSHLRDLGNT 540
Cdd:PRK13641 126 LKWLKKVGLSEDLISKSPFELSGGQMRRV--------AIAGVMAYepeilcLDEPAAGLDPEGRKEMMQLFKDYQKAGHT 197
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 648489723 541 VIVVEHDEDAIrqADYVVDIgpGAGRHgGQIVASGTPEAVTQHPDSLTGAYL 592
Cdd:PRK13641 198 VILVTHNMDDV--AEYADDV--LVLEH-GKLIKHASPKEIFSDKEWLKKHYL 244
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
804-896 1.12e-06

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: 50.48  E-value: 1.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 804 VIHRKLEMLME-VGLSYiQLGQNATTLSGGEAQRIKLARELSKRDTgrtLYILDEPTTGLHFEDIAQLLRVLHRLRDHGN 882
Cdd:cd03292  112 EIRKRVPAALElVGLSH-KHRALPAELSGGEQQRVAIARAIVNSPT---ILIADEPTGNLDPDTTWEIMNLLKKINKAGT 187
                         90
                 ....*....|....
gi 648489723 883 TIVVIEHNLDVIKT 896
Cdd:cd03292  188 TVVVATHAKELVDT 201
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
823-903 1.21e-06

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: 50.16  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 823 GQNATTLSGGEAQRIKLAREL-SKRDtgrtLYILDEP------TTGLH-FEDIaqllrVLHRLRDhGNTIVVIEHNLDVI 894
Cdd:cd03250  122 GEKGINLSGGQKQRISLARAVySDAD----IYLLDDPlsavdaHVGRHiFENC-----ILGLLLN-NKTRILVTHQLQLL 191

                 ....*....
gi 648489723 895 KTADWLIDI 903
Cdd:cd03250  192 PHADQIVVL 200
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
470-575 1.23e-06

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: 50.58  E-value: 1.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 470 LNDVGLDYLTLDRSADTLSGGEAQRIRLAsqigSALVG--VMYILDEPSIGLHQRDNARLLNTLSHLRD-LGNTVIVVEH 546
Cdd:cd03257  129 LVGVGLPEEVLNRYPHELSGGQRQRVAIA----RALALnpKLLIADEPTSALDVSVQAQILDLLKKLQEeLGLTLLFITH 204
                         90       100       110
                 ....*....|....*....|....*....|
gi 648489723 547 DEDAIRQ-ADYVVDIgpgagrHGGQIVASG 575
Cdd:cd03257  205 DLGVVAKiADRVAVM------YAGKIVEEG 228
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
822-891 1.24e-06

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: 52.36  E-value: 1.24e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  822 LGQNATTLSGGEAQRIKLARELSkrdTGRTLYILDEPTTGLHFEDIAQLLRVLhRLRDHGNTIVVIEHNL 891
Cdd:TIGR02868 465 LGEGGARLSGGERQRLALARALL---ADAPILLLDEPTEHLDAETADELLEDL-LAALSGRTVVLITHHL 530
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
822-898 1.41e-06

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: 49.62  E-value: 1.41e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648489723 822 LGQN-ATTLSGGEAQRIKLARELsKRDTgrTLYILDEPTTGLHFEDIAQLLR-VLHRLRDhgNTIVVIEHNLDVIKTAD 898
Cdd:cd03247   91 LRNNlGRRFSGGERQRLALARIL-LQDA--PIVLLDEPTVGLDPITERQLLSlIFEVLKD--KTLIWITHHLTGIEHMD 164
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
470-592 1.69e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 50.57  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 470 LNDVGLDYLtLDRSADTLSGGEAQRIRLASQIgsALVGVMYILDEPSIGLH---QRDNARLLNTLShlRDLGNTVIVVEH 546
Cdd:PRK13652 122 LHMLGLEEL-RDRVPHHLSGGEKKRVAIAGVI--AMEPQVLVLDEPTAGLDpqgVKELIDFLNDLP--ETYGMTVIFSTH 196
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 648489723 547 DEDAIRQ-ADYVVDIgpgagrHGGQIVASGTPEAVTQHPDSLTGAYL 592
Cdd:PRK13652 197 QLDLVPEmADYIYVM------DKGRIVAYGTVEEIFLQPDLLARVHL 237
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
789-880 1.90e-06

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: 49.66  E-value: 1.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  789 EMTVEEALDFFQPVPVIHRK--LEMLMEVGLSYIQlGQNATTLSGGEAQRIKLARELSkrdTGRTLYILDEPTTGLhfeD 866
Cdd:TIGR01189  87 ELSALENLHFWAAIHGGAQRtiEDALAAVGLTGFE-DLPAAQLSAGQQRRLALARLWL---SRRPLWILDEPTTAL---D 159
                          90
                  ....*....|....
gi 648489723  867 IAQLLRVLHRLRDH 880
Cdd:TIGR01189 160 KAGVALLAGLLRAH 173
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
829-896 2.18e-06

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: 49.11  E-value: 2.18e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648489723 829 LSGGEAQRIKLARELSKRDtgrTLYILDEPTTGLHFEDIAQLLRVLHRLRD-HGNTIVVIEHNLDVIKT 896
Cdd:cd03229  101 LSGGQQQRVALARALAMDP---DVLLLDEPTSALDPITRREVRALLKSLQAqLGITVVLVTHDLDEAAR 166
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
820-903 2.30e-06

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: 48.21  E-value: 2.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 820 IQLGQNATT-----LSGGEAQRIKLARELSKRDTgrtLYILDEPTTGLHFEDIAQLLRVlhrLRDHGNTIVVIEHNLDVI 894
Cdd:cd03221   57 VTWGSTVKIgyfeqLSGGEKMRLALAKLLLENPN---LLLLDEPTNHLDLESIEALEEA---LKEYPGTVILVSHDRYFL 130
                         90
                 ....*....|
gi 648489723 895 -KTADWLIDI 903
Cdd:cd03221  131 dQVATKIIEL 140
cbiO PRK13637
energy-coupling factor transporter ATPase;
785-901 2.54e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 50.43  E-value: 2.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 785 HEVLEMTVEEALDFfQPVPV------IHRKLEMLME-VGLSYIQL-GQNATTLSGGEAQRIKLARELSKRDTgrtLYILD 856
Cdd:PRK13637  94 YQLFEETIEKDIAF-GPINLglseeeIENRVKRAMNiVGLDYEDYkDKSPFELSGGQKRRVAIAGVVAMEPK---ILILD 169
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 648489723 857 EPTTGLH---FEDIAQLLRVLHrlRDHGNTIVVIEHNL-DVIKTADWLI 901
Cdd:PRK13637 170 EPTAGLDpkgRDEILNKIKELH--KEYNMTIILVSHSMeDVAKLADRII 216
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
787-887 2.58e-06

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 51.17  E-value: 2.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 787 VLEMTVEE-----ALDFFQPVPVIHRKLEMlmEVGLSYIQ--------LGQNATTLSGGEAQRIKLARELSkrdTGRTLY 853
Cdd:COG1129  342 VLDLSIREnitlaSLDRLSRGGLLDRRRER--ALAEEYIKrlriktpsPEQPVGNLSGGNQQKVVLAKWLA---TDPKVL 416
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 648489723 854 ILDEPTTGLhfeDI---AQLLRVLHRLRDHGNTIVVI 887
Cdd:COG1129  417 ILDEPTRGI---DVgakAEIYRLIRELAAEGKAVIVI 450
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
474-584 2.60e-06

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 51.38  E-value: 2.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 474 GLDYLTLDRSAdTLSGGEAQRIRLAsqigSALV--GVMYILDEPSIGLHQRDNARLLNTLSHLRdLGNTVIVVEHDEDAI 551
Cdd:PRK11174 474 GLDTPIGDQAA-GLSVGQAQRLALA----RALLqpCQLLLLDEPTASLDAHSEQLVMQALNAAS-RRQTTLMVTHQLEDL 547
                         90       100       110
                 ....*....|....*....|....*....|...
gi 648489723 552 RQADYVVDIgpgagrHGGQIVASGTPEAVTQHP 584
Cdd:PRK11174 548 AQWDQIWVM------QDGQIVQQGDYAELSQAG 574
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
487-564 2.83e-06

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: 48.37  E-value: 2.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 487 LSGGEAQRIRLASqigsALVG--VMYILDEPSIGLHQRDNARLLNTLSHLRDLGNTVIVVEHDEDAIRQADYVVDIGPGA 564
Cdd:cd03246   97 LSGGQRQRLGLAR----ALYGnpRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGR 172
cbiO PRK13645
energy-coupling factor transporter ATPase;
482-588 2.85e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 50.01  E-value: 2.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 482 RSADTLSGGEAQRIRLASQIgsALVGVMYILDEPSIGLHQRDNARLLNTLSHL-RDLGNTVIVVEHDEDAI-RQADYVVD 559
Cdd:PRK13645 146 RSPFELSGGQKRRVALAGII--AMDGNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVlRIADEVIV 223
                         90       100
                 ....*....|....*....|....*....
gi 648489723 560 IgpgagrHGGQIVASGTPEAVTQHPDSLT 588
Cdd:PRK13645 224 M------HEGKVISIGSPFEIFSNQELLT 246
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
824-893 3.01e-06

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 50.61  E-value: 3.01e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 824 QNATTLSGGEAQRIKLARELSKRdtgRTLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHNLDV 893
Cdd:PRK09536 135 RPVTSLSGGERQRVLLARALAQA---TPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDL 201
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
829-889 3.18e-06

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: 48.70  E-value: 3.18e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648489723 829 LSGGEAQRIKLARELSKRDTgrtLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEH 889
Cdd:cd03213  112 LSGGERKRVSIALELVSNPS---LLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIH 169
cbiO PRK13640
energy-coupling factor transporter ATPase;
458-592 3.20e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 49.80  E-value: 3.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 458 KIVREIssrlgfLNDVG-LDYLtlDRSADTLSGGEAQRIRLAS--QIGSALVgvmyILDEPSIGLHQRDNARLLNTLSHL 534
Cdd:PRK13640 122 KIVRDV------LADVGmLDYI--DSEPANLSGGQKQRVAIAGilAVEPKII----ILDESTSMLDPAGKEQILKLIRKL 189
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 648489723 535 RDLGN-TVIVVEHDEDAIRQADYVVDIgpgagrHGGQIVASGTPEAVTQHPDSLTGAYL 592
Cdd:PRK13640 190 KKKNNlTVISITHDIDEANMADQVLVL------DDGKLLAQGSPVEIFSKVEMLKEIGL 242
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
828-895 3.36e-06

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 50.80  E-value: 3.36e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648489723 828 TLSGGEAQRIKLARELSkRDTgRTLyILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHNLDVIK 895
Cdd:COG3845  141 DLSVGEQQRVEILKALY-RGA-RIL-ILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVM 205
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
481-598 4.17e-06

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 49.60  E-value: 4.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 481 DRSADTLSGGEAQRIRLASQIGSAlVGVMyILDEPSIGL---HQRDnarLLNTLSHL-RDLGNTVIVVEHD-EDAIRQAD 555
Cdd:PRK10253 138 DQSVDTLSGGQRQRAWIAMVLAQE-TAIM-LLDEPTTWLdisHQID---LLELLSELnREKGYTLAAVLHDlNQACRYAS 212
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 648489723 556 YVVDIgpgagrHGGQIVASGTP-EAVTqhPDSLTGAYlrGTRCI 598
Cdd:PRK10253 213 HLIAL------REGKIVAQGAPkEIVT--AELIERIY--GLRCM 246
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
457-588 4.26e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 49.36  E-value: 4.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 457 EKIVREISSrlgFLNDVG-LDYLtlDRSADTLSGGEAQRIRLASQIgsALVGVMYILDEPSIGLHQRDNARLLNTLSHLR 535
Cdd:PRK13648 117 DEMHRRVSE---ALKQVDmLERA--DYEPNALSGGQKQRVAIAGVL--ALNPSVIILDEATSMLDPDARQNLLDLVRKVK 189
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 648489723 536 DLGN-TVIVVEHDEDAIRQADYVVDIgpgagrHGGQIVASGTPEAVTQHPDSLT 588
Cdd:PRK13648 190 SEHNiTIISITHDLSEAMEADHVIVM------NKGTVYKEGTPTEIFDHAEELT 237
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
3-51 5.10e-06

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: 47.35  E-value: 5.10e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 648489723   3 SISIRGARtHNLKNVDLDLPRERLIVITGVSGSGKSSLAFDTLFAEGQR 51
Cdd:cd03227    1 KIVLGRFP-SYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGA 48
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
821-891 5.96e-06

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 49.11  E-value: 5.96e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648489723 821 QLGQnattLSGGEAQRIKLARELSKRDTgrtLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHNL 891
Cdd:PRK15056 139 QIGE----LSGGQKKRVFLARAIAQQGQ---VILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNL 202
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
487-601 6.00e-06

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 48.99  E-value: 6.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 487 LSGGEAQRIRLASQIgsALVGVMYILDEPSIGlhqRDN------ARLLNTLSHlrDLGNTVIVVEHD-EDAIRQADYVVD 559
Cdd:PRK11831 144 LSGGMARRAALARAI--ALEPDLIMFDEPFVG---QDPitmgvlVKLISELNS--ALGVTCVVVSHDvPEVLSIADHAYI 216
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 648489723 560 IgpgAGRHggqIVASGTPEAVTQHPDSLTGAYLRGTRCIPVP 601
Cdd:PRK11831 217 V---ADKK---IVAHGSAQALQANPDPRVRQFLDGIADGPVP 252
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
470-564 6.22e-06

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: 48.02  E-value: 6.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 470 LNDVGLDYLTlDRSADTLSGGEAQRIRLASQIGSAlvGVMYILDEPSIGLHQRDNARLLNTLSHLRDLGNTVIVVEHDED 549
Cdd:cd03226  111 LKDLDLYALK-ERHPLSLSGGQKQRLAIAAALLSG--KDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYE 187
                         90
                 ....*....|....*.
gi 648489723 550 -AIRQADYVVDIGPGA 564
Cdd:cd03226  188 fLAKVCDRVLLLANGA 203
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
789-927 6.24e-06

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: 48.31  E-value: 6.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 789 EMTVEE----ALDFFQ-PVPVIHRKLE-MLMEVGLSYIQLgQNATTLSGGEAQRIKLARELSkrdTGRTLYILDEPTTGL 862
Cdd:cd03218   89 KLTVEEnilaVLEIRGlSKKEREEKLEeLLEEFHITHLRK-SKASSLSGGERRRVEIARALA---TNPKFLLLDEPFAGV 164
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648489723 863 HFEDIAQLLRVLHRLRDHGNTIVVIEHN----LDVIKTADWLIDigpeggsggGELLVAGTPEAVAGHP 927
Cdd:cd03218  165 DPIAVQDIQKIIKILKDRGIGVLITDHNvretLSITDRAYIIYE---------GKVLAEGTPEEIAANE 224
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
810-901 6.31e-06

ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 48.60  E-value: 6.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 810 EMLMEVGLSYIqLGQNATTLSGGEAQRIKLARELSKRdtgRTLYILDEPTTGLhfeDIA------QLLRVLHrlRDHGNT 883
Cdd:COG3840  112 QALERVGLAGL-LDRLPGQLSGGQRQRVALARCLVRK---RPILLLDEPFSAL---DPAlrqemlDLVDELC--RERGLT 182
                         90
                 ....*....|....*....
gi 648489723 884 IVVIEHNL-DVIKTADWLI 901
Cdd:COG3840  183 VLMVTHDPeDAARIADRVL 201
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
829-903 6.79e-06

ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 47.57  E-value: 6.79e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648489723 829 LSGGEAQRIKLARELSKRdtgRTLYILDEPTTGLHFEDIAQLLRVLHRLRDHGN-TIVVIEHNLDVIktaDWLIDI 903
Cdd:cd03222   72 LSGGELQRVAIAAALLRN---ATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVL---DYLSDR 141
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
829-894 6.88e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 48.92  E-value: 6.88e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648489723 829 LSGGEAQRIKLARELSKRDTgrtLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHNLDVI 894
Cdd:PRK13639 138 LSGGQKKRVAIAGILAMKPE---IIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLV 200
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
482-578 7.54e-06

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 48.73  E-value: 7.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 482 RSADTLSGGEAQRIRLASQIgsALVGVMYILDEPSIGLHQRDNARLLNTLSHLRDLGNTVIVVEHDEDAIRQ-ADYVVDI 560
Cdd:PRK15056 138 RQIGELSGGQKKRVFLARAI--AQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEfCDYTVMV 215
                         90
                 ....*....|....*...
gi 648489723 561 gpgagrhGGQIVASGTPE 578
Cdd:PRK15056 216 -------KGTVLASGPTE 226
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
790-895 7.99e-06

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 48.93  E-value: 7.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 790 MTV----EEALDFFQP----VPVIHRKLEMLMEVGLSYIQLGQNATTLSGGEAQRIKLARELSKRDtgrTLYILDEPTTG 861
Cdd:PRK15079 115 MTIgeiiAEPLRTYHPklsrQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEP---KLIICDEPVSA 191
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 648489723 862 LHFEDIAQLLRVLHRL-RDHGNTIVVIEHNLDVIK 895
Cdd:PRK15079 192 LDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVK 226
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
821-901 8.27e-06

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: 48.00  E-value: 8.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 821 QLGQNATTLSGGEAQRIKLARELSKRDtgrTLYILDEPTTGLHFEDIAQLLRVLHRLRDhGNTIVVIEHNLDVIKTADWL 900
Cdd:cd03253  130 IVGERGLKLSGGEKQRVAIARAILKNP---PILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTIVNADKI 205

                 .
gi 648489723 901 I 901
Cdd:cd03253  206 I 206
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
790-889 8.46e-06

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: 47.49  E-value: 8.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 790 MTVEEALDFFQPVPVIHRKLEMLMEVGLSYIQlGQNATTLSGGEAQRIKLARELSkrdTGRTLYILDEPTTGLhfeDIAQ 869
Cdd:cd03231   88 LSVLENLRFWHADHSDEQVEEALARVGLNGFE-DRPVAQLSAGQQRRVALARLLL---SGRPLWILDEPTTAL---DKAG 160
                         90       100
                 ....*....|....*....|...
gi 648489723 870 LLRVLHRLRDH---GNTIVVIEH 889
Cdd:cd03231  161 VARFAEAMAGHcarGGMVVLTTH 183
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
623-898 8.52e-06

ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 48.12  E-value: 8.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 623 LKGGDFAFPTGLFTCVTGVSGSGKSTLvnntlypavateLH--GGrhhieeheridglelIDKV----VDIDQSPIGRTP 696
Cdd:COG1136   24 LRGVSLSIEAGEFVAIVGPSGSGKSTL------------LNilGG---------------LDRPtsgeVLIDGQDISSLS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 697 RsnpatytglftpiRELfaatAEARSRgykpgRFSFnvrggrceacqgdgvikvemhflpdVF-----VPcdvckghryn 771
Cdd:COG1136   77 E-------------REL----ARLRRR-----HIGF-------------------------VFqffnlLP---------- 99
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 772 retlevrykgknvhevlEMTVEE----ALDFF-QPVPVIHRK-LEMLMEVGLSYiQLGQNATTLSGGEAQRIKLARELSK 845
Cdd:COG1136  100 -----------------ELTALEnvalPLLLAgVSRKERRERaRELLERVGLGD-RLDHRPSQLSGGQQQRVAIARALVN 161
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 648489723 846 RdtgRTLYILDEPTTGLHFEDIAQLLRVLHRL-RDHGNTIVVIEHNLDVIKTAD 898
Cdd:COG1136  162 R---PKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHDPELAARAD 212
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
454-575 9.76e-06

Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 47.74  E-value: 9.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 454 QIAEKIVREISSRLGF-LNDVGLDYLtLDRSADTLSGGEAQRIRLASqigsALVG--VMYILDEPSIGLHQRDNARLLNT 530
Cdd:COG2884  105 RVTGKSRKEIRRRVREvLDLVGLSDK-AKALPHELSGGEQQRVAIAR----ALVNrpELLLADEPTGNLDPETSWEIMEL 179
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 648489723 531 LSHLRDLGNTVIVVEHDEDAIRQADY-VVDIgpgagrHGGQIVASG 575
Cdd:COG2884  180 LEEINRRGTTVLIATHDLELVDRMPKrVLEL------EDGRLVRDE 219
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
809-891 1.01e-05

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 49.44  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 809 LEMLMEVGLSYIQ---------LGQNATTLSGGEAQRIKLARELsKRDTgrTLYILDEPTTGLhfeDIAQLLRVLHRLRD 879
Cdd:PRK11160 447 IEVLQQVGLEKLLeddkglnawLGEGGRQLSGGEQRRLGIARAL-LHDA--PLLLLDEPTEGL---DAETERQILELLAE 520
                         90
                 ....*....|....
gi 648489723 880 H--GNTIVVIEHNL 891
Cdd:PRK11160 521 HaqNKTVLMITHRL 534
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
469-586 1.06e-05

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 48.04  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 469 FLNDVGLDYLTLDRSADTLSGGEAQRIRLASQIgsALVGVMYILDEPSIGLHQRDNARLLNTLSHLRDLGNTVIVVEHDE 548
Cdd:PRK10619 135 YLAKVGIDERAQGKYPVHLSGGQQQRVSIARAL--AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEM 212
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 648489723 549 DAIRQ-ADYVVDIgpgagrHGGQIVASGTPEAVTQHPDS 586
Cdd:PRK10619 213 GFARHvSSHVIFL------HQGKIEEEGAPEQLFGNPQS 245
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
805-903 1.31e-05

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: 48.78  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  805 IHRKLEMLMEvGLSYIQLGQNATTLSGGEAQRIKLAREL-SKRDtgrtLYILDEPTTGLHFEDIAQLLRVLHrlrDHGNT 883
Cdd:TIGR03719 139 LDSQLEIAMD-ALRCPPWDADVTKLSGGERRRVALCRLLlSKPD----MLLLDEPTNHLDAESVAWLERHLQ---EYPGT 210
                          90       100
                  ....*....|....*....|...
gi 648489723  884 IVVIEHN---LDVIktADWLIDI 903
Cdd:TIGR03719 211 VVAVTHDryfLDNV--AGWILEL 231
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
785-927 1.37e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 48.09  E-value: 1.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 785 HEVLEMTVEEALDFfQP----VPVIHRKL---EMLMEVGLSYIQLGQNATTLSGGEAQRIKLARELSKRDtgrTLYILDE 857
Cdd:PRK13634  96 HQLFEETVEKDICF-GPmnfgVSEEDAKQkarEMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEP---EVLVLDE 171
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648489723 858 PTTGLH---FEDIAQLLRVLHrlRDHGNTIVVIEHNL-DVIKTADWLIdigpegGSGGGELLVAGTPEAVAGHP 927
Cdd:PRK13634 172 PTAGLDpkgRKEMMEMFYKLH--KEKGLTTVLVTHSMeDAARYADQIV------VMHKGTVFLQGTPREIFADP 237
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
433-558 1.47e-05

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: 47.25  E-value: 1.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 433 HMSVANAQAFfsDLQLPGRFAQIAEKIVREISSRLGflndvgLDYLtLDRSADTLSGGEAQRIRLasqiGSALVG--VMY 510
Cdd:cd03301   86 HMTVYDNIAF--GLKLRKVPKDEIDERVREVAELLQ------IEHL-LDRKPKQLSGGQRQRVAL----GRAIVRepKVF 152
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 648489723 511 ILDEPSIGLHQRDNARLLNTLSHL-RDLGNTVIVVEHDE-DAIRQADYVV 558
Cdd:cd03301  153 LMDEPLSNLDAKLRVQMRAELKRLqQRLGTTTIYVTHDQvEAMTMADRIA 202
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
828-903 1.58e-05

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: 45.99  E-value: 1.58e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648489723 828 TLSGGEAQRIKLARELSKRDtgrTLYILDEPTTGLhfeDIAQLLRVLHRLRDHGNTIVVIEHNLDVIKTADWLIDI 903
Cdd:cd03223   91 VLSGGEQQRLAFARLLLHKP---KFVFLDEATSAL---DEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDL 160
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
827-903 1.73e-05

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: 47.04  E-value: 1.73e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648489723 827 TTLSGGEAQRIKLARELSKRdtgRTLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHNLDVIKT-ADWLIDI 903
Cdd:COG4778  151 ATFSGGEQQRVNIARGFIAD---PPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAvADRVVDV 225
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
480-622 1.81e-05

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 47.42  E-value: 1.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 480 LDRSADTLSGGEAQRIRLASqigsALVGV--MYILDEPSIGLHQRDNARLLNTLSHLR-DLGNTVIVVEHD-EDAIRQAD 555
Cdd:PRK09544 114 IDAPMQKLSGGETQRVLLAR----ALLNRpqLLVLDEPTQGVDVNGQVALYDLIDQLRrELDCAVLMVSHDlHLVMAKTD 189
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648489723 556 YVVDIGpgagrhgGQIVASGTPEAVTQHPDSLTGAYLRGTRCIPVPEHRIEPDPDREIRVIGARGNN 622
Cdd:PRK09544 190 EVLCLN-------HHICCSGTPEVVSLHPEFISMFGPRGAEQLGIYRHHHNHRHDLQGRIVLRRGND 249
cbiO PRK13645
energy-coupling factor transporter ATPase;
785-901 1.91e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 47.70  E-value: 1.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 785 HEVLEMTVEEALDFfQPVPV------IHRKL-EMLMEVGLSYIQLGQNATTLSGGEAQRIKLARELSKrdTGRTLyILDE 857
Cdd:PRK13645 101 YQLFQETIEKDIAF-GPVNLgenkqeAYKKVpELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAM--DGNTL-VLDE 176
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 648489723 858 PTTGLHFEDIAQLLRVLHRL-RDHGNTIVVIEHNLD-VIKTADWLI 901
Cdd:PRK13645 177 PTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDqVLRIADEVI 222
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
823-898 2.21e-05

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 48.42  E-value: 2.21e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648489723 823 GQNATTLSGGEAQRIKLARELSKRDtgrTLYILDEPTTGLHFEDIAQLLRVLHRLRdHGNTIVVIEHNLDVIKTAD 898
Cdd:PRK13657 466 GERGRQLSGGERQRLAIARALLKDP---PILILDEATSALDVETEAKVKAALDELM-KGRTTFIIAHRLSTVRNAD 537
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
790-889 2.52e-05

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 48.12  E-value: 2.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  790 MTVEEALdFFQPVPVIHRKL----------EMLMEVGL-----SYIQLGQNATTLSGGEAQRIKLARELSkrdTGRTLYI 854
Cdd:TIGR00955 114 LTVREHL-MFQAHLRMPRRVtkkekrervdEVLQALGLrkcanTRIGVPGRVKGLSGGERKRLAFASELL---TDPPLLF 189
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 648489723  855 LDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEH 889
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
792-895 2.70e-05

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 47.78  E-value: 2.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 792 VEEALDFFQPVPVIH----RKLEMLMEVGLSYIQLGQNATTLSGGEAQRIKLARELSKRDtgrTLYILDEPTTGLHFEDI 867
Cdd:PRK15134 385 IEEGLRVHQPTLSAAqreqQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKP---SLIILDEPTSSLDKTVQ 461
                         90       100
                 ....*....|....*....|....*....
gi 648489723 868 AQLLRVLHRLR-DHGNTIVVIEHNLDVIK 895
Cdd:PRK15134 462 AQILALLKSLQqKHQLAYLFISHDLHVVR 490
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
790-887 2.71e-05

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: 46.42  E-value: 2.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 790 MTVEEALDFF---QPVP---VIHRKLEMLMEVGLsYIQLGQNATTLSGGEAQRIKLARELSKRDTgrtLYILDEPTTGLh 863
Cdd:cd03264   87 FTVREFLDYIawlKGIPskeVKARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGDPS---ILIVDEPTAGL- 161
                         90       100
                 ....*....|....*....|....
gi 648489723 864 feDIAQLLRVLHRLRDHGNTIVVI 887
Cdd:cd03264  162 --DPEERIRFRNLLSELGEDRIVI 183
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
807-895 2.75e-05

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 47.86  E-value: 2.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 807 RKLEMLMEVGLSyIQLGQNATTLSGGEAQRIKLARELSkrdTGRTLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVV 886
Cdd:PRK09700 125 RAAMMLLRVGLK-VDLDEKVANLSISHKQMLEIAKTLM---LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVY 200

                 ....*....
gi 648489723 887 IEHNLDVIK 895
Cdd:PRK09700 201 ISHKLAEIR 209
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
798-895 2.77e-05

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: 46.79  E-value: 2.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 798 FFQPVPVIHRK--LEMLMEVGLSYiQLGQNATTLSGGEAQRIKLARELSKRDtgrTLYILDEPTTGLhfeDIAQLLRVLH 875
Cdd:cd03256  113 LFGLFPKEEKQraLAALERVGLLD-KAYQRADQLSGGQQQRVAIARALMQQP---KLILADEPVASL---DPASSRQVMD 185
                         90       100
                 ....*....|....*....|....
gi 648489723 876 RLRD----HGNTIVVIEHNLDVIK 895
Cdd:cd03256  186 LLKRinreEGITVIVSLHQVDLAR 209
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
790-896 2.87e-05

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: 46.56  E-value: 2.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 790 MTVEEALDF-----FQPVPVIHRK-LEMLMEVGLSYIqLGQNATTLSGGEAQRIKLARELSKRDtgrTLYILDEPTTGLH 863
Cdd:cd03299   86 MTVYKNIAYglkkrKVDKKEIERKvLEIAEMLGIDHL-LNRKPETLSGGEQQRVAIARALVVNP---KILLLDEPFSALD 161
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 648489723 864 F---EDIAQLLRVLHRLrdHGNTIVVIEHNLDVIKT 896
Cdd:cd03299  162 VrtkEKLREELKKIRKE--FGVTVLHVTHDFEEAWA 195
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
449-559 2.97e-05

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 46.63  E-value: 2.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 449 PGRFAQIAEKIVREISSRLGFLNDV----GLDYLtLDRSADTLSGGEAQRIRLASQIGSAlvGVMYILDEPSIGLHQRDN 524
Cdd:cd03237   75 EGTVRDLLSSITKDFYTHPYFKTEIakplQIEQI-LDREVPELSGGELQRVAIAACLSKD--ADIYLLDEPSAYLDVEQR 151
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 648489723 525 ARLLNTLSHLRDLGN-TVIVVEHDedaIRQADYVVD 559
Cdd:cd03237  152 LMASKVIRRFAENNEkTAFVVEHD---IIMIDYLAD 184
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
484-594 3.23e-05

high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 46.41  E-value: 3.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 484 ADTLSGGEAQRIrlasQIGSALVGV--MYILDEPSIGLHQRDNARLLNTLSHLRDLGNTVIVVEHDED-AIRQAD--YVV 558
Cdd:PRK11614 135 AGTMSGGEQQML----AIGRALMSQprLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANqALKLADrgYVL 210
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 648489723 559 DigpgagrhGGQIVASGTPEAVTQHpDSLTGAYLRG 594
Cdd:PRK11614 211 E--------NGHVVLEDTGDALLAN-EAVRSAYLGG 237
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
805-891 3.33e-05

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 46.60  E-value: 3.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 805 IHRKLEMLMEVGLSYIQLGQNATTLSGGEAQRIKLARELSkrdTGRTLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNT- 883
Cdd:PRK10419 128 LARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALA---VEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTa 204

                 ....*...
gi 648489723 884 IVVIEHNL 891
Cdd:PRK10419 205 CLFITHDL 212
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
487-575 3.48e-05

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: 45.38  E-value: 3.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 487 LSGGEAQRIRLASQI--GSALVgvmyILDEPSIGLHQRDNARLLNTL-SHLRDlgNTVIVVEHDEDAIRQADYVVDIgpg 563
Cdd:cd03247   99 FSGGERQRLALARILlqDAPIV----LLDEPTVGLDPITERQLLSLIfEVLKD--KTLIWITHHLTGIEHMDKILFL--- 169
                         90
                 ....*....|..
gi 648489723 564 agrHGGQIVASG 575
Cdd:cd03247  170 ---ENGKIIMQG 178
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
776-895 3.54e-05

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.


Pssm-ID: 213184 [Multi-domain]  Cd Length: 200  Bit Score: 45.60  E-value: 3.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 776 EVRYKGKNVhevLEMTVEE------ALDFFQPVPVIHRKLEMLmevgLSYIQLGqnattLSGGEAQRIKLARELSKRDTg 849
Cdd:cd03217   58 EILFKGEDI---TDLPPEErarlgiFLAFQYPPEIPGVKNADF----LRYVNEG-----FSGGEKKRNEILQLLLLEPD- 124
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 648489723 850 rtLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHN---LDVIK 895
Cdd:cd03217  125 --LAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYqrlLDYIK 171
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
434-575 3.77e-05

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: 45.82  E-value: 3.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 434 MSVANAQAFFSDLQlpGRFAQIAEKIVREISSRLGFLNdvgldylTLDRSADTLSGGEAQRIRLASqigsALV---GVMy 510
Cdd:cd03266   93 LTARENLEYFAGLY--GLKGDELTARLEELADRLGMEE-------LLDRRVGGFSTGMRQKVAIAR----ALVhdpPVL- 158
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648489723 511 ILDEPSIGLHQRDNARLLNTLSHLRDLGNTVIVVEHD-EDAIRQADYVVDIgpgagrHGGQIVASG 575
Cdd:cd03266  159 LLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHImQEVERLCDRVVVL------HRGRVVYEG 218
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
480-594 3.84e-05

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 46.44  E-value: 3.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 480 LDRSADTLSGGEAQRIRLASQIgsALVGVMYILDEPSIGLHQRDNARLLNTLSHLRDLGNTVIVVEHDEDAIRQADYVvd 559
Cdd:PRK14247 140 LDAPAGKLSGGQQQRLCIARAL--AFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYV-- 215
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 648489723 560 igpgAGRHGGQIVASG-TPEAVTQHPDSLTGAYLRG 594
Cdd:PRK14247 216 ----AFLYKGQIVEWGpTREVFTNPRHELTEKYVTG 247
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
791-920 4.15e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 46.77  E-value: 4.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 791 TVEEALdFFQPVPVIHRKLEM-------LMEVGLSYIQLGQNATTLSGGEAQRIKLARELSKRDTgrtLYILDEPTTGLH 863
Cdd:PRK13631 133 TIEKDI-MFGPVALGVKKSEAkklakfyLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPE---ILIFDEPTAGLD 208
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 648489723 864 FEDIAQLLRVLHRLRDHGNTIVVIEHNLD-VIKTADWLIdigpegGSGGGELLVAGTP 920
Cdd:PRK13631 209 PKGEHEMMQLILDAKANNKTVFVITHTMEhVLEVADEVI------VMDKGKILKTGTP 260
cbiO PRK13649
energy-coupling factor transporter ATPase;
810-899 4.26e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 46.28  E-value: 4.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 810 EMLMEVGLSYIQLGQNATTLSGGEAQRIKLARELSKRDTgrtLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEH 889
Cdd:PRK13649 127 EKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPK---ILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
                         90
                 ....*....|.
gi 648489723 890 NL-DVIKTADW 899
Cdd:PRK13649 204 LMdDVANYADF 214
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
821-898 4.91e-05

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: 45.68  E-value: 4.91e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648489723 821 QLGQNATTLSGGEAQRIKLARELSKRDtgrTLYILDEPTTGLHFEDIAQLLRVLHRLRDhGNTIVVIEHNLDVIKTAD 898
Cdd:cd03251  131 VIGERGVKLSGGQRQRIAIARALLKDP---PILILDEATSALDTESERLVQAALERLMK-NRTTFVIAHRLSTIENAD 204
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
812-901 4.95e-05

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 45.86  E-value: 4.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 812 LMEVGLSYIQLGQNATTLSGGEAQRIKLARELskRDTGRTLyILDEPTTGLHFEDIAQLLRVLHRL-RDHGNTIVVIEHN 890
Cdd:PRK10247 121 LERFALPDTILTKNIAELSGGEKQRISLIRNL--QFMPKVL-LLDEITSALDESNKHNVNEIIHRYvREQNIAVLWVTHD 197
                         90
                 ....*....|.
gi 648489723 891 LDVIKTADWLI 901
Cdd:PRK10247 198 KDEINHADKVI 208
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
829-895 5.03e-05

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 45.78  E-value: 5.03e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648489723 829 LSGGEAQRIKLARELSKRDtgrTLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHNLDVIK 895
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEP---QVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVAR 205
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
785-894 5.13e-05

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 46.83  E-value: 5.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 785 HEVLEMTVEEALdFFQPVP----VIHRKL------EMLMEVGLSyIQLGQNATTLSGGEAQRIKLARELSkRDTgrTLYI 854
Cdd:PRK11288  89 HLVPEMTVAENL-YLGQLPhkggIVNRRLlnyearEQLEHLGVD-IDPDTPLKYLSIGQRQMVEIAKALA-RNA--RVIA 163
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 648489723 855 LDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHNLDVI 894
Cdd:PRK11288 164 FDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEI 203
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
457-594 5.23e-05

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 45.81  E-value: 5.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 457 EKIVREISSRLGFLNDVgldYLTLDRSADTLSGGEAQRIRLASQIgsALVGVMYILDEPSIGLHQRDNARLLNTLSHLRD 536
Cdd:PRK14246 127 KKIVEECLRKVGLWKEV---YDRLNSPASQLSGGQQQRLTIARAL--ALKPKVLLMDEPTSMIDIVNSQAIEKLITELKN 201
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 648489723 537 LGNTVIVVEHDEDAIRQADYVvdigpgAGRHGGQIVASGTPEAVTQHP-DSLTGAYLRG 594
Cdd:PRK14246 202 EIAIVIVSHNPQQVARVADYV------AFLYNGELVEWGSSNEIFTSPkNELTEKYVIG 254
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
805-901 5.54e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 45.90  E-value: 5.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 805 IHRKL-EMLMEVGLsYIQLGQNATTLSGGEAQRIKLARELSkrdTGRTLYILDEPTTGLHFEDIAQLLRVLHRLR-DHGN 882
Cdd:PRK13648 119 MHRRVsEALKQVDM-LERADYEPNALSGGQKQRVAIAGVLA---LNPSVIILDEATSMLDPDARQNLLDLVRKVKsEHNI 194
                         90
                 ....*....|....*....
gi 648489723 883 TIVVIEHNLDVIKTADWLI 901
Cdd:PRK13648 195 TIISITHDLSEAMEADHVI 213
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
462-559 6.14e-05

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 46.73  E-value: 6.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 462 EISSRLGflndvgLDYLtLDRSADTLSGGEAQriRLAsqIGSALV--GVMYILDEPSIGL--HQRDN-ARLLNTLSHLRD 536
Cdd:PRK13409 436 EIIKPLQ------LERL-LDKNVKDLSGGELQ--RVA--IAACLSrdADLYLLDEPSAHLdvEQRLAvAKAIRRIAEERE 504
                         90       100
                 ....*....|....*....|...
gi 648489723 537 lgNTVIVVEHDedaIRQADYVVD 559
Cdd:PRK13409 505 --ATALVVDHD---IYMIDYISD 522
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
807-889 6.28e-05

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: 45.50  E-value: 6.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 807 RKLEMLMEVGLSYiQLGQNATTLSGGEAQRIKLARELSkrdTGRTLYILDEPTTGLHF---EDIAQLLRVLHrlRDHGNT 883
Cdd:COG4181  126 RARALLERVGLGH-RLDHYPAQLSGGEQQRVALARAFA---TEPAILFADEPTGNLDAatgEQIIDLLFELN--RERGTT 199

                 ....*.
gi 648489723 884 IVVIEH 889
Cdd:COG4181  200 LVLVTH 205
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
807-897 6.84e-05

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 45.27  E-value: 6.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 807 RKLEMLMEVGLSYIQ--LGQnatTLSGGEAQRIKLARELSkrdTGRTLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTI 884
Cdd:PRK10895 117 RANELMEEFHIEHLRdsMGQ---SLSGGERRRVEIARALA---ANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGV 190
                         90
                 ....*....|....*..
gi 648489723 885 VVIEHN----LDVIKTA 897
Cdd:PRK10895 191 LITDHNvretLAVCERA 207
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
441-562 7.04e-05

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: 44.91  E-value: 7.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 441 AFFSDLQLPGRFAQIAEKIVREISSR----LGFLNDVGLDYLT---------------------LDRSADTLSGGE---- 491
Cdd:cd03240   45 ALTGELPPNSKGGAHDPKLIREGEVRaqvkLAFENANGKKYTItrslailenvifchqgesnwpLLDMRGRCSGGEkvla 124
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648489723 492 AQRIRLA-SQIGSALVGVMyILDEPSIGLhQRDNAR--LLNTL-SHLRDLGNTVIVVEHDEDAIRQADYVVDIGP 562
Cdd:cd03240  125 SLIIRLAlAETFGSNCGIL-ALDEPTTNL-DEENIEesLAEIIeERKSQKNFQLIVITHDEELVDAADHIYRVEK 197
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
787-889 7.61e-05

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: 44.83  E-value: 7.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 787 VLEMTVEEALDffqpvpvihRKLEMLMEVGLSYiQLGQNATTLSGGEAQRIKLARELSKRDtgrTLYILDEPTTGLHFED 866
Cdd:cd03262  104 VKGMSKAEAEE---------RALELLEKVGLAD-KADAYPAQLSGGQQQRVAIARALAMNP---KVMLFDEPTSALDPEL 170
                         90       100
                 ....*....|....*....|...
gi 648489723 867 IAQLLRVLHRLRDHGNTIVVIEH 889
Cdd:cd03262  171 VGEVLDVMKDLAEEGMTMVVVTH 193
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
830-894 8.32e-05

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 45.87  E-value: 8.32e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648489723 830 SGGEAQRIKLARELSKRDTgrtLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNT-IVVIEHNLDVI 894
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPK---LLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVV 225
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
829-898 8.39e-05

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: 45.19  E-value: 8.39e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648489723 829 LSGGEAQRIKLARELSkrdTGRTLYILDEPTTGLhfeD------IAQLLRVLHRLrdHGNTIVVIEHNLD-VIKTAD 898
Cdd:cd03261  137 LSGGMKKRVALARALA---LDPELLLYDEPTAGL---DpiasgvIDDLIRSLKKE--LGLTSIMVTHDLDtAFAIAD 205
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
807-895 9.05e-05

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 44.81  E-value: 9.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 807 RKLEMLMEVGLSYiQLGQNATTLSGGEAQRIKLARELSKRDtgrTLYILDEPTTGL---HFEDIAQLLRVLHRLrdHGNT 883
Cdd:PRK11629 125 RALEMLAAVGLEH-RANHRPSELSGGERQRVAIARALVNNP---RLVLADEPTGNLdarNADSIFQLLGELNRL--QGTA 198
                         90
                 ....*....|..
gi 648489723 884 IVVIEHNLDVIK 895
Cdd:PRK11629 199 FLVVTHDLQLAK 210
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
811-901 9.40e-05

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: 44.77  E-value: 9.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 811 MLMEVGLsYIQLGQNATTLSGGEAQRIKLARELSKrdTGRTLyILDEPTTGLHFED---IAQLLRVLHRLRdhgnTIVVI 887
Cdd:cd03248  134 SELASGY-DTEVGEKGSQLSGGQKQRVAIARALIR--NPQVL-ILDEATSALDAESeqqVQQALYDWPERR----TVLVI 205
                         90
                 ....*....|....
gi 648489723 888 EHNLDVIKTADWLI 901
Cdd:cd03248  206 AHRLSTVERADQIL 219
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
790-892 9.47e-05

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: 44.82  E-value: 9.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 790 MTVEEALDF---FQPVP---VIHRKLEMLMEVGLSyIQLGQNATTLSGGEAQRIKLARELSKRDtgrTLYILDEPTTGLH 863
Cdd:cd03259   87 LTVAENIAFglkLRGVPkaeIRARVRELLELVGLE-GLLNRYPHELSGGQQQRVALARALAREP---SLLLLDEPLSALD 162
                         90       100       110
                 ....*....|....*....|....*....|
gi 648489723 864 FEDIAQLLRVLHRL-RDHGNTIVVIEHNLD 892
Cdd:cd03259  163 AKLREELREELKELqRELGITTIYVTHDQE 192
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
829-895 9.77e-05

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 46.24  E-value: 9.77e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648489723 829 LSGGEAQRIKLARELSKRDTgrtLYILDEPTTGLHFEDIAQLLRVLHRLRDHGN-TIVVIEHNLDVIK 895
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPE---LLIADEPTTALDVSVQAQILQLLRELQQELNmGLLFITHNLSIVR 221
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
433-584 1.03e-04

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 45.79  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 433 HMSVANAQAFfsDLQLPGrfaqiAEKivREISSRLGFLNDV-GLDYLtLDRSADTLSGGeaQRIRLAsqIGSALVG--VM 509
Cdd:PRK11000  89 HLSVAENMSF--GLKLAG-----AKK--EEINQRVNQVAEVlQLAHL-LDRKPKALSGG--QRQRVA--IGRTLVAepSV 154
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648489723 510 YILDEPSIGLHQ--RDNARLLNTLSHLRdLGNTVIVVEHDE-DAIRQADYVVDIgpgagrHGGQIVASGTPEAVTQHP 584
Cdd:PRK11000 155 FLLDEPLSNLDAalRVQMRIEISRLHKR-LGRTMIYVTHDQvEAMTLADKIVVL------DAGRVAQVGKPLELYHYP 225
cbiO PRK13646
energy-coupling factor transporter ATPase;
776-898 1.04e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 45.16  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 776 EVRYKGKNvhevLEMTVEEALDffqpvpvihRKLEMLMEVGLSYIQLGQNATTLSGGEAQRIKLARELSkrdTGRTLYIL 855
Cdd:PRK13646 106 EIIFGPKN----FKMNLDEVKN---------YAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILA---MNPDIIVL 169
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 648489723 856 DEPTTGLHFEDIAQLLRVLHRLR-DHGNTIVVIEHNL-DVIKTAD 898
Cdd:PRK13646 170 DEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMnEVARYAD 214
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
822-898 1.05e-04

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 46.56  E-value: 1.05e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648489723  822 LGQNATTLSGGEAQRIKLARELSKRDtgrTLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTI-VVIEHNLDVIKTAD 898
Cdd:PTZ00265  573 VGSNASKLSGGQKQRISIARAIIRNP---KILILDEATSSLDNKSEYLVQKTINNLKGNENRItIIIAHRLSTIRYAN 647
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
468-575 1.14e-04

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: 44.41  E-value: 1.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 468 GFLNDVGLDYLTLdRSADTLSGGEAQRIRLAsqigSALV---GVMyILDEPSIGLHQRDNARLLNTLSHL-RDLGNTVIV 543
Cdd:cd03298  111 VALARVGLAGLEK-RLPGELSGGERQRVALA----RVLVrdkPVL-LLDEPFAALDPALRAEMLDLVLDLhAETKMTVLM 184
                         90       100       110
                 ....*....|....*....|....*....|...
gi 648489723 544 VEHD-EDAIRQADYVVDIgpgagrHGGQIVASG 575
Cdd:cd03298  185 VTHQpEDAKRLAQRVVFL------DNGRIAAQG 211
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
462-559 1.18e-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: 45.93  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 462 EISSRLGflndvgLDYLtLDRSADTLSGGEAQRirLAsqIGSALV--GVMYILDEPSIGL--HQRDN-ARLLNTLSHLRd 536
Cdd:COG1245  438 EIIKPLG------LEKL-LDKNVKDLSGGELQR--VA--IAACLSrdADLYLLDEPSAHLdvEQRLAvAKAIRRFAENR- 505
                         90       100
                 ....*....|....*....|...
gi 648489723 537 lGNTVIVVEHDedaIRQADYVVD 559
Cdd:COG1245  506 -GKTAMVVDHD---IYLIDYISD 524
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
824-894 1.34e-04

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 45.00  E-value: 1.34e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648489723 824 QNATTLSGGEAQRIKLARELSKRdtGRTLyILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHNLDVI 894
Cdd:PRK13638 132 QPIQCLSHGQKKRVAIAGALVLQ--ARYL-LLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLI 199
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
790-895 1.39e-04

ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 45.11  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 790 MTVEEALDFfqpVPVIHRKL----------EMLMEVGLSYIQLGQNATTLSGGEAQRIKLARELSkrdTGRTLYILDEPT 859
Cdd:COG4608  112 MTVGDIIAE---PLRIHGLAskaerrervaELLELVGLRPEHADRYPHEFSGGQRQRIGIARALA---LNPKLIVCDEPV 185
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 648489723 860 TGLhfeDI---AQLLRVLHRLRD-HGNTIVVIEHNLDVIK 895
Cdd:COG4608  186 SAL---DVsiqAQVLNLLEDLQDeLGLTYLFISHDLSVVR 222
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
440-580 1.45e-04

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 44.61  E-value: 1.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 440 QAFF----SDLQLPGRFAQIAE-KIVREISSRLGFLNDVGLDYltldRSADTLSGGEAQRIRLAsqiGSALVGVMYIL-D 513
Cdd:PRK13638  89 QIFYtdidSDIAFSLRNLGVPEaEITRRVDEALTLVDAQHFRH----QPIQCLSHGQKKRVAIA---GALVLQARYLLlD 161
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 514 EPSIGLHQRDNARLLNTLSHLRDLGNTVIVVEHDEDAIRQ---ADYVVdigpgagRHgGQIVASGTPEAV 580
Cdd:PRK13638 162 EPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEisdAVYVL-------RQ-GQILTHGAPGEV 223
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
827-893 1.52e-04

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 44.53  E-value: 1.52e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648489723 827 TTLSGGEAQRIKLARELSkrdTGRTLYILDEPTTGLHFEDIAQLLRVLHRL-RDHGNTIVVIEHNLDV 893
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLV---THPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAV 214
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
807-891 1.57e-04

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: 44.41  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  807 RKLEMLMEVGLSYIQLGQNATTLSGGEAQRIKLARELSKRDtgrTLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNT-IV 885
Cdd:TIGR02769 129 RIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKP---KLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTaYL 205

                  ....*.
gi 648489723  886 VIEHNL 891
Cdd:TIGR02769 206 FITHDL 211
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
806-892 1.60e-04

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 44.62  E-value: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 806 HRKLEMLMEVGLSYIQlGQNATTLSGGEAQRIKLARELSKRdtgRTLYILDEPTTGLHFEDIAQLLRVLHRL-RDHGNTI 884
Cdd:PRK09984 131 QRALQALTRVGMVHFA-HQRVSTLSGGQQQRVAIARALMQQ---AKVILADEPIASLDPESARIVMDTLRDInQNDGITV 206

                 ....*...
gi 648489723 885 VVIEHNLD 892
Cdd:PRK09984 207 VVTLHQVD 214
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
829-901 1.64e-04

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: 44.20  E-value: 1.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 829 LSGGEAQRIKLARelskrdtgrTL-----YIL-DEPTTGLhfeD------IAQLLRvlhRLRD-HGNTIVVIEHNLD-VI 894
Cdd:COG1127  142 LSGGMRKRVALAR---------ALaldpeILLyDEPTAGL---DpitsavIDELIR---ELRDeLGLTSVVVTHDLDsAF 206

                 ....*..
gi 648489723 895 KTADWLI 901
Cdd:COG1127  207 AIADRVA 213
cbiO PRK13643
energy-coupling factor transporter ATPase;
808-900 1.66e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 44.72  E-value: 1.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 808 KLEMlmeVGLSYIQLGQNATTLSGGEAQRIKLARELSKRDTgrtLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVI 887
Cdd:PRK13643 127 KLEM---VGLADEFWEKSPFELSGGQMRRVAIAGILAMEPE---VLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLV 200
                         90
                 ....*....|....
gi 648489723 888 EHNL-DVIKTADWL 900
Cdd:PRK13643 201 THLMdDVADYADYV 214
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
487-560 1.71e-04

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: 43.33  E-value: 1.71e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648489723 487 LSGGEAQRIRLASQIGSAlvGVMYILDEPSIGLHQRDNARLLNTLSHLRDLGN-TVIVVEHDedaIRQADYVVDI 560
Cdd:cd03222   72 LSGGELQRVAIAAALLRN--ATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHD---LAVLDYLSDR 141
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
810-903 1.80e-04

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 45.06  E-value: 1.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 810 EMLMEVGLSYIQLGQNATTLSGGEAQRIKLAREL-SKRDtgrtLYILDEPTTGLHFEDIAQLLRVlhrLRDHGNTIVVIE 888
Cdd:COG0488  134 EILSGLGFPEEDLDRPVSELSGGWRRRVALARALlSEPD----LLLLDEPTNHLDLESIEWLEEF---LKNYPGTVLVVS 206
                         90
                 ....*....|....*...
gi 648489723 889 HN---LDviKTADWLIDI 903
Cdd:COG0488  207 HDryfLD--RVATRILEL 222
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
420-546 1.97e-04

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: 43.80  E-value: 1.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 420 HVFVNDMTLPEVThmsVANAQAFFSDLQLPGRFAQiAEKIVREISSRLGFLND--VGLDYLTldrsadTLSGGEAQRIRL 497
Cdd:cd03234   85 YVRQDDILLPGLT---VRETLTYTAILRLPRKSSD-AIRKKRVEDVLLRDLALtrIGGNLVK------GISGGERRRVSI 154
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 648489723 498 ASQIgsALVGVMYILDEPSIGLHQRDNARLLNTLSHLRDLGNTVIVVEH 546
Cdd:cd03234  155 AVQL--LWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIH 201
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
461-546 2.08e-04

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: 43.31  E-value: 2.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 461 REISSRLGFL--NDVGLDYLT----LDRSAD--TLSGGEaqRIRLAsqIGSALV---GVMyILDEPSIGLHQRDNARLLN 529
Cdd:cd03213   78 RSFRKIIGYVpqDDILHPTLTvretLMFAAKlrGLSGGE--RKRVS--IALELVsnpSLL-FLDEPTSGLDSSSALQVMS 152
                         90
                 ....*....|....*..
gi 648489723 530 TLSHLRDLGNTVIVVEH 546
Cdd:cd03213  153 LLRRLADTGRTIICSIH 169
ycf16 CHL00131
sulfate ABC transporter protein; Validated
771-895 2.08e-04

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 43.86  E-value: 2.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 771 NRETLEVRYKGKNVHEVL-EMtveEALDFFQpvpVIHRKLEMlmeVGLSYIQLGQNATT-LSGGEAQR------IKLARE 842
Cdd:CHL00131 101 NADFLRLAYNSKRKFQGLpEL---DPLEFLE---IINEKLKL---VGMDPSFLSRNVNEgFSGGEKKRneilqmALLDSE 171
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 648489723 843 LSkrdtgrtlyILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHN---LDVIK 895
Cdd:CHL00131 172 LA---------ILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYqrlLDYIK 218
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
823-892 2.15e-04

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 44.21  E-value: 2.15e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648489723 823 GQNATTLSGGEAQRIKLARELSKRDtgrTLYILDEPTTGLHFEDIAQLLRVLHRL-RDHGNTIVVIEHNLD 892
Cdd:PRK10253 138 DQSVDTLSGGQRQRAWIAMVLAQET---AIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLN 205
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
807-890 2.19e-04

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 43.61  E-value: 2.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 807 RKLEMLMEVGLSYiQLGQNATTLSGGEAQRIKLARELSKRDtgrTLYILDEPTTGLHF---EDIAQLLRVLHrlRDHGNT 883
Cdd:PRK10584 126 GAKALLEQLGLGK-RLDHLPAQLSGGEQQRVALARAFNGRP---DVLFADEPTGNLDRqtgDKIADLLFSLN--REHGTT 199

                 ....*..
gi 648489723 884 IVVIEHN 890
Cdd:PRK10584 200 LILVTHD 206
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
810-892 2.21e-04

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: 43.44  E-value: 2.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 810 EMLMEVGLSYIqLGQNATTLSGGEAQRIKLARELSKRDtgrTLYILDEPTTGLHFEDIAQLLRVLHRLRDHGN-TIVVIE 888
Cdd:cd03297  114 ELLDLLGLDHL-LNRYPAQLSGGEKQRVALARALAAQP---ELLLLDEPFSALDRALRLQLLPELKQIKKNLNiPVIFVT 189

                 ....
gi 648489723 889 HNLD 892
Cdd:cd03297  190 HDLS 193
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
828-894 2.32e-04

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 44.99  E-value: 2.32e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648489723 828 TLSGGEAQRIKLARELSKRDTgrtLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHNLDVI 894
Cdd:PRK10762 141 ELSIGEQQMVEIAKVLSFESK---VIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEI 204
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
821-901 2.46e-04

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: 43.35  E-value: 2.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 821 QLGQNATTLSGGEAQRIKLARELSKRdtgRTLYILDEPTTGLhfeDIAQLLRVLHRLRD--HGNTIVVIEHNLDVIKTAD 898
Cdd:cd03245  133 QIGERGRGLSGGQRQAVALARALLND---PPILLLDEPTSAM---DMNSEERLKERLRQllGDKTLIIITHRPSLLDLVD 206

                 ...
gi 648489723 899 WLI 901
Cdd:cd03245  207 RII 209
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
470-583 2.73e-04

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: 43.71  E-value: 2.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 470 LNDVGLDYLTLDRsADTLSGGEAQRIRLAsqigSALV-GVMYIL-DEPSIGLHQRDNARLLNTLSHL-RDLGNTVIVVEH 546
Cdd:cd03256  129 LERVGLLDKAYQR-ADQLSGGQQQRVAIA----RALMqQPKLILaDEPVASLDPASSRQVMDLLKRInREEGITVIVSLH 203
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 648489723 547 DEDAIRQ-ADYVVdigpgaGRHGGQIVASGTPEAVTQH 583
Cdd:cd03256  204 QVDLAREyADRIV------GLKDGRIVFDGPPAELTDE 235
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
786-898 2.90e-04

SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 44.71  E-value: 2.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 786 EVLEMTVEEALDFFQPVPVIHRklemlMEVGLsYIQLGQNATTLSGGEAQRIKLARELSkrDTGRTLyILDEPTTGLHF- 864
Cdd:PRK10790 440 DISEEQVWQALETVQLAELARS-----LPDGL-YTPLGEQGNNLSVGQKQLLALARVLV--QTPQIL-ILDEATANIDSg 510
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 648489723 865 --EDIAQLLRVlhrLRDHgNTIVVIEHNLDVIKTAD 898
Cdd:PRK10790 511 teQAIQQALAA---VREH-TTLVVIAHRLSTIVEAD 542
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
481-593 2.94e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 43.96  E-value: 2.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 481 DRSADTLSGGEAQRIRLASQIgsALVGVMYILDEPSIGLHQRDNARLLNTLSHLRDLGNTVIVVEHDED-AIRQADYVVD 559
Cdd:PRK13647 133 DKPPYHLSYGQKKRVAIAGVL--AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDlAAEWADQVIV 210
                         90       100       110
                 ....*....|....*....|....*....|....
gi 648489723 560 IgpgagrHGGQIVASGTPEAVTQhPDSLTGAYLR 593
Cdd:PRK13647 211 L------KEGRVLAEGDKSLLTD-EDIVEQAGLR 237
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
433-586 3.01e-04

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 44.30  E-value: 3.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 433 HMSVANAQAFFSDLqLPGR----FAQIAEKIVReissrlgFLNDVGLDYLTlDRSADTLSGGEAQRIRLASQIgsALVGV 508
Cdd:PRK10851  88 HMTVFDNIAFGLTV-LPRRerpnAAAIKAKVTQ-------LLEMVQLAHLA-DRYPAQLSGGQKQRVALARAL--AVEPQ 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 509 MYILDEPSIGLHQRDNARLLNTLSHL-RDLGNTVIVVEHD-EDAIRQADYVVDIGPgagrhgGQIVASGTPEAVTQHPDS 586
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKELRRWLRQLhEELKFTSVFVTHDqEEAMEVADRVVVMSQ------GNIEQAGTPDQVWREPAT 230
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
776-900 3.19e-04

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 43.50  E-value: 3.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 776 EVRYKGKNVHEV--LEMTVEEALDFFQPVPVIH-------------------RKLEMLME-----VGL---SYIQLGQNA 826
Cdd:PRK14246  72 KVLYFGKDIFQIdaIKLRKEVGMVFQQPNPFPHlsiydniayplkshgikekREIKKIVEeclrkVGLwkeVYDRLNSPA 151
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648489723 827 TTLSGGEAQRIKLARELSKRDtgrTLYILDEPTTGLHFEDIAQLLRVLHRLRDHgNTIVVIEHN-LDVIKTADWL 900
Cdd:PRK14246 152 SQLSGGQQQRLTIARALALKP---KVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNpQQVARVADYV 222
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
777-891 3.19e-04

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: 43.32  E-value: 3.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 777 VRYKGKNVHEVLEMTVEEALdffqpvpvihRKLEMLMEVGLSyiqlgQNATTLSGGEAQRIKLARELSKRDtgrTLYILD 856
Cdd:cd03260  105 LRLHGIKLKEELDERVEEAL----------RKAALWDEVKDR-----LHALGLSGGQQQRLCLARALANEP---EVLLLD 166
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 648489723 857 EPTTGL---HFEDIAQLLRVLHrlRDHgnTIVVIEHNL 891
Cdd:cd03260  167 EPTSALdpiSTAKIEELIAELK--KEY--TIVIVTHNM 200
hmuV PRK13547
heme ABC transporter ATP-binding protein;
482-604 3.56e-04

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 43.66  E-value: 3.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 482 RSADTLSGGEAQRIRLASQIG------SALVGVMY-ILDEPSIGLHQRDNARLLNTLSHL-RDLGNTVIVVEHDED-AIR 552
Cdd:PRK13547 141 RDVTTLSGGELARVQFARVLAqlwpphDAAQPPRYlLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNlAAR 220
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 648489723 553 QADYVVDIGPGAgrhggqIVASGTPEAVTQhPDSLTGAYLRGTRCIPVPEHR 604
Cdd:PRK13547 221 HADRIAMLADGA------IVAHGAPADVLT-PAHIARCYGFAVRLVDAGDGV 265
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
487-558 3.65e-04

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: 42.56  E-value: 3.65e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648489723 487 LSGGEAQRIRLAsqigSALV---GVMyILDEPSIGLHQRDNARLLNTLSHLRD-LGNTVIVVEHD-EDAIRQADYVV 558
Cdd:cd03229  101 LSGGQQQRVALA----RALAmdpDVL-LLDEPTSALDPITRREVRALLKSLQAqLGITVVLVTHDlDEAARLADRVV 172
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
446-580 3.67e-04

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: 44.02  E-value: 3.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  446 LQLPGRFAQIAEKIVREIssrLGFLNDVGLDylTLDRSADTLSGGEAQRIRLAsqigSALVGV--MYILDEPSIGLHQRD 523
Cdd:TIGR03269 392 LELPDELARMKAVITLKM---VGFDEEKAEE--ILDKYPDELSEGERHRVALA----QVLIKEprIVILDEPTGTMDPIT 462
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 648489723  524 NARLLNTLSHLR-DLGNTVIVVEHDedairqADYVVDIGPGAG-RHGGQIVASGTPEAV 580
Cdd:TIGR03269 463 KVDVTHSILKAReEMEQTFIIVSHD------MDFVLDVCDRAAlMRDGKIVKIGDPEEI 515
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
487-578 3.70e-04

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: 42.51  E-value: 3.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 487 LSGGEAQRIRLASQIgsALVGVMYILDEPSIGLhQRDNARLL-NTLSHLRDLGNTVIVVEHDE---DAIRqADYVVDIgp 562
Cdd:cd03217  105 FSGGEKKRNEILQLL--LLEPDLAILDEPDSGL-DIDALRLVaEVINKLREEGKSVLIITHYQrllDYIK-PDRVHVL-- 178
                         90
                 ....*....|....*.
gi 648489723 563 gagrHGGQIVASGTPE 578
Cdd:cd03217  179 ----YDGRIVKSGDKE 190
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
461-549 3.74e-04

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: 42.78  E-value: 3.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 461 REISSRL-GFLNDVGLDYlTLDRSADTLSGGEAQRIRLASQIGSAlvGVMYILDEPSIGLHQRDNARLLNTLSHLRDLGN 539
Cdd:cd03292  111 REIRKRVpAALELVGLSH-KHRALPAELSGGEQQRVAIARAIVNS--PTILIADEPTGNLDPDTTWEIMNLLKKINKAGT 187
                         90
                 ....*....|
gi 648489723 540 TVIVVEHDED 549
Cdd:cd03292  188 TVVVATHAKE 197
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
829-901 4.01e-04

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 43.47  E-value: 4.01e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648489723 829 LSGGEAQRIKLARELSKRDtgrTLYILDEPTTGLHFEDIAQLLRVLHRLRDHGN-TIVVIEHNLDVIKTADWLI 901
Cdd:PRK13635 141 LSGGQKQRVAIAGVLALQP---DIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQADRVI 211
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
789-890 4.05e-04

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 42.55  E-value: 4.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 789 EMTVEEALDFFQPVPVIHRKlemlmevglsyiqlgqnATTLSGGEAQRIKLARELSkrdTGRTLYILDEPTTGLHFEDIA 868
Cdd:PRK13539 105 ELDIAAALEAVGLAPLAHLP-----------------FGYLSAGQKRRVALARLLV---SNRPIWILDEPTAALDAAAVA 164
                         90       100
                 ....*....|....*....|..
gi 648489723 869 QLLRVLHRLRDHGNTIVVIEHN 890
Cdd:PRK13539 165 LFAELIRAHLAQGGIVIAATHI 186
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
470-592 4.24e-04

leucine/isoleucine/valine transporter ATP-binding subunit; Provisional


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 43.05  E-value: 4.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 470 LNDVGLDYLTlDRSADTLSGGEAQRIRLASQIGSALVGVMyiLDEPSIGLHQRDNARLLNTLSHLRD-LGNTVIVVEHD- 547
Cdd:PRK11300 138 LERVGLLEHA-NRQAGNLAYGQQRRLEIARCMVTQPEILM--LDEPAAGLNPKETKELDELIAELRNeHNVTVLLIEHDm 214
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 648489723 548 ------EDAIrqadYVVDigpgagrHGGQIvASGTPEAVTQHPDSLTgAYL 592
Cdd:PRK11300 215 klvmgiSDRI----YVVN-------QGTPL-ANGTPEEIRNNPDVIK-AYL 252
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
474-580 4.28e-04

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 43.71  E-value: 4.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 474 GLDYLtLDRSADTLSGGEAQRIrlasQIGSALVGV--MYILDEPsigLHQRDNAR---LLNTLSHLRDLGNTVIV-VEHD 547
Cdd:PRK11144 117 GIEPL-LDRYPGSLSGGEKQRV----AIGRALLTApeLLLMDEP---LASLDLPRkreLLPYLERLAREINIPILyVSHS 188
                         90       100       110
                 ....*....|....*....|....*....|....
gi 648489723 548 EDAI-RQADYVVDIgpgagrHGGQIVASGTPEAV 580
Cdd:PRK11144 189 LDEIlRLADRVVVL------EQGKVKAFGPLEEV 216
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
804-900 4.36e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 43.25  E-value: 4.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 804 VIHRKLEMLMEVGLSYIqLGQNATTLSGGEAQRIKLARELSKRDTgrtLYILDEPTTGLHFEDIAQLLRVLHRL-RDHGN 882
Cdd:PRK13652 114 VAHRVSSALHMLGLEEL-RDRVPHHLSGGEKKRVAIAGVIAMEPQ---VLVLDEPTAGLDPQGVKELIDFLNDLpETYGM 189
                         90
                 ....*....|....*....
gi 648489723 883 TIVVIEHNLDVI-KTADWL 900
Cdd:PRK13652 190 TVIFSTHQLDLVpEMADYI 208
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
482-586 4.43e-04

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 43.67  E-value: 4.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 482 RSADTLSGGEAQRIRLASQIgsALVGVMYILDEPSIGLHQRDNARL-LNTLSHLRDLGNTVIVVEHD-EDAIRQAdyvvd 559
Cdd:PRK11607 145 RKPHQLSGGQRQRVALARSL--AKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDqEEAMTMA----- 217
                         90       100
                 ....*....|....*....|....*..
gi 648489723 560 iGPGAGRHGGQIVASGTPEAVTQHPDS 586
Cdd:PRK11607 218 -GRIAIMNRGKFVQIGEPEEIYEHPTT 243
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
433-587 4.44e-04

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 43.78  E-value: 4.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 433 HMSVANAQAFFSDLQ-LPgrFAQIAEKiVREIssrlgfLNDVGLDYLTlDRSADTLSGGEAQRIRLAsqigSALVG--VM 509
Cdd:PRK09452 100 HMTVFENVAFGLRMQkTP--AAEITPR-VMEA------LRMVQLEEFA-QRKPHQLSGGQQQRVAIA----RAVVNkpKV 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 510 YILDEPSIGLHQRDNARLLNTLSHL-RDLGNTVIVVEHD-EDAIRQADYVVDIgpgagrHGGQIVASGTPEAVTQHPDSL 587
Cdd:PRK09452 166 LLLDESLSALDYKLRKQMQNELKALqRKLGITFVFVTHDqEEALTMSDRIVVM------RDGRIEQDGTPREIYEEPKNL 239
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
432-569 4.51e-04

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: 42.67  E-value: 4.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 432 THMSVANAQAFfsdlQLPGRFAQIAEKIVREISSRLGflndvgLDYLtLDRSADTLSGGEAQRIRLASQIGS--ALVgvm 509
Cdd:cd03297   88 PHLNVRENLAF----GLKRKRNREDRISVDELLDLLG------LDHL-LNRYPAQLSGGEKQRVALARALAAqpELL--- 153
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648489723 510 yILDEPSIGLhqrDNARLLNTLSHLR----DLGNTVIVVEHD-EDAIRQADYVVDIGPGAGRHGG 569
Cdd:cd03297  154 -LLDEPFSAL---DRALRLQLLPELKqikkNLNIPVIFVTHDlSEAEYLADRIVVMEDGRLQYIG 214
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
829-892 4.70e-04

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: 42.74  E-value: 4.70e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648489723 829 LSGGEAQRIKLARELSKRDTgrtLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHNLD 892
Cdd:cd03266  137 FSTGMRQKVAIARALVHDPP---VLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQ 197
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
829-895 4.81e-04

ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 43.53  E-value: 4.81e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648489723 829 LSGGEAQRIKLARELSkrdTGRTLYILDEPTTGLHFEDIAQLLRVLHRL-RDHGNTIVVIEHNLDVIK 895
Cdd:COG1135  141 LSGGQKQRVGIARALA---NNPKVLLCDEATSALDPETTRSILDLLKDInRELGLTIVLITHEMDVVR 205
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
767-902 5.23e-04

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: 42.36  E-value: 5.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 767 GHRYNRETLEVRykgKNVHEVLEM-TVEEALDFFQPVpVIHRKL---------EMLMEVgLSYIQLGQNA----TTLSGG 832
Cdd:cd03265   61 GHDVVREPREVR---RRIGIVFQDlSVDDELTGWENL-YIHARLygvpgaerrERIDEL-LDFVGLLEAAdrlvKTYSGG 135
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648489723 833 EAQRIKLARELSKRDTgrtLYILDEPTTGLHFEDIAQLLRVLHRL-RDHGNTIVVIEHNLDvikTADWLID 902
Cdd:cd03265  136 MRRRLEIARSLVHRPE---VLFLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYME---EAEQLCD 200
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
790-936 5.36e-04

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 43.29  E-value: 5.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 790 MTVEEALDF------FQPVPVIHRKLEMLmevGLSYIQ--LGQNATTLSGGEAQRIKLARELSKRDtgrTLYILDEPTTG 861
Cdd:PRK11607 106 MTVEQNIAFglkqdkLPKAEIASRVNEML---GLVHMQefAKRKPHQLSGGQRQRVALARSLAKRP---KLLLLDEPMGA 179
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648489723 862 L--HFEDIAQlLRVLHRLRDHGNTIVVIEHNLDVIKTADWLIDIgpeggSGGGELLVAGTPEAVAGHPrshTGRFLA 936
Cdd:PRK11607 180 LdkKLRDRMQ-LEVVDILERVGVTCVMVTHDQEEAMTMAGRIAI-----MNRGKFVQIGEPEEIYEHP---TTRYSA 247
cbiO PRK13642
energy-coupling factor transporter ATPase;
791-901 5.98e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 42.77  E-value: 5.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 791 TVEEALDF---FQPVP---VIHRKLEMLMEVGLSYIQLGQNATtLSGGEAQRIKLARELSKRDTgrtLYILDEPTTGLHF 864
Cdd:PRK13642  98 TVEDDVAFgmeNQGIPreeMIKRVDEALLAVNMLDFKTREPAR-LSGGQKQRVAVAGIIALRPE---IIILDESTSMLDP 173
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 648489723 865 EDIAQLLRVLHRLRDHGN-TIVVIEHNLDVIKTADWLI 901
Cdd:PRK13642 174 TGRQEIMRVIHEIKEKYQlTVLSITHDLDEAASSDRIL 211
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
475-578 6.22e-04

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: 42.36  E-value: 6.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 475 LDYLTL----DRSADTLSGGEAQRIrlasQIGSALV---GVMYiLDEPSIGLHQRDNARLLNTLSHL-RDLGNTVIVVEH 546
Cdd:cd03265  116 LDFVGLleaaDRLVKTYSGGMRRRL----EIARSLVhrpEVLF-LDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTH 190
                         90       100       110
                 ....*....|....*....|....*....|...
gi 648489723 547 D-EDAIRQADYVVDIgpgagrHGGQIVASGTPE 578
Cdd:cd03265  191 YmEEAEQLCDRVAII------DHGRIIAEGTPE 217
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
486-578 6.27e-04

ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 43.61  E-value: 6.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 486 TLSGGEAQRIRLA------SQIgsalvgvmYILDEPSIGLhqrDN---ARLLNTLSHLRDlGNTVIVVEHDEDAIRQAD- 555
Cdd:COG1132  476 NLSGGQRQRIAIArallkdPPI--------LILDEATSAL---DTeteALIQEALERLMK-GRTTIVIAHRLSTIRNADr 543
                         90       100
                 ....*....|....*....|....
gi 648489723 556 -YVVDigpgagrhGGQIVASGTPE 578
Cdd:COG1132  544 iLVLD--------DGRIVEQGTHE 559
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
823-898 6.47e-04

Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 43.56  E-value: 6.47e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648489723  823 GQNATTLSGGEAQRIKLARELSKRDtgrTLYILDEPTTGLHfediAQLLRVLHRLRDHGN-TIVVIEHNLDVIKTAD 898
Cdd:TIGR00958 612 GEKGSQLSGGQKQRIAIARALVRKP---RVLILDEATSALD----AECEQLLQESRSRASrTVLLIAHRLSTVERAD 681
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
807-894 6.98e-04

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 43.03  E-value: 6.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 807 RKLEMLMEVGLSYIQLGQNATTLSGGEAQRIKLARELSKRDtgrTLYILDEPTTGLHFEDIAQLLRVLHRL-RDHGNTIV 885
Cdd:PRK11308 133 KALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDP---DVVVADEPVSALDVSVQAQVLNLMMDLqQELGLSYV 209

                 ....*....
gi 648489723 886 VIEHNLDVI 894
Cdd:PRK11308 210 FISHDLSVV 218
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
826-894 7.19e-04

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 43.09  E-value: 7.19e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648489723 826 ATTLSGGEAQRIKLARELSKRdtgRTLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHNLDVI 894
Cdd:COG3845  400 ARSLSGGNQQKVILARELSRD---PKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEI 465
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
487-558 7.42e-04

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: 41.26  E-value: 7.42e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648489723 487 LSGGEAQRIRLASQI--GSALVgvmyILDEPSIGLHQRDNARLLNTLSHLRDLGNTVIVVEHDEDAIRQ-ADYVV 558
Cdd:cd03216   83 LSVGERQMVEIARALarNARLL----ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVT 153
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
12-40 7.48e-04

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: 41.08  E-value: 7.48e-04
                         10        20
                 ....*....|....*....|....*....
gi 648489723  12 HNLKNVDLDLPRERLIVITGVSGSGKSSL 40
Cdd:cd00267   13 TALDNVSLTLKAGEIVALVGPNGSGKSTL 41
cbiO PRK13640
energy-coupling factor transporter ATPase;
810-901 8.26e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 42.48  E-value: 8.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 810 EMLMEVG-LSYIQlgQNATTLSGGEAQRIKLARELSkrdTGRTLYILDEPTTGLHFEDIAQLLRVLHRLRDHGN-TIVVI 887
Cdd:PRK13640 126 DVLADVGmLDYID--SEPANLSGGQKQRVAIAGILA---VEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNlTVISI 200
                         90
                 ....*....|....
gi 648489723 888 EHNLDVIKTADWLI 901
Cdd:PRK13640 201 THDIDEANMADQVL 214
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
829-927 8.52e-04

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 42.02  E-value: 8.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 829 LSGGEAQRIKLARELSKRDtgrTLYILDEPTTGLHFEDIAQLLRVLHRLRDHGN-TIVVIEHNLDVI--KTADWLIdigp 905
Cdd:PRK09544 121 LSGGETQRVLLARALLNRP---QLLVLDEPTQGVDVNGQVALYDLIDQLRRELDcAVLMVSHDLHLVmaKTDEVLC---- 193
                         90       100
                 ....*....|....*....|..
gi 648489723 906 eggsGGGELLVAGTPEAVAGHP 927
Cdd:PRK09544 194 ----LNHHICCSGTPEVVSLHP 211
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
805-894 8.58e-04

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: 42.87  E-value: 8.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  805 IHRKLEMLMEVGLSYiQLGQNATTLSGGEAQRIKLARELSKRDtgrTLYILDEPTTGLHFEdIAQLLR--VLHRLRDHGN 882
Cdd:TIGR03269 146 VGRAVDLIEMVQLSH-RITHIARDLSGGEKQRVVLARQLAKEP---FLFLADEPTGTLDPQ-TAKLVHnaLEEAVKASGI 220
                          90
                  ....*....|..
gi 648489723  883 TIVVIEHNLDVI 894
Cdd:TIGR03269 221 SMVLTSHWPEVI 232
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
776-889 8.62e-04

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 41.71  E-value: 8.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 776 EVRYKGKNVHEV------------------LEMTVEEALDFFQPvpvIHRKL------EMLMEVGLSyiqlGQN---ATT 828
Cdd:PRK13538  57 EVLWQGEPIRRQrdeyhqdllylghqpgikTELTALENLRFYQR---LHGPGddealwEALAQVGLA----GFEdvpVRQ 129
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648489723 829 LSGGEAQRIKLARELSkrdTGRTLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEH 889
Cdd:PRK13538 130 LSAGQQRRVALARLWL---TRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTH 187
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
821-901 8.91e-04

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: 43.19  E-value: 8.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  821 QLGQNATTLSGGEAQRIKLARELSkrdTGRTLYILDEPTTGLHFEDIAQLLRVLHRLRDhgNTIVVIEHNLDVIKTADWL 900
Cdd:TIGR01193 604 ELSEEGSSISGGQKQRIALARALL---TDSKVLILDESTSNLDTITEKKIVNNLLNLQD--KTIIFVAHRLSVAKQSDKI 678

                  .
gi 648489723  901 I 901
Cdd:TIGR01193 679 I 679
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
470-547 9.16e-04

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 42.22  E-value: 9.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 470 LNDVGLDYLTLDRSADTLSGGEAQRIRLASQIGSA--LVgvmyILDEPSIGLHQRDNARLLNTLSHL-RDLGNTVIVVEH 546
Cdd:PRK11701 135 LERVEIDAARIDDLPTTFSGGMQQRLQIARNLVTHprLV----FMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTH 210

                 .
gi 648489723 547 D 547
Cdd:PRK11701 211 D 211
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
822-891 9.55e-04

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 42.85  E-value: 9.55e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 822 LGQNATTLSGGEAQRIKLARELSkrdTGRTLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHNL 891
Cdd:PRK09700 403 VNQNITELSGGNQQKVLISKWLC---CCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSEL 469
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
804-891 9.90e-04

putative amino-acid ABC transporter ATP-binding protein YecC; Provisional


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 42.04  E-value: 9.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 804 VIHRKLEMLMEVGLSyiqlGQNAT---TLSGGEAQRIKLARELSKRDtgrTLYILDEPTTGLHFEDIAQLLRVLHRLRDH 880
Cdd:PRK11264 121 ATARARELLAKVGLA----GKETSyprRLSGGQQQRVAIARALAMRP---EVILFDEPTSALDPELVGEVLNTIRQLAQE 193
                         90
                 ....*....|.
gi 648489723 881 GNTIVVIEHNL 891
Cdd:PRK11264 194 KRTMVIVTHEM 204
cbiO PRK13650
energy-coupling factor transporter ATPase;
481-580 1.18e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 42.03  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 481 DRSADTLSGGEAQRIRLASQIgsALVGVMYILDEPSIGLHQRDNARLLNTLSHLRD-LGNTVIVVEHDEDAIRQADYVVD 559
Cdd:PRK13650 135 EREPARLSGGQKQRVAIAGAV--AMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdYQMTVISITHDLDEVALSDRVLV 212
                         90       100
                 ....*....|....*....|.
gi 648489723 560 IgpgagrHGGQIVASGTPEAV 580
Cdd:PRK13650 213 M------KNGQVESTSTPREL 227
cbiO PRK13641
energy-coupling factor transporter ATPase;
809-898 1.30e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 41.74  E-value: 1.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 809 LEMLMEVGLSYIQLGQNATTLSGGEAQRIKLARELSKRDTgrtLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIE 888
Cdd:PRK13641 126 LKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPE---ILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVT 202
                         90
                 ....*....|.
gi 648489723 889 HNL-DVIKTAD 898
Cdd:PRK13641 203 HNMdDVAEYAD 213
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
792-893 1.37e-03

Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 41.70  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 792 VEEALDFFQPVPVIHRKLEmlmevglsyiqlgqnatTLSGGEAQRIKLARELSKrdTGRTLyILDEPTTGLhfeDIAQLL 871
Cdd:PRK10575 128 VEEAISLVGLKPLAHRLVD-----------------SLSGGERQRAWIAMLVAQ--DSRCL-LLDEPTSAL---DIAHQV 184
                         90       100
                 ....*....|....*....|....*.
gi 648489723 872 RVL---HRL-RDHGNTIVVIEHNLDV 893
Cdd:PRK10575 185 DVLalvHRLsQERGLTVIAVLHDINM 210
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
810-895 1.37e-03

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: 42.36  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 810 EMLMEVGLSyiqlgqnATTL-------SGGEAQRIKLARELSKRDtgrTLYILDEPTTGLhfeDI---AQLLRVLHRL-R 878
Cdd:COG4172  407 EALEEVGLD-------PAARhryphefSGGQRQRIAIARALILEP---KLLVLDEPTSAL---DVsvqAQILDLLRDLqR 473
                         90
                 ....*....|....*..
gi 648489723 879 DHGNTIVVIEHNLDVIK 895
Cdd:COG4172  474 EHGLAYLFISHDLAVVR 490
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
487-580 1.40e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 41.61  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 487 LSGGEAQRIRLASQIgsALVGVMYILDEPSIGLHQRDNARLLNTLSHL-RDLGNTVIVVEHDEDAIRQADYVVDIgpgag 565
Cdd:PRK13633 145 LSGGQKQRVAIAGIL--AMRPECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVEADRIIVM----- 217
                         90
                 ....*....|....*
gi 648489723 566 rHGGQIVASGTPEAV 580
Cdd:PRK13633 218 -DSGKVVMEGTPKEI 231
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
14-41 1.51e-03

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: 39.94  E-value: 1.51e-03
                          10        20
                  ....*....|....*....|....*...
gi 648489723   14 LKNVDLDLPRERLIVITGVSGSGKSSLA 41
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLL 28
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
774-891 1.51e-03

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 41.30  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 774 TLEVRYKGKNVH----EVLEMTVEEALDFFQPVPV----------------IHRKLEMLMEVGLSYIQ----------LG 823
Cdd:PRK14239  64 TGSIVYNGHNIYsprtDTVDLRKEIGMVFQQPNPFpmsiyenvvyglrlkgIKDKQVLDEAVEKSLKGasiwdevkdrLH 143
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648489723 824 QNATTLSGGEAQRIKLARELSkrdTGRTLYILDEPTTGLHFEDIAQLLRVLHRLRDHgNTIVVIEHNL 891
Cdd:PRK14239 144 DSALGLSGGQQQRVCIARVLA---TSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSM 207
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
456-650 1.52e-03

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 42.32  E-value: 1.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 456 AEKIVREISSRLGFlndvGLDyltLDRSADTLSGGEAQR---IRLASQiGSALVgvmyILDEPSIGLHQRDNARLLNTLS 532
Cdd:COG3845  118 ARARIRELSERYGL----DVD---PDAKVEDLSVGEQQRveiLKALYR-GARIL----ILDEPTAVLTPQEADELFEILR 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 533 HLRDLGNTVIVVEHDEDAIRQ-ADYVVDIgpgagRHgGQIVASGTPEAVTqhPDSLT----GaylrgtRCIPVPEHRIEP 607
Cdd:COG3845  186 RLAAEGKSIIFITHKLREVMAiADRVTVL-----RR-GKVVGTVDTAETS--EEELAelmvG------REVLLRVEKAPA 251
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 648489723 608 DPDREI------RVIGARGNN-LKGGDFAFPTGLFTCVTGVSGSGKSTLV 650
Cdd:COG3845  252 EPGEVVlevenlSVRDDRGVPaLKDVSLEVRAGEILGIAGVAGNGQSELA 301
cbiO PRK13646
energy-coupling factor transporter ATPase;
467-580 1.53e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 41.69  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 467 LGFLNDVgldyltLDRSADTLSGGEAQRIRLASQIgsALVGVMYILDEPSIGLHQRDNARLLNTLSHLR-DLGNTVIVVE 545
Cdd:PRK13646 132 LGFSRDV------MSQSPFQMSGGQMRKIAIVSIL--AMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVS 203
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 648489723 546 HD-EDAIRQADYVVDIgpgagrHGGQIVASGTPEAV 580
Cdd:PRK13646 204 HDmNEVARYADEVIVM------KEGSIVSQTSPKEL 233
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
14-41 1.58e-03

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: 40.44  E-value: 1.58e-03
                         10        20
                 ....*....|....*....|....*...
gi 648489723  14 LKNVDLDLPRERLIVITGVSGSGKSSLA 41
Cdd:cd03228   18 LKDVSLTIKPGEKVAIVGPSGSGKSTLL 45
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
431-607 1.66e-03

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: 41.33  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  431 VTHMSVANAQAFFSDLQL-----PGRF--AQIAEKIVRE---------ISSRLG----FLNDVGLDYLTLDRSADTLSGG 490
Cdd:TIGR02769  75 LYQLDRKQRRAFRRDVQLvfqdsPSAVnpRMTVRQIIGEplrhltsldESEQKAriaeLLDMVGLRSEDADKLPRQLSGG 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723  491 EAQRIRLASQIgsALVGVMYILDEPSIGLHQRDNARLLNTLSHLRDLGNTVIV-VEHDedaIRQADYVVDigPGAGRHGG 569
Cdd:TIGR02769 155 QLQRINIARAL--AVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLfITHD---LRLVQSFCQ--RVAVMDKG 227
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 648489723  570 QIVAsgtpEAVTQHPDSLT---GAYLRGTRCIPVPEHRIEP 607
Cdd:TIGR02769 228 QIVE----ECDVAQLLSFKhpaGRNLQSAVLPEHPVRRSIT 264
CP_lyasePhnL TIGR02324
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ...
486-562 1.66e-03

phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.


Pssm-ID: 131377 [Multi-domain]  Cd Length: 224  Bit Score: 40.84  E-value: 1.66e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648489723  486 TLSGGEAQRIRLASqiGSALVGVMYILDEPSIGLHQRDNARLLNTLSHLRDLGNTVIVVEHDEDAIRQ-ADYVVDIGP 562
Cdd:TIGR02324 149 TFSGGEQQRVNIAR--GFIADYPILLLDEPTASLDAANRQVVVELIAEAKARGAALIGIFHDEEVRELvADRVMDVTP 224
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
447-547 1.94e-03

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 41.97  E-value: 1.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 447 QLPGRFAQI----AEKIVREISSRLGFLNDvgldylTLDRSADTLSGGEAQRIRLAsqigSALVG---VMyILDEPSIGL 519
Cdd:COG0488  115 ELQEEFEALggweAEARAEEILSGLGFPEE------DLDRPVSELSGGWRRRVALA----RALLSepdLL-LLDEPTNHL 183
                         90       100       110
                 ....*....|....*....|....*....|..
gi 648489723 520 hqrDnarlLNTL----SHLRDLGNTVIVVEHD 547
Cdd:COG0488  184 ---D----LESIewleEFLKNYPGTVLVVSHD 208
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
807-898 2.02e-03

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 41.33  E-value: 2.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 807 RKLEMLMEVGLS--YIQLGQNATTLSGGEAQRIKLARELSKRDTgrtLYILDEPTTGLHFEDIAQLLRVLHRLRDHGN-T 883
Cdd:PRK15093 135 RAIELLHRVGIKdhKDAMRSFPYELTEGECQKVMIAIALANQPR---LLIADEPTNAMEPTTQAQIFRLLTRLNQNNNtT 211
                         90
                 ....*....|....*.
gi 648489723 884 IVVIEHNLDVI-KTAD 898
Cdd:PRK15093 212 ILLISHDLQMLsQWAD 227
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
789-887 2.03e-03

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: 40.72  E-value: 2.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 789 EMTVEEALDF------------FQPVPVIhrKLEMLMEVGLSYIQlGQNATTLSGGEAQRIKLARELSkRDTGrtLYILD 856
Cdd:cd03234   95 GLTVRETLTYtailrlprkssdAIRKKRV--EDVLLRDLALTRIG-GNLVKGISGGERRRVSIAVQLL-WDPK--VLILD 168
                         90       100       110
                 ....*....|....*....|....*....|.
gi 648489723 857 EPTTGLHFEDIAQLLRVLHRLRdHGNTIVVI 887
Cdd:cd03234  169 EPTSGLDSFTALNLVSTLSQLA-RRNRIVIL 198
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
14-40 2.14e-03

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: 40.53  E-value: 2.14e-03
                         10        20
                 ....*....|....*....|....*..
gi 648489723  14 LKNVDLDLPRERLIVITGVSGSGKSSL 40
Cdd:cd03250   21 LKDINLEVPKGELVAIVGPVGSGKSSL 47
cbiO PRK13650
energy-coupling factor transporter ATPase;
829-898 2.29e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 40.87  E-value: 2.29e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648489723 829 LSGGEAQRIKLARELSKRDtgrTLYILDEPTTGLHFEDIAQLLRVLHRLRD-HGNTIVVIEHNLDVIKTAD 898
Cdd:PRK13650 141 LSGGQKQRVAIAGAVAMRP---KIIILDEATSMLDPEGRLELIKTIKGIRDdYQMTVISITHDLDEVALSD 208
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
821-891 2.35e-03

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 40.79  E-value: 2.35e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648489723 821 QLGQNATTLSGGEAQRIKLARELSKRDtgrTLYILDEPTTGLhfeDIAQLLRVLH-----RLRDHgNTIVVIEHNL 891
Cdd:PRK14258 143 KIHKSALDLSGGQQQRLCIARALAVKP---KVLLMDEPCFGL---DPIASMKVESliqslRLRSE-LTMVIVSHNL 211
PLN03211 PLN03211
ABC transporter G-25; Provisional
829-889 2.38e-03

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 41.79  E-value: 2.38e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648489723 829 LSGGEAQRIKLARELSkrdTGRTLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEH 889
Cdd:PLN03211 207 ISGGERKRVSIAHEML---INPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
cbiO PRK13644
energy-coupling factor transporter ATPase;
482-584 2.38e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 41.13  E-value: 2.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 482 RSADTLSGGEAQRIRLASQIgsALVGVMYILDEPSIGLHQRDNARLLNTLSHLRDLGNTVIVVEHDEDAIRQADYVVDIg 561
Cdd:PRK13644 132 RSPKTLSGGQGQCVALAGIL--TMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVM- 208
                         90       100
                 ....*....|....*....|...
gi 648489723 562 pgagrHGGQIVASGTPEAVTQHP 584
Cdd:PRK13644 209 -----DRGKIVLEGEPENVLSDV 226
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
14-41 2.62e-03

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: 40.14  E-value: 2.62e-03
                         10        20
                 ....*....|....*....|....*...
gi 648489723  14 LKNVDLDLPRERLIVITGVSGSGKSSLA 41
Cdd:cd03225   17 LDDISLTIKKGEFVLIVGPNGSGKSTLL 44
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
781-898 2.75e-03

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: 41.21  E-value: 2.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 781 GKNVHEVLE----MTVEEALDffqpvpvihRKLEMLMEVGLsyiqlgQNATT--------LSGGEAQRIKLARELSKR-D 847
Cdd:COG4172  112 GKQIAEVLRlhrgLSGAAARA---------RALELLERVGI------PDPERrldayphqLSGGQRQRVMIAMALANEpD 176
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 648489723 848 tgrtLYILDEPTTGLhfeDI---AQLLRVLHRL-RDHGNTIVVIEHNLDVI-KTAD 898
Cdd:COG4172  177 ----LLIADEPTTAL---DVtvqAQILDLLKDLqRELGMALLLITHDLGVVrRFAD 225
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
829-894 2.80e-03

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 41.15  E-value: 2.80e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648489723 829 LSGGEAQRIKLAREL-SKRDtgrtLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHNLDVI 894
Cdd:PRK10938 136 LSTGETRKTLLCQALmSEPD----LLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEI 198
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
815-898 2.81e-03

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 41.19  E-value: 2.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 815 VGLSYIQLGQNATTLSGGEAQRIKLARELSKRDtgrTLYILDEPTTGLHF---EDIAQLLRvlhRLRDHGNTIVVIEHNL 891
Cdd:PRK15439 390 LNIKFNHAEQAARTLSGGNQQKVLIAKCLEASP---QLLIVDEPTRGVDVsarNDIYQLIR---SIAAQNVAVLFISSDL 463

                 ....*...
gi 648489723 892 D-VIKTAD 898
Cdd:PRK15439 464 EeIEQMAD 471
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
826-928 3.21e-03

leucine/isoleucine/valine transporter ATP-binding subunit; Provisional


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 40.36  E-value: 3.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 826 ATTLSGGEAQRIKLARELSkrdTGRTLYILDEPTTGLH---FEDIAQLLRVLHrlRDHGNTIVVIEHNLD-VIKTADWLI 901
Cdd:PRK11300 151 AGNLAYGQQRRLEIARCMV---TQPEILMLDEPAAGLNpkeTKELDELIAELR--NEHNVTVLLIEHDMKlVMGISDRIY 225
                         90       100
                 ....*....|....*....|....*..
gi 648489723 902 DIGPEGGsgggelLVAGTPEAVAGHPR 928
Cdd:PRK11300 226 VVNQGTP------LANGTPEEIRNNPD 246
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
807-892 3.44e-03

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: 40.15  E-value: 3.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 807 RKLEMLMEVGLS-----YIQlgqnatTLSGGEAQRIKLARELSKRdtGRTLyILDEPTTGLhfeDiAQLLRVLHRL---- 877
Cdd:cd03293  111 RAEELLELVGLSgfenaYPH------QLSGGMRQRVALARALAVD--PDVL-LLDEPFSAL---D-ALTREQLQEElldi 177
                         90
                 ....*....|....*.
gi 648489723 878 -RDHGNTIVVIEHNLD 892
Cdd:cd03293  178 wRETGKTVLLVTHDID 193
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
470-575 3.50e-03

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: 39.87  E-value: 3.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 470 LNDVGLdYLTLDRSADTLSGGEAQRIRLASqigsALVG--VMYILDEPSIGLHQRDNARLLNtlsHLRDLGNTVIVV--E 545
Cdd:cd03264  115 LELVNL-GDRAKKKIGSLSGGMRRRVGIAQ----ALVGdpSILIVDEPTAGLDPEERIRFRN---LLSELGEDRIVIlsT 186
                         90       100       110
                 ....*....|....*....|....*....|.
gi 648489723 546 HD-EDAIRQADYVVDIgpgagrHGGQIVASG 575
Cdd:cd03264  187 HIvEDVESLCNQVAVL------NKGKLVFEG 211
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
828-894 3.82e-03

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 40.87  E-value: 3.82e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648489723 828 TLSGGEAQRIKLARELSKRdtgRTLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHNLDVI 894
Cdd:PRK10982 134 TLSVSQMQMIEIAKAFSYN---AKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEI 197
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
470-578 3.92e-03

ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 40.95  E-value: 3.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 470 LNDVGLDYLT--LDRSAD---TLSGGEAQRIRLAsqigSALV---GVMyILDEPSIGLhqrDNARLLNTLSHLRDL--GN 539
Cdd:COG4178  464 LEAVGLGHLAerLDEEADwdqVLSLGEQQRLAFA----RLLLhkpDWL-FLDEATSAL---DEENEAALYQLLREElpGT 535
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 648489723 540 TVIVVEHDEDAIRQADYVVDIgpgAGRHGGQIVASGTPE 578
Cdd:COG4178  536 TVISVGHRSTLAAFHDRVLEL---TGDGSWQLLPAEAPA 571
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
481-575 3.99e-03

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: 39.57  E-value: 3.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 481 DRSADTLSGGEAQRIRLASQIGS--ALVgvmyILDEPSIGLhqrD--NARLLNT-LSHLRDLGNTVIVVEHD-EDAIRQA 554
Cdd:cd03269  123 NKRVEELSKGNQQKVQFIAAVIHdpELL----ILDEPFSGL---DpvNVELLKDvIRELARAGKTVILSTHQmELVEELC 195
                         90       100
                 ....*....|....*....|.
gi 648489723 555 DYVVDIgpgagrHGGQIVASG 575
Cdd:cd03269  196 DRVLLL------NKGRAVLYG 210
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
829-895 4.14e-03

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 40.55  E-value: 4.14e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 829 LSGGEAQRIKLARELSKRDTgrtlyIL--DEPTTGLHFEDIAQLLRVLHRL-RDHGNTIVVIEHNLDVIK 895
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPK-----VLlcDEATSALDPATTRSILELLKDInRELGLTIVLITHEMDVVK 205
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
411-571 4.20e-03

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: 39.76  E-value: 4.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 411 GTRLNSAARH---VFVNDMTLPevtHMSVANAQAFfsDLQLPGRFAQIAEKIVREissrlgFLNDVGLDYlTLDRSADTL 487
Cdd:cd03293   65 GEPVTGPGPDrgyVFQQDALLP---WLTVLDNVAL--GLELQGVPKAEARERAEE------LLELVGLSG-FENAYPHQL 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 488 SGGEAQRIRLAsqigSALV---GVMyILDEPSIGL--HQRDNARLLnTLSHLRDLGNTVIVVEHD-EDAIRQADYVVDIG 561
Cdd:cd03293  133 SGGMRQRVALA----RALAvdpDVL-LLDEPFSALdaLTREQLQEE-LLDIWRETGKTVLLVTHDiDEAVFLADRVVVLS 206
                        170
                 ....*....|
gi 648489723 562 PGAGRHGGQI 571
Cdd:cd03293  207 ARPGRIVAEV 216
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
8-40 4.27e-03

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: 39.78  E-value: 4.27e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 648489723   8 GARTHNLKNVDLDLPRERLIVITGVSGSGKSSL 40
Cdd:cd03255   14 GEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTL 46
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
828-895 4.40e-03

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: 39.78  E-value: 4.40e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648489723 828 TLSGGEAQRIKLARELSKRdtgRTLYILDEPTTGLH---FEDIAQLLRVLHRLRdhGNTIVVIEHNLDVIK 895
Cdd:cd03298  128 ELSGGERQRVALARVLVRD---KPVLLLDEPFAALDpalRAEMLDLVLDLHAET--KMTVLMVTHQPEDAK 193
CxxC_CxxC_SSSS TIGR02605
putative regulatory protein, FmdB family; This model represents a region of about 50 amino ...
251-306 4.51e-03

putative regulatory protein, FmdB family; This model represents a region of about 50 amino acids found in a number of small proteins in a wide range of bacteria. The region begins usually with the initiator Met and contains two CxxC motifs separated by 17 amino acids. One member of this family is has been noted as a putative regulatory protein, designated FmdB (SP:Q50229, ). Most members of this family have a C-terminal region containing highly degenerate sequence, such as SSTSESTKSSGSSGSSGSSESKASGSTEKSTSSTTAAAAV in Mycobacterium tuberculosis and VAVGGSAPAPSPAPRAGGGGGGCCGGGCCG in Streptomyces avermitilis. These low complexity regions, which are not included in the model, resemble low-complexity C-terminal regions of some heterocycle-containing bacteriocin precursors. [Regulatory functions, DNA interactions]


Pssm-ID: 274226  Cd Length: 52  Bit Score: 36.17  E-value: 4.51e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 648489723  251 YACPVCGYALRELEPrlFSFNNPAgACPTCDGLgvrqyfDPERVVSQPALSLGGGA 306
Cdd:TIGR02605   6 YRCTACGHRFEVLQK--MSDDPLA-TCPACGGT------KLRRLLSAAGFALKGSG 52
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
810-903 4.57e-03

ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 40.56  E-value: 4.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 810 EMLMEVGLSYI--QLGQNA---TTLSGGEAQRIKLAR-ELSKRDtgrtLYILDEPTTGLhfeDIAQLLRVLHRLRDH--G 881
Cdd:COG4178  462 EALEAVGLGHLaeRLDEEAdwdQVLSLGEQQRLAFARlLLHKPD----WLFLDEATSAL---DEENEAALYQLLREElpG 534
                         90       100
                 ....*....|....*....|..
gi 648489723 882 NTIVVIEHNLDVIKTADWLIDI 903
Cdd:COG4178  535 TTVISVGHRSTLAAFHDRVLEL 556
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
470-576 4.60e-03

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 40.58  E-value: 4.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 470 LNDVGLDYL-TLDRSADT--------LSGGEAQRIRLASqigsALV--GVMYILDEPSIGLHQRDNARLLNTL-SHLRDl 537
Cdd:PRK11160 450 LQQVGLEKLlEDDKGLNAwlgeggrqLSGGEQRRLGIAR----ALLhdAPLLLLDEPTEGLDAETERQILELLaEHAQN- 524
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 648489723 538 gNTVIVVEHDEDAIRQAD--YVVDigpgagrhGGQIVASGT 576
Cdd:PRK11160 525 -KTVLMITHRLTGLEQFDriCVMD--------NGQIIEQGT 556
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
828-892 4.70e-03

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: 39.57  E-value: 4.70e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648489723 828 TLSGGEAQRIKLARELSKRDTgrtLYILDEPTTGLHFEDIAQLLRVLHRLRDHGNTIVVIEHNLD 892
Cdd:cd03269  128 ELSKGNQQKVQFIAAVIHDPE---LLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQME 189
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
481-560 4.74e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 4.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 481 DRSADTLSGGEaqRI------RLASQIgsALVGVM--YILDEPSIGLHQRDNARLLNTLS-HLRDLGNtVIVVEHDEDAI 551
Cdd:PRK03918 783 ERPLTFLSGGE--RIalglafRLALSL--YLAGNIplLILDEPTPFLDEERRRKLVDIMErYLRKIPQ-VIIVSHDEELK 857

                 ....*....
gi 648489723 552 RQADYVVDI 560
Cdd:PRK03918 858 DAADYVIRV 866
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
827-889 4.84e-03

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 40.49  E-value: 4.84e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648489723 827 TTLSGGEAQRIKLAREL-SKRDtgrtLYILDEPTTGLHFEDIAQLLRVLHrlrDHGNTIVVIEH 889
Cdd:PRK11819 162 TKLSGGERRRVALCRLLlEKPD----MLLLDEPTNHLDAESVAWLEQFLH---DYPGTVVAVTH 218
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
445-548 4.98e-03

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 39.76  E-value: 4.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 445 DLQLPGRFAQIAEKIVREISSRLgfLNDVGLDYlTLDRSADTLSGGEAQRIRLAsqigSALVGVMYIL--DEPSIGLHQR 522
Cdd:PRK10584 108 NVELPALLRGESSRQSRNGAKAL--LEQLGLGK-RLDHLPAQLSGGEQQRVALA----RAFNGRPDVLfaDEPTGNLDRQ 180
                         90       100
                 ....*....|....*....|....*..
gi 648489723 523 DNARLLNTLSHL-RDLGNTVIVVEHDE 548
Cdd:PRK10584 181 TGDKIADLLFSLnREHGTTLILVTHDL 207
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
8-40 5.60e-03

ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 39.26  E-value: 5.60e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 648489723   8 GARTHNLKNVDLDLPRERLIVITGVSGSGKSSL 40
Cdd:COG1136   18 EGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTL 50
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
807-892 6.02e-03

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: 39.55  E-value: 6.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 807 RKLEMLMEVGL-----SYIQlgqnatTLSGGEAQRIKLARELSkrdTGRTLYILDEPttglhFEDIAQLLR-----VLHR 876
Cdd:cd03294  140 RAAEALELVGLegwehKYPD------ELSGGMQQRVGLARALA---VDPDILLMDEA-----FSALDPLIRremqdELLR 205
                         90
                 ....*....|....*..
gi 648489723 877 L-RDHGNTIVVIEHNLD 892
Cdd:cd03294  206 LqAELQKTIVFITHDLD 222
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
486-564 6.59e-03

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: 39.34  E-value: 6.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 486 TLSGGEAQRIRLAsqigSALVG---VMyILDEPSIGLHQRDNARLLNTLSHLRDLGNTVIVVEHDEDAIRQ-ADYVVDIG 561
Cdd:COG4778  152 TFSGGEQQRVNIA----RGFIAdppLL-LLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAvADRVVDVT 226

                 ...
gi 648489723 562 PGA 564
Cdd:COG4778  227 PFS 229
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
788-902 7.31e-03

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 39.81  E-value: 7.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 788 LEMTVEEALDFFQPVPVIH-RKLEMLMEVGLSYIQLGQNATT----LSGGEAQRIKLARELSKRDTgrtLYILDEPTTGL 862
Cdd:PRK13536 127 LEFTVRENLLVFGRYFGMStREIEAVIPSLLEFARLESKADArvsdLSGGMKRRLTLARALINDPQ---LLILDEPTTGL 203
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 648489723 863 hfEDIAQLLrVLHRLRD---HGNTIVVIEHnldVIKTADWLID 902
Cdd:PRK13536 204 --DPHARHL-IWERLRSllaRGKTILLTTH---FMEEAERLCD 240
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
484-548 7.69e-03

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: 40.04  E-value: 7.69e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648489723  484 ADTLSGGEAQRIRLAsqigSALVG---VMyILDEPSIGLHQRDNARLLNTLSHLRDlGNTVIVVEHDE 548
Cdd:TIGR02868 469 GARLSGGERQRLALA----RALLAdapIL-LLDEPTEHLDAETADELLEDLLAALS-GRTVVLITHHL 530
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
486-563 9.99e-03

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: 38.60  E-value: 9.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489723 486 TLSGGEAQRIRLA------SQIgsalvgvmYILDEP------SIGLHQRDNArLLNTLSHLRdlgnTVIVVEHDEDAIRQ 553
Cdd:cd03250  127 NLSGGQKQRISLAravysdADI--------YLLDDPlsavdaHVGRHIFENC-ILGLLLNNK----TRILVTHQLQLLPH 193
                         90
                 ....*....|
gi 648489723 554 ADYVVDIGPG 563
Cdd:cd03250  194 ADQIVVLDNG 203
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH