NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|446585350|ref|WP_000662696|]
View 

excinuclease ABC subunit UvrA [Staphylococcus aureus]

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: 1990.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350   1 MKEPSIVVKGARAHNLKDIDIELPKNKLIVMTGLSGSGKSSLAFDTIYAEGQRRYVESLSTYARQFLGQMDKPDVDTIEG 80
Cdd:PRK00349   1 MMMDKIIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  81 LSPAISIDQKTTSKNPRSTVATVTEIYDYIRLLYARVGKPYCPNHNIEIESQTVQQMVDRIMELEARTKIQLLAPVIAHR 160
Cdd:PRK00349  81 LSPAISIDQKTTSHNPRSTVGTVTEIYDYLRLLYARVGKPHCPNCGRPIEAQTVSQMVDRVLELPEGTRLQILAPVVRGR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 161 KGSHEKLIEDIGKKGYVRLRIDGEIVDVNDVPTLDKNKNHTIEVVVDRLVVKDGIETRLADSIETALELSEGQLTVDVID 240
Cdd:PRK00349 161 KGEHKKLLENLRKQGFVRVRVDGEVYDLDEPPKLDKNKKHTIEVVVDRLVVKEDIRQRLADSIETALKLSDGLVVVEVMD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 241 G---EDLKFSESHACPICGFSIGELEPRMFSFNSPFGACPTCDGLGQKLTVDVDLVVPDKDKTLNEGAIEPWIPTSSDFY 317
Cdd:PRK00349 241 DpeaEELLFSEKFACPVCGFSIPELEPRLFSFNSPYGACPTCDGLGVKLEFDPDLVVPDPELSLAEGAIAPWSRSSSSYY 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 318 PTLLKRVCEVYKINMDKPFKKLTERQRDILLYGSGDKEIEFTFTQRQGGTRKRTMVFEGVVPNISRRFHESPSEYTREMM 397
Cdd:PRK00349 321 FQMLKSLAEHYGFDLDTPWKDLPEEVQDIILYGSGDEEIEFRYKNDRGRTRERKHPFEGVIPNLERRYRETESEYVREEL 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 398 SKYMTELPCETCHGKRLSREALSVYVGGLNIGEVVEYSISQALNYYKNIDLSEQDQAIANQILKEIISRLTFLNNVGLEY 477
Cdd:PRK00349 401 EKYMSERPCPSCKGKRLKPEALAVKVGGKNIGEVSELSIGEALEFFENLKLSEQEAKIAEPILKEIRERLKFLVDVGLDY 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 478 LTLNRASGTLSGGEAQRIRLATQIGSRLTGVLYVLDEPSIGLHQRDNDRLINTLKEMRDLGNTLIVVEHDDDTMRAADYL 557
Cdd:PRK00349 481 LTLSRSAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDEDTIRAADYI 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 558 VDIGPGAGEHGGQIVSSGTPQKVMKDKKSLTGQYLSGKKRIDVPEYRRPASDRKISIRGARSNNLKGIDVDIPLSIMTVV 637
Cdd:PRK00349 561 VDIGPGAGVHGGEVVASGTPEEIMKNPNSLTGQYLSGKKKIEVPKERRKGNGKFLKLKGARENNLKNVDVEIPLGKFTCV 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 638 TGVSGSGKSSLVNEVLYKSLAQKINKSKVKPGLYDKIEGIDQLDKIIDIDQSPIGRTPRSNPATYTGVFDDIRDVFAQTN 717
Cdd:PRK00349 641 TGVSGSGKSTLINETLYKALARKLNGAKKVPGKHKEIEGLEHLDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAGTP 720
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 718 EAKIRGYQKGRFSFNVKGGRCEACKGDGIIKIEMHFLPDVYVPCEVCDGKRYNRETLEVTYKGKNIADILEMTVEEATQF 797
Cdd:PRK00349 721 EAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEF 800
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 798 FENIPKIKRKLQTLVDVGLGYVTLGQQATTLSGGEAQRVKLASELHKRSTGKSIYILDEPTTGLHVDDISRLLKVLNRLV 877
Cdd:PRK00349 801 FEAIPKIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELSKRSTGKTLYILDEPTTGLHFEDIRKLLEVLHRLV 880
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446585350 878 ENGDTVVIIEHNLDVIKTADYIIDLGPEGGSGGGTIVATGTPEDIAQTKSSYTGKYLKEVLER 940
Cdd:PRK00349 881 DKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVATGTPEEVAKVEASYTGRYLKPVLER 943
 
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: 1990.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350   1 MKEPSIVVKGARAHNLKDIDIELPKNKLIVMTGLSGSGKSSLAFDTIYAEGQRRYVESLSTYARQFLGQMDKPDVDTIEG 80
Cdd:PRK00349   1 MMMDKIIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  81 LSPAISIDQKTTSKNPRSTVATVTEIYDYIRLLYARVGKPYCPNHNIEIESQTVQQMVDRIMELEARTKIQLLAPVIAHR 160
Cdd:PRK00349  81 LSPAISIDQKTTSHNPRSTVGTVTEIYDYLRLLYARVGKPHCPNCGRPIEAQTVSQMVDRVLELPEGTRLQILAPVVRGR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 161 KGSHEKLIEDIGKKGYVRLRIDGEIVDVNDVPTLDKNKNHTIEVVVDRLVVKDGIETRLADSIETALELSEGQLTVDVID 240
Cdd:PRK00349 161 KGEHKKLLENLRKQGFVRVRVDGEVYDLDEPPKLDKNKKHTIEVVVDRLVVKEDIRQRLADSIETALKLSDGLVVVEVMD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 241 G---EDLKFSESHACPICGFSIGELEPRMFSFNSPFGACPTCDGLGQKLTVDVDLVVPDKDKTLNEGAIEPWIPTSSDFY 317
Cdd:PRK00349 241 DpeaEELLFSEKFACPVCGFSIPELEPRLFSFNSPYGACPTCDGLGVKLEFDPDLVVPDPELSLAEGAIAPWSRSSSSYY 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 318 PTLLKRVCEVYKINMDKPFKKLTERQRDILLYGSGDKEIEFTFTQRQGGTRKRTMVFEGVVPNISRRFHESPSEYTREMM 397
Cdd:PRK00349 321 FQMLKSLAEHYGFDLDTPWKDLPEEVQDIILYGSGDEEIEFRYKNDRGRTRERKHPFEGVIPNLERRYRETESEYVREEL 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 398 SKYMTELPCETCHGKRLSREALSVYVGGLNIGEVVEYSISQALNYYKNIDLSEQDQAIANQILKEIISRLTFLNNVGLEY 477
Cdd:PRK00349 401 EKYMSERPCPSCKGKRLKPEALAVKVGGKNIGEVSELSIGEALEFFENLKLSEQEAKIAEPILKEIRERLKFLVDVGLDY 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 478 LTLNRASGTLSGGEAQRIRLATQIGSRLTGVLYVLDEPSIGLHQRDNDRLINTLKEMRDLGNTLIVVEHDDDTMRAADYL 557
Cdd:PRK00349 481 LTLSRSAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDEDTIRAADYI 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 558 VDIGPGAGEHGGQIVSSGTPQKVMKDKKSLTGQYLSGKKRIDVPEYRRPASDRKISIRGARSNNLKGIDVDIPLSIMTVV 637
Cdd:PRK00349 561 VDIGPGAGVHGGEVVASGTPEEIMKNPNSLTGQYLSGKKKIEVPKERRKGNGKFLKLKGARENNLKNVDVEIPLGKFTCV 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 638 TGVSGSGKSSLVNEVLYKSLAQKINKSKVKPGLYDKIEGIDQLDKIIDIDQSPIGRTPRSNPATYTGVFDDIRDVFAQTN 717
Cdd:PRK00349 641 TGVSGSGKSTLINETLYKALARKLNGAKKVPGKHKEIEGLEHLDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAGTP 720
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 718 EAKIRGYQKGRFSFNVKGGRCEACKGDGIIKIEMHFLPDVYVPCEVCDGKRYNRETLEVTYKGKNIADILEMTVEEATQF 797
Cdd:PRK00349 721 EAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEF 800
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 798 FENIPKIKRKLQTLVDVGLGYVTLGQQATTLSGGEAQRVKLASELHKRSTGKSIYILDEPTTGLHVDDISRLLKVLNRLV 877
Cdd:PRK00349 801 FEAIPKIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELSKRSTGKTLYILDEPTTGLHFEDIRKLLEVLHRLV 880
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446585350 878 ENGDTVVIIEHNLDVIKTADYIIDLGPEGGSGGGTIVATGTPEDIAQTKSSYTGKYLKEVLER 940
Cdd:PRK00349 881 DKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVATGTPEEVAKVEASYTGRYLKPVLER 943
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
1-942 0e+00

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


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 1926.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350   1 MKEPSIVVKGARAHNLKDIDIELPKNKLIVMTGLSGSGKSSLAFDTIYAEGQRRYVESLSTYARQFLGQMDKPDVDTIEG 80
Cdd:COG0178    1 MMMDKIRIRGAREHNLKNIDVDIPRNKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  81 LSPAISIDQKTTSKNPRSTVATVTEIYDYIRLLYARVGKPYCPNHNIEIESQTVQQMVDRIMELEARTKIQLLAPVIAHR 160
Cdd:COG0178   81 LSPAISIEQKTTSRNPRSTVGTVTEIYDYLRLLFARVGTPHCPICGRPVEKQTVDQIVDRILALPEGTRLQILAPVVRGR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 161 KGSHEKLIEDIGKKGYVRLRIDGEIVDVNDVPTLDKNKNHTIEVVVDRLVVKDGIETRLADSIETALELSEGQLTVDVID 240
Cdd:COG0178  161 KGEHKELLEELRKQGFVRVRVDGEVYDLDEEPELDKNKKHTIEVVVDRLVVKEDIRSRLADSVETALKLGDGLVIVEVVD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 241 -GEDLKFSESHACPICGFSIGELEPRMFSFNSPFGACPTCDGLGQKLTVDVDLVVPDKDKTLNEGAIEPWIPTSSDFYPT 319
Cdd:COG0178  241 eGEELLFSEKFACPDCGISFEELEPRLFSFNSPYGACPTCDGLGRVLEFDPDLVIPDPSLSLAEGAIAPWSGPSSSYYFQ 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 320 LLKRVCEVYKINMDKPFKKLTERQRDILLYGSGDKeIEFTFTQRqGGTRKRTMVFEGVVPNISRRFHESPSEYTREMMSK 399
Cdd:COG0178  321 LLEALAKHYGFDLDTPWKDLPEEQRDLILYGSDEK-IKFRYKNR-GRRRTYEKPFEGVIPFLERRYRETYSEHVREELSR 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 400 YMTELPCETCHGKRLSREALSVYVGGLNIGEVVEYSISQALNYYKNIDLSEQDQAIANQILKEIISRLTFLNNVGLEYLT 479
Cdd:COG0178  399 YMSETPCPACKGARLKPEALAVKIGGKNIAELTALSIDEALEFFENLELTEREAEIAERILKEIRSRLGFLVDVGLDYLT 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 480 LNRASGTLSGGEAQRIRLATQIGSRLTGVLYVLDEPSIGLHQRDNDRLINTLKEMRDLGNTLIVVEHDDDTMRAADYLVD 559
Cdd:COG0178  479 LDRSAGTLSGGEAQRIRLATQIGSGLVGVLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDTIRAADYIID 558
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 560 IGPGAGEHGGQIVSSGTPQKVMKDKKSLTGQYLSGKKRIDVPEYRRPASDRKISIRGARSNNLKGIDVDIPLSIMTVVTG 639
Cdd:COG0178  559 IGPGAGEHGGEVVAQGTPEEILKNPDSLTGQYLSGRKRIPVPKKRRKGNGKFLTIKGARENNLKNVDVEIPLGVLTCVTG 638
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 640 VSGSGKSSLVNEVLYKSLAQKINKSKVKPGLYDKIEGIDQLDKIIDIDQSPIGRTPRSNPATYTGVFDDIRDVFAQTNEA 719
Cdd:COG0178  639 VSGSGKSTLVNDILYPALARKLNGAKEKPGPHDSIEGLEHIDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAQTPEA 718
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 720 KIRGYQKGRFSFNVKGGRCEACKGDGIIKIEMHFLPDVYVPCEVCDGKRYNRETLEVTYKGKNIADILEMTVEEATQFFE 799
Cdd:COG0178  719 KARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEFFE 798
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 800 NIPKIKRKLQTLVDVGLGYVTLGQQATTLSGGEAQRVKLASELHKRSTGKSIYILDEPTTGLHVDDISRLLKVLNRLVEN 879
Cdd:COG0178  799 NIPKIARKLQTLQDVGLGYIKLGQPATTLSGGEAQRVKLASELSKRSTGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDK 878
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446585350 880 GDTVVIIEHNLDVIKTADYIIDLgpeggsgggTIVATGTPEDIAQTKSSYTGKYLKEVLERDK 942
Cdd:COG0178  879 GNTVVVIEHNLDVIKTADWIIDLgpeggdgggEIVAEGTPEEVAKVKASYTGRYLKEYLEAAR 941
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
6-923 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: 1558.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350    6 IVVKGARAHNLKDIDIELPKNKLIVMTGLSGSGKSSLAFDTIYAEGQRRYVESLSTYARQFLGQMDKPDVDTIEGLSPAI 85
Cdd:TIGR00630   2 IIVRGAREHNLKNIDVEIPRDKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGVMDKPDVDSIEGLSPAI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350   86 SIDQKTTSKNPRSTVATVTEIYDYIRLLYARVGKPYCPNHNIEIESQTVQQMVDRIMELEARTKIQLLAPVIAHRKGSHE 165
Cdd:TIGR00630  82 SIDQKTTSHNPRSTVGTITEIYDYLRLLFARVGTPYCPTCGRPISRQTPSQIVDQILALPEGTRVILLAPIVRGRKGEFR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  166 KLIEDIGKKGYVRLRIDGEIVDVNDVPTLDKNKNHTIEVVVDRLVVKDGIETRLADSIETALELSEGQLTVDVIDGEDL- 244
Cdd:TIGR00630 162 KLLEKLRKQGFARVRVDGEVYPLEDPPKLEKNKKHTIDVVIDRLTVKNENRSRLAESVETALRLGDGLLEVEFDDDEEVa 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  245 -----KFSESHACPICGFSIGELEPRMFSFNSPFGACPTCDGLGQKLTVDVDLVVPDKDKTLNEGAIEPWIPTSSDFYPT 319
Cdd:TIGR00630 242 eskeeLFSEKFACPECGFSLPELEPRLFSFNSPYGACPECSGLGIKQEFDPELIIPDPLLSLNGGAIVPFKKSTTSYYRQ 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  320 LLKRVCEVYKINMDKPFKKLTERQRDILLYGSGDKEIEFTFTQRQGGTRKRTMVFEGVVPNISRRFHESPSEYTREMMSK 399
Cdd:TIGR00630 322 MFASLAEHLGFDLDTPWKDLPEEAQKAILYGSGEEVIVVKYRNGGGETFRYHKPFEGVIPELERRYLETESESMREYLEK 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  400 YMTELPCETCHGKRLSREALSVYVGGLNIGEVVEYSISQALNYYKNIDLSEQDQAIANQILKEIISRLTFLNNVGLEYLT 479
Cdd:TIGR00630 402 FMSERPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFNQLTLTPEEKKIAEEVLKEIRERLGFLIDVGLDYLS 481
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  480 LNRASGTLSGGEAQRIRLATQIGSRLTGVLYVLDEPSIGLHQRDNDRLINTLKEMRDLGNTLIVVEHDDDTMRAADYLVD 559
Cdd:TIGR00630 482 LSRAAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVID 561
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  560 IGPGAGEHGGQIVSSGTPQKVMKDKKSLTGQYLSGKKRIDVPEYRRPASDRKISIRGARSNNLKGIDVDIPLSIMTVVTG 639
Cdd:TIGR00630 562 IGPGAGEHGGEVVASGTPEEILANPDSLTGQYLSGRKKIEVPAERRPGNGKFLTLKGARENNLKNITVSIPLGLFTCITG 641
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  640 VSGSGKSSLVNEVLYKSLAQKINKSKVKPGLYDKIEGIDQLDKIIDIDQSPIGRTPRSNPATYTGVFDDIRDVFAQTNEA 719
Cdd:TIGR00630 642 VSGSGKSTLINDTLYPALANRLNGAKTVPGRYTSIEGLEHLDKVIHIDQSPIGRTPRSNPATYTGVFDEIRELFAETPEA 721
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  720 KIRGYQKGRFSFNVKGGRCEACKGDGIIKIEMHFLPDVYVPCEVCDGKRYNRETLEVTYKGKNIADILEMTVEEATQFFE 799
Cdd:TIGR00630 722 KVRGYTPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEAYEFFE 801
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  800 NIPKIKRKLQTLVDVGLGYVTLGQQATTLSGGEAQRVKLASELHKRSTGKSIYILDEPTTGLHVDDISRLLKVLNRLVEN 879
Cdd:TIGR00630 802 AVPSISRKLQTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKRSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDK 881
                         890       900       910       920
                  ....*....|....*....|....*....|....*....|....
gi 446585350  880 GDTVVIIEHNLDVIKTADYIIDLGPEGGSGGGTIVATGTPEDIA 923
Cdd:TIGR00630 882 GNTVVVIEHNLDVIKTADYIIDLGPEGGDGGGTVVASGTPEEVA 925
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
612-919 1.25e-155

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: 458.23  E-value: 1.25e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 612 ISIRGARSNNLKGIDVDIPLSIMTVVTGVSGSGKSSLVNEVLYKSLAQKINKSKVKPGLYDKIEGIDQLDKIIDIDQSPI 691
Cdd:cd03271    1 LTLKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPALARRLHLKKEQPGNHDRIEGLEHIDKVIVIDQSPI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 692 GRTPRSNPATYTGVFDDIRDVFaqtneakirgyqkgrfsfnvkggrceackgdgiikiemhflpdvyvpCEVCDGKRYNR 771
Cdd:cd03271   81 GRTPRSNPATYTGVFDEIRELF-----------------------------------------------CEVCKGKRYNR 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 772 ETLEVTYKGKNIADILEMTVEEATQFFENIPKIKRKLQTLVDVGLGYVTLGQQATTLSGGEAQRVKLASELHKRSTGKSI 851
Cdd:cd03271  114 ETLEVRYKGKSIADVLDMTVEEALEFFENIPKIARKLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRSTGKTL 193
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446585350 852 YILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHNLDVIKTADYIIDLGPEGGSGGGTIVATGTP 919
Cdd:cd03271  194 YILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLGPEGGDGGGQVVASGTP 261
UvrA_inter pfam17760
UvrA interaction domain; This domain found in UvrA proteins interacts with the UvrB protein.
132-240 7.17e-50

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


Pssm-ID: 436020 [Multi-domain]  Cd Length: 109  Bit Score: 171.12  E-value: 7.17e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  132 QTVQQMVDRIMELEARTKIQLLAPVIAHRKGSHEKLIEDIGKKGYVRLRIDGEIVDVNDVPTLDKNKNHTIEVVVDRLVV 211
Cdd:pfam17760   1 QTVDQIVDRILALPEGTKIQILAPVVRGRKGEHKELLDDLRKQGFVRVRVDGEIYDLDDEPKLDKNKKHTIEVVVDRLVV 80
                          90       100
                  ....*....|....*....|....*....
gi 446585350  212 KDGIETRLADSIETALELSEGQLTVDVID 240
Cdd:pfam17760  81 KEDNRSRLADSVETALKLGKGLVIVLVLD 109
GguA NF040905
sugar ABC transporter ATP-binding protein;
820-886 6.45e-03

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 40.16  E-value: 6.45e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446585350 820 TLGQQATTLSGGEAQRVKLASELHkrsTGKSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVII 886
Cdd:NF040905 397 SVFQKVGNLSGGNQQKVVLSKWLF---TDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVI 460
 
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: 1990.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350   1 MKEPSIVVKGARAHNLKDIDIELPKNKLIVMTGLSGSGKSSLAFDTIYAEGQRRYVESLSTYARQFLGQMDKPDVDTIEG 80
Cdd:PRK00349   1 MMMDKIIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  81 LSPAISIDQKTTSKNPRSTVATVTEIYDYIRLLYARVGKPYCPNHNIEIESQTVQQMVDRIMELEARTKIQLLAPVIAHR 160
Cdd:PRK00349  81 LSPAISIDQKTTSHNPRSTVGTVTEIYDYLRLLYARVGKPHCPNCGRPIEAQTVSQMVDRVLELPEGTRLQILAPVVRGR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 161 KGSHEKLIEDIGKKGYVRLRIDGEIVDVNDVPTLDKNKNHTIEVVVDRLVVKDGIETRLADSIETALELSEGQLTVDVID 240
Cdd:PRK00349 161 KGEHKKLLENLRKQGFVRVRVDGEVYDLDEPPKLDKNKKHTIEVVVDRLVVKEDIRQRLADSIETALKLSDGLVVVEVMD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 241 G---EDLKFSESHACPICGFSIGELEPRMFSFNSPFGACPTCDGLGQKLTVDVDLVVPDKDKTLNEGAIEPWIPTSSDFY 317
Cdd:PRK00349 241 DpeaEELLFSEKFACPVCGFSIPELEPRLFSFNSPYGACPTCDGLGVKLEFDPDLVVPDPELSLAEGAIAPWSRSSSSYY 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 318 PTLLKRVCEVYKINMDKPFKKLTERQRDILLYGSGDKEIEFTFTQRQGGTRKRTMVFEGVVPNISRRFHESPSEYTREMM 397
Cdd:PRK00349 321 FQMLKSLAEHYGFDLDTPWKDLPEEVQDIILYGSGDEEIEFRYKNDRGRTRERKHPFEGVIPNLERRYRETESEYVREEL 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 398 SKYMTELPCETCHGKRLSREALSVYVGGLNIGEVVEYSISQALNYYKNIDLSEQDQAIANQILKEIISRLTFLNNVGLEY 477
Cdd:PRK00349 401 EKYMSERPCPSCKGKRLKPEALAVKVGGKNIGEVSELSIGEALEFFENLKLSEQEAKIAEPILKEIRERLKFLVDVGLDY 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 478 LTLNRASGTLSGGEAQRIRLATQIGSRLTGVLYVLDEPSIGLHQRDNDRLINTLKEMRDLGNTLIVVEHDDDTMRAADYL 557
Cdd:PRK00349 481 LTLSRSAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDEDTIRAADYI 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 558 VDIGPGAGEHGGQIVSSGTPQKVMKDKKSLTGQYLSGKKRIDVPEYRRPASDRKISIRGARSNNLKGIDVDIPLSIMTVV 637
Cdd:PRK00349 561 VDIGPGAGVHGGEVVASGTPEEIMKNPNSLTGQYLSGKKKIEVPKERRKGNGKFLKLKGARENNLKNVDVEIPLGKFTCV 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 638 TGVSGSGKSSLVNEVLYKSLAQKINKSKVKPGLYDKIEGIDQLDKIIDIDQSPIGRTPRSNPATYTGVFDDIRDVFAQTN 717
Cdd:PRK00349 641 TGVSGSGKSTLINETLYKALARKLNGAKKVPGKHKEIEGLEHLDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAGTP 720
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 718 EAKIRGYQKGRFSFNVKGGRCEACKGDGIIKIEMHFLPDVYVPCEVCDGKRYNRETLEVTYKGKNIADILEMTVEEATQF 797
Cdd:PRK00349 721 EAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEF 800
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 798 FENIPKIKRKLQTLVDVGLGYVTLGQQATTLSGGEAQRVKLASELHKRSTGKSIYILDEPTTGLHVDDISRLLKVLNRLV 877
Cdd:PRK00349 801 FEAIPKIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELSKRSTGKTLYILDEPTTGLHFEDIRKLLEVLHRLV 880
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446585350 878 ENGDTVVIIEHNLDVIKTADYIIDLGPEGGSGGGTIVATGTPEDIAQTKSSYTGKYLKEVLER 940
Cdd:PRK00349 881 DKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVATGTPEEVAKVEASYTGRYLKPVLER 943
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
1-942 0e+00

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


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 1926.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350   1 MKEPSIVVKGARAHNLKDIDIELPKNKLIVMTGLSGSGKSSLAFDTIYAEGQRRYVESLSTYARQFLGQMDKPDVDTIEG 80
Cdd:COG0178    1 MMMDKIRIRGAREHNLKNIDVDIPRNKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  81 LSPAISIDQKTTSKNPRSTVATVTEIYDYIRLLYARVGKPYCPNHNIEIESQTVQQMVDRIMELEARTKIQLLAPVIAHR 160
Cdd:COG0178   81 LSPAISIEQKTTSRNPRSTVGTVTEIYDYLRLLFARVGTPHCPICGRPVEKQTVDQIVDRILALPEGTRLQILAPVVRGR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 161 KGSHEKLIEDIGKKGYVRLRIDGEIVDVNDVPTLDKNKNHTIEVVVDRLVVKDGIETRLADSIETALELSEGQLTVDVID 240
Cdd:COG0178  161 KGEHKELLEELRKQGFVRVRVDGEVYDLDEEPELDKNKKHTIEVVVDRLVVKEDIRSRLADSVETALKLGDGLVIVEVVD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 241 -GEDLKFSESHACPICGFSIGELEPRMFSFNSPFGACPTCDGLGQKLTVDVDLVVPDKDKTLNEGAIEPWIPTSSDFYPT 319
Cdd:COG0178  241 eGEELLFSEKFACPDCGISFEELEPRLFSFNSPYGACPTCDGLGRVLEFDPDLVIPDPSLSLAEGAIAPWSGPSSSYYFQ 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 320 LLKRVCEVYKINMDKPFKKLTERQRDILLYGSGDKeIEFTFTQRqGGTRKRTMVFEGVVPNISRRFHESPSEYTREMMSK 399
Cdd:COG0178  321 LLEALAKHYGFDLDTPWKDLPEEQRDLILYGSDEK-IKFRYKNR-GRRRTYEKPFEGVIPFLERRYRETYSEHVREELSR 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 400 YMTELPCETCHGKRLSREALSVYVGGLNIGEVVEYSISQALNYYKNIDLSEQDQAIANQILKEIISRLTFLNNVGLEYLT 479
Cdd:COG0178  399 YMSETPCPACKGARLKPEALAVKIGGKNIAELTALSIDEALEFFENLELTEREAEIAERILKEIRSRLGFLVDVGLDYLT 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 480 LNRASGTLSGGEAQRIRLATQIGSRLTGVLYVLDEPSIGLHQRDNDRLINTLKEMRDLGNTLIVVEHDDDTMRAADYLVD 559
Cdd:COG0178  479 LDRSAGTLSGGEAQRIRLATQIGSGLVGVLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDTIRAADYIID 558
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 560 IGPGAGEHGGQIVSSGTPQKVMKDKKSLTGQYLSGKKRIDVPEYRRPASDRKISIRGARSNNLKGIDVDIPLSIMTVVTG 639
Cdd:COG0178  559 IGPGAGEHGGEVVAQGTPEEILKNPDSLTGQYLSGRKRIPVPKKRRKGNGKFLTIKGARENNLKNVDVEIPLGVLTCVTG 638
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 640 VSGSGKSSLVNEVLYKSLAQKINKSKVKPGLYDKIEGIDQLDKIIDIDQSPIGRTPRSNPATYTGVFDDIRDVFAQTNEA 719
Cdd:COG0178  639 VSGSGKSTLVNDILYPALARKLNGAKEKPGPHDSIEGLEHIDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAQTPEA 718
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 720 KIRGYQKGRFSFNVKGGRCEACKGDGIIKIEMHFLPDVYVPCEVCDGKRYNRETLEVTYKGKNIADILEMTVEEATQFFE 799
Cdd:COG0178  719 KARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEFFE 798
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 800 NIPKIKRKLQTLVDVGLGYVTLGQQATTLSGGEAQRVKLASELHKRSTGKSIYILDEPTTGLHVDDISRLLKVLNRLVEN 879
Cdd:COG0178  799 NIPKIARKLQTLQDVGLGYIKLGQPATTLSGGEAQRVKLASELSKRSTGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDK 878
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446585350 880 GDTVVIIEHNLDVIKTADYIIDLgpeggsgggTIVATGTPEDIAQTKSSYTGKYLKEVLERDK 942
Cdd:COG0178  879 GNTVVVIEHNLDVIKTADWIIDLgpeggdgggEIVAEGTPEEVAKVKASYTGRYLKEYLEAAR 941
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
6-923 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: 1558.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350    6 IVVKGARAHNLKDIDIELPKNKLIVMTGLSGSGKSSLAFDTIYAEGQRRYVESLSTYARQFLGQMDKPDVDTIEGLSPAI 85
Cdd:TIGR00630   2 IIVRGAREHNLKNIDVEIPRDKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGVMDKPDVDSIEGLSPAI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350   86 SIDQKTTSKNPRSTVATVTEIYDYIRLLYARVGKPYCPNHNIEIESQTVQQMVDRIMELEARTKIQLLAPVIAHRKGSHE 165
Cdd:TIGR00630  82 SIDQKTTSHNPRSTVGTITEIYDYLRLLFARVGTPYCPTCGRPISRQTPSQIVDQILALPEGTRVILLAPIVRGRKGEFR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  166 KLIEDIGKKGYVRLRIDGEIVDVNDVPTLDKNKNHTIEVVVDRLVVKDGIETRLADSIETALELSEGQLTVDVIDGEDL- 244
Cdd:TIGR00630 162 KLLEKLRKQGFARVRVDGEVYPLEDPPKLEKNKKHTIDVVIDRLTVKNENRSRLAESVETALRLGDGLLEVEFDDDEEVa 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  245 -----KFSESHACPICGFSIGELEPRMFSFNSPFGACPTCDGLGQKLTVDVDLVVPDKDKTLNEGAIEPWIPTSSDFYPT 319
Cdd:TIGR00630 242 eskeeLFSEKFACPECGFSLPELEPRLFSFNSPYGACPECSGLGIKQEFDPELIIPDPLLSLNGGAIVPFKKSTTSYYRQ 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  320 LLKRVCEVYKINMDKPFKKLTERQRDILLYGSGDKEIEFTFTQRQGGTRKRTMVFEGVVPNISRRFHESPSEYTREMMSK 399
Cdd:TIGR00630 322 MFASLAEHLGFDLDTPWKDLPEEAQKAILYGSGEEVIVVKYRNGGGETFRYHKPFEGVIPELERRYLETESESMREYLEK 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  400 YMTELPCETCHGKRLSREALSVYVGGLNIGEVVEYSISQALNYYKNIDLSEQDQAIANQILKEIISRLTFLNNVGLEYLT 479
Cdd:TIGR00630 402 FMSERPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFNQLTLTPEEKKIAEEVLKEIRERLGFLIDVGLDYLS 481
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  480 LNRASGTLSGGEAQRIRLATQIGSRLTGVLYVLDEPSIGLHQRDNDRLINTLKEMRDLGNTLIVVEHDDDTMRAADYLVD 559
Cdd:TIGR00630 482 LSRAAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVID 561
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  560 IGPGAGEHGGQIVSSGTPQKVMKDKKSLTGQYLSGKKRIDVPEYRRPASDRKISIRGARSNNLKGIDVDIPLSIMTVVTG 639
Cdd:TIGR00630 562 IGPGAGEHGGEVVASGTPEEILANPDSLTGQYLSGRKKIEVPAERRPGNGKFLTLKGARENNLKNITVSIPLGLFTCITG 641
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  640 VSGSGKSSLVNEVLYKSLAQKINKSKVKPGLYDKIEGIDQLDKIIDIDQSPIGRTPRSNPATYTGVFDDIRDVFAQTNEA 719
Cdd:TIGR00630 642 VSGSGKSTLINDTLYPALANRLNGAKTVPGRYTSIEGLEHLDKVIHIDQSPIGRTPRSNPATYTGVFDEIRELFAETPEA 721
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  720 KIRGYQKGRFSFNVKGGRCEACKGDGIIKIEMHFLPDVYVPCEVCDGKRYNRETLEVTYKGKNIADILEMTVEEATQFFE 799
Cdd:TIGR00630 722 KVRGYTPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEAYEFFE 801
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  800 NIPKIKRKLQTLVDVGLGYVTLGQQATTLSGGEAQRVKLASELHKRSTGKSIYILDEPTTGLHVDDISRLLKVLNRLVEN 879
Cdd:TIGR00630 802 AVPSISRKLQTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKRSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDK 881
                         890       900       910       920
                  ....*....|....*....|....*....|....*....|....
gi 446585350  880 GDTVVIIEHNLDVIKTADYIIDLGPEGGSGGGTIVATGTPEDIA 923
Cdd:TIGR00630 882 GNTVVVIEHNLDVIKTADYIIDLGPEGGDGGGTVVASGTPEEVA 925
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
4-942 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 446585350    4 PSIVVK--GARAHNLKDIDIELPKNKLIVMTGLSGSGKSSLAFDTIYAEGQRRYVESLSTYARQFLGQMDKPDVDTIEGL 81
Cdd:PRK00635    2 PSLPVRlsGITVRNLKNISIEFCPREIVLLTGVSGSGKSSLAFDTIYAAGRKRYLSTLPSFFATTLDSLPDPSVEKIEGL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350   82 SPAISIDQKTTSKNPRSTVATVTEIYDYIRLLYARVGKPYCPNHNIEIESQTVQQMVDRIMELEARTKIQLLAPVIAHRK 161
Cdd:PRK00635   82 SPTIAVKQNHFSQHSHATVGSTTELNSHLALLFSLEGQARDPVTLHPLTLYSKEKILSTIAAIPDGTQITLLAPLPAKDI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  162 GSheklIEDIGKKGYVRLRIDGEIVDVNDVPTLDKNKNHTIEVVVDRLVVKDGIETRLADSIETALELSEGQLTVDViDG 241
Cdd:PRK00635  162 LA----IRECLRQGFTKVRIDGEISPIYKFLTSGIPEDVPVDIVVDTLIKNESNTARLKVSLFTALDIGHGECSLHF-DN 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  242 EDLKFSESHACPICGFSIGELEPRMFSFNSPFGACPTCDGLGQKLTVDvDLVVPDKDKTLNEGAIEPWIPTSSDFYPTLL 321
Cdd:PRK00635  237 QKRTFSTQATIPETQQTYTPLTPQLFSPHSLEDRCPQCQGSGIFISID-DPSLIQQNLSIEENCCPFAGNCSTYLYHTIY 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  322 KRVCEVYKINMDKPFKKLTERQRDILLYGSGDKEIEFT-FTQRQGGTRKRTMVFEGVVPNISR--RFHESPSEYtremMS 398
Cdd:PRK00635  316 QSLADSLGFSLSTPWKDLSPEIQNIFLYGKEGLVLPVRlFDGTLGKKTLTHKVWRGVLNEIGEkvRYSNKPSRY----LP 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  399 KYMTELPCETCHGKRLSREALSVYVGGLNIGEVVEYSISQALNYYKNIdlSEQDQAIaNQILKEIISRLTFLNNVGLEYL 478
Cdd:PRK00635  392 KGTSATSCPRCQGTGLGDYANAATWHGKTFAEFQQMSLQELFIFLSQL--PSKSLSI-EEVLQGLKSRLSILIDLGLPYL 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  479 TLNRASGTLSGGEAQRIRLATQIGSRLTGVLYVLDEPSIGLHQRDNDRLINTLKEMRDLGNTLIVVEHDDDTMRAADYLV 558
Cdd:PRK00635  469 TPERALATLSGGEQERTALAKHLGAELIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMISLADRII 548
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  559 DIGPGAGEHGGQIVSSGTPQKVMKDKKSLTGQYLSGKKRIDVPEyRRPASDRKISIRGARSNNLKGIDVDIPLSIMTVVT 638
Cdd:PRK00635  549 DIGPGAGIFGGEVLFNGSPREFLAKSDSLTAKYLRQELTIPIPE-KRTNSLGTLTLSKATKHNLKDLTISLPLGRLTVVT 627
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  639 GVSGSGKSSLVNEVLYKSLAQKInKSKVKPGLYdkIEGiDQLDKIIDIDQSPIGRTPRSNPATYTGVFDDIRDVFAQTNE 718
Cdd:PRK00635  628 GVSGSGKSSLINDTLVPAVEEFI-EQGFCSNLS--IQW-GAISRLVHITRDLPGRSQRSIPLTYIKAFDDLRELFAEQPR 703
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  719 AKIRGYQKGRFSFNVKGGRCEACKGDGIIKIEMHFLPdvyVPCEVCDGKRYNRETLEVTYKGKNIADILEMTVEEATQFF 798
Cdd:PRK00635  704 SKRLGLTKSHFSFNTPLGACAECQGLGSITTTDNRTS---IPCPSCLGKRFLPQVLEVRYKGKNIADILEMTAYEAEKFF 780
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  799 ENIPKIKRKLQTLVDVGLGYVTLGQQATTLSGGEAQRVKLASELHKRSTGKSIYILDEPTTGLHVDDISRLLKVLNRLVE 878
Cdd:PRK00635  781 LDEPSIHEKIHALCSLGLDYLPLGRPLSSLSGGEIQRLKLAYELLAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTH 860
                         890       900       910       920       930       940
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446585350  879 NGDTVVIIEHNLDVIKTADYIIDLGPEGGSGGGTIVATGTPEDIAQtKSSYTGKYLKEVLERDK 942
Cdd:PRK00635  861 QGHTVVIIEHNMHVVKVADYVLELGPEGGNLGGYLLASCSPEELIH-LHTPTAKALRPYLSSPQ 923
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
612-919 1.25e-155

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: 458.23  E-value: 1.25e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 612 ISIRGARSNNLKGIDVDIPLSIMTVVTGVSGSGKSSLVNEVLYKSLAQKINKSKVKPGLYDKIEGIDQLDKIIDIDQSPI 691
Cdd:cd03271    1 LTLKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPALARRLHLKKEQPGNHDRIEGLEHIDKVIVIDQSPI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 692 GRTPRSNPATYTGVFDDIRDVFaqtneakirgyqkgrfsfnvkggrceackgdgiikiemhflpdvyvpCEVCDGKRYNR 771
Cdd:cd03271   81 GRTPRSNPATYTGVFDEIRELF-----------------------------------------------CEVCKGKRYNR 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 772 ETLEVTYKGKNIADILEMTVEEATQFFENIPKIKRKLQTLVDVGLGYVTLGQQATTLSGGEAQRVKLASELHKRSTGKSI 851
Cdd:cd03271  114 ETLEVRYKGKSIADVLDMTVEEALEFFENIPKIARKLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRSTGKTL 193
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446585350 852 YILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHNLDVIKTADYIIDLGPEGGSGGGTIVATGTP 919
Cdd:cd03271  194 YILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLGPEGGDGGGQVVASGTP 261
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
6-934 2.62e-116

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 392.27  E-value: 2.62e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350    6 IVVKGARAHNLKDIDIELPKNKLIVMTGLSGSGKSSLAFDTIYAEGQRRYVESLSTYARQ-FLGQMDKPDVDTIEGLSPA 84
Cdd:PRK00635  941 ITIKNAYQHNLKHIDLSLPRNALTAVTGPSASGKHSLVFDILYAAGNIAYAELFPPYIRQaLIKKTPLPSVDKVTGLSPV 1020
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350   85 ISIDQKTTSKNPRSTVATVTEIYDYIRLLYARVGKPYCPNHNIEIESQTVQQMVDRIMELEARTKIQLLAPViahrkGSH 164
Cdd:PRK00635 1021 IAIEKTSASKNSNHSVASALEISNGLEKLFARLGHPYSPLSGDALRKITPQTIAEELLTHYTKGYVTITSPI-----PKE 1095
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  165 EKLI---EDIGKKGYVRLRIDGEIVDVND-VPTLDKNKnhtiEVVVDRLVVKDGIETRLADSIETALELS-EGQLTVdvi 239
Cdd:PRK00635 1096 EDLFiylQEKLKEGFLKLYANEQFYDLDEpLPTSLENP----AIVIQHTKISEKNLSSLLSSLTLAFSLSsSICLHI--- 1168
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  240 dgEDLKFSESHACPI-----CGFSIGELEPRMFSFNSPFGACPTCDGLGQKLTVDVdlvVPDKDKTLNEGAIEPWIPTSS 314
Cdd:PRK00635 1169 --EYAGTSLSLTYRLgwqdsSGNLYPNITTPLLSRDHEEGLCPLCHGKGFILKCSL---LPHKEKIAHYTPLSLFTLFFP 1243
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  315 DFYPTLLKRVCEVYKINMDKPFKKLTERQRDILLYGsgdkeieftfTQRQGGTRKRTMVFEGVVPnisrrfhESPseytr 394
Cdd:PRK00635 1244 NQDPKPVYPLLKELGIPSIALFQELDTLSFESLCLG----------TQQHPGLNALLMEAMLMES-------EEP----- 1301
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  395 eMMSKYMTELPCETCHGKRLSREALSVYVGGLNIGEVVEYSISQALNYYKNIDlSEQDQAIanqiLKEIISRLTFLNNVG 474
Cdd:PRK00635 1302 -LPPPLISKTPCNQCQGLGVYTYAHCVRIHNTSLSDIYQEDVTFLKKFLLTIH-DDEEPSI----IQDLLNRLTFIDKVG 1375
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  475 LEYLTLNRASGTLSGGEAQRIRLATQIGSRLTGVLYVLDEPSIGLHQRDNDRLINTLKEMRDLGNTLIVVEHDDDTMRAA 554
Cdd:PRK00635 1376 LSYITLGQEQDTLSDGEHYRLHLAKKISSNLTDIIYLLEDPLSGLHPQDAPTLLQLIKELVTNNNTVIATDRSGSLAEHA 1455
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  555 DYLVDIGPGAGEHGGQIVSSGTpqkvmkdkksltgqylsgkKRIDVPEYRRPASDRKISIRGAR--SNNLKGIDVDIPLS 632
Cdd:PRK00635 1456 DHLIHLGPGSGPQGGYLLSTSA-------------------LKQSQPDLHNTRSSEETPTLSVSlsIHTIQNLNVSAPLH 1516
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  633 IMTVVTGVSGSGKSSLVNEVLYKSLAQKINKskvkpglydkieGIDQLDKIIDIDQSPIGRTPRSNPATYTGVFDDIRDV 712
Cdd:PRK00635 1517 SLVAISGVSGSGKTSLLLEGFYKQACALIEK------------GPSVFSEIIFLDSHPQISSQRSDISTYFDIAPSLRNF 1584
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  713 FAQTNEAKIRGYQKGRFSFNVKGGRCEACKGDGIIKIEMHFLPDVYVPCEVCDGKRYNRETLEVTYKGKNIADILEMTVE 792
Cdd:PRK00635 1585 YASLTQAKALNISASMFSTNTKQGQCSDCWGLGYQWIDRAFYALEKRPCPTCSGFRIQPLAQEVVYEGKHFGQLLQTPIE 1664
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  793 EATQFFENIPKIKRKLQTLVDVGLGYVTLGQQATTLSGGEAQRVKLASELHKRSTGKSIYILDEPTTGLHVDDISRLLKV 872
Cdd:PRK00635 1665 EVAETFPFLKKIQKPLQALIDNGLGYLPLGQNLSSLSLSEKIAIKIAKFLYLPPKHPTLFLLDEIATSLDNQQKSALLVQ 1744
                         890       900       910       920       930       940
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446585350  873 LNRLVENGDTVVIIEHNLDVIKTADYIIDLGPEGGSGGGTIVATGTPEDIAQTKSSYTGKYL 934
Cdd:PRK00635 1745 LRTLVSLGHSVIYIDHDPALLKQADYLIEMGPGSGKTGGKILFSGPPKDISASKDSLLKTYM 1806
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
6-118 1.47e-73

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: 241.39  E-value: 1.47e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350   6 IVVKGARAHNLKDIDIELPKNKLIVMTGLSGSGKSSLAFDTIYAEGQRRYVESLSTYARQFLGQMDKPDVDTIEGLSPAI 85
Cdd:cd03270    1 IIVRGAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLSPAI 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 446585350  86 SIDQKTTSKNPRSTVATVTEIYDYIRLLYARVG 118
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 3.17e-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: 226.76  E-value: 3.17e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 463 IISRLTFLNNVGLEYLTLNRASGTLSGGEAQRIRLATQIGSRLTGVLYVLDEPSIGLHQRDNDRLINTLKEMRDLGNTLI 542
Cdd:cd03270  114 IRERLGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVL 193
                         90       100       110
                 ....*....|....*....|....*....|...
gi 446585350 543 VVEHDDDTMRAADYLVDIGPGAGEHGGQIVSSG 575
Cdd:cd03270  194 VVEHDEDTIRAADHVIDIGPGAGVHGGEIVAQG 226
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
389-577 5.02e-51

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: 180.12  E-value: 5.02e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 389 PSEYTREMmsKYMTELPCETCHGKRLSREALSVYVGGLNIGEVVEYSISQALNYYKNIdlseqdqaianqilKEIISRLT 468
Cdd:cd03271   88 PATYTGVF--DEIRELFCEVCKGKRYNRETLEVRYKGKSIADVLDMTVEEALEFFENI--------------PKIARKLQ 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 469 FLNNVGLEYLTLNRASGTLSGGEAQRIRLATQIGSRLTG-VLYVLDEPSIGLHQRDNDRLINTLKEMRDLGNTLIVVEHD 547
Cdd:cd03271  152 TLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRSTGkTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHN 231
                        170       180       190
                 ....*....|....*....|....*....|
gi 446585350 548 DDTMRAADYLVDIGPGAGEHGGQIVSSGTP 577
Cdd:cd03271  232 LDVIKCADWIIDLGPEGGDGGGQVVASGTP 261
UvrA_inter pfam17760
UvrA interaction domain; This domain found in UvrA proteins interacts with the UvrB protein.
132-240 7.17e-50

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


Pssm-ID: 436020 [Multi-domain]  Cd Length: 109  Bit Score: 171.12  E-value: 7.17e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  132 QTVQQMVDRIMELEARTKIQLLAPVIAHRKGSHEKLIEDIGKKGYVRLRIDGEIVDVNDVPTLDKNKNHTIEVVVDRLVV 211
Cdd:pfam17760   1 QTVDQIVDRILALPEGTKIQILAPVVRGRKGEHKELLDDLRKQGFVRVRVDGEIYDLDDEPKLDKNKKHTIEVVVDRLVV 80
                          90       100
                  ....*....|....*....|....*....
gi 446585350  212 KDGIETRLADSIETALELSEGQLTVDVID 240
Cdd:pfam17760  81 KEDNRSRLADSVETALKLGKGLVIVLVLD 109
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
611-934 4.93e-49

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: 188.30  E-value: 4.93e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  611 KISIRGARSNNLKGIDVDIPLSIMTVVTGVSGSGKSSLVNEVLY--------KSL----AQKINKSKvKPGLyDKIEGid 678
Cdd:TIGR00630   1 KIIVRGAREHNLKNIDVEIPRDKLVVITGLSGSGKSSLAFDTIYaegqrryvESLsayaRQFLGVMD-KPDV-DSIEG-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  679 qLDKIIDIDQSPIGRTPRSNPATYTGVFDDIRDVFA----------------QTNE------------------------ 718
Cdd:TIGR00630  77 -LSPAISIDQKTTSHNPRSTVGTITEIYDYLRLLFArvgtpycptcgrpisrQTPSqivdqilalpegtrvillapivrg 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  719 ---------AKIR--GYQKGR----------------------------------------------------------- 728
Cdd:TIGR00630 156 rkgefrkllEKLRkqGFARVRvdgevypledppkleknkkhtidvvidrltvknenrsrlaesvetalrlgdgllevefd 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  729 ---------------------------------FSFNVKGGRCEACKGDGIiKIE------------------------- 750
Cdd:TIGR00630 236 ddeevaeskeelfsekfacpecgfslpeleprlFSFNSPYGACPECSGLGI-KQEfdpeliipdpllslnggaivpfkks 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  751 ---------------MHFLPDV---------------------------------------------------------- 757
Cdd:TIGR00630 315 ttsyyrqmfaslaehLGFDLDTpwkdlpeeaqkailygsgeevivvkyrngggetfryhkpfegvipelerryleteses 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  758 ----------YVPCEVCDGKRYNRETLEVTYKGKNIADILEMTVEEATQFFEN--------------IPKIKRKLQTLVD 813
Cdd:TIGR00630 395 mreylekfmsERPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFNQltltpeekkiaeevLKEIRERLGFLID 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  814 VGLGYVTLGQQATTLSGGEAQRVKLASELHKRSTGkSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHNLDVI 893
Cdd:TIGR00630 475 VGLDYLSLSRAAGTLSGGEAQRIRLATQIGSGLTG-VLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTI 553
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|.
gi 446585350  894 KTADYIIDLGPEGGSGGGTIVATGTPEDIAQTKSSYTGKYL 934
Cdd:TIGR00630 554 RAADYVIDIGPGAGEHGGEVVASGTPEEILANPDSLTGQYL 594
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
612-917 2.39e-47

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: 168.59  E-value: 2.39e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 612 ISIRGARSNNLKGIDVDIPLSIMTVVTGVSGSGKSSLVNEVLY-----------KSLAQKINKSKVKPGlYDKIEGidqL 680
Cdd:cd03270    1 IIVRGAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIYaegqrryveslSAYARQFLGQMDKPD-VDSIEG---L 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 681 DKIIDIDQSPIGRTPRSNPATYTGVFDDIRDVFAqtneakirgyqkgrfsfnvkggrceackgdgiikiemhflpdvyvp 760
Cdd:cd03270   77 SPAIAIDQKTTSRNPRSTVGTVTEIYDYLRLLFA---------------------------------------------- 110
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 761 cevcdgkrynretlevtykgkniadilemtveeatqffeNIPkIKRKLQTLVDVGLGYVTLGQQATTLSGGEAQRVKLAS 840
Cdd:cd03270  111 ---------------------------------------RVG-IRERLGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLAT 150
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446585350 841 ELHKRSTGkSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHNLDVIKTADYIIDLGPEGGSGGGTIVATG 917
Cdd:cd03270  151 QIGSGLTG-VLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDIGPGAGVHGGEIVAQG 226
UvrA_DNA-bind pfam17755
UvrA DNA-binding domain;
289-399 2.55e-47

UvrA DNA-binding domain;


Pssm-ID: 465484 [Multi-domain]  Cd Length: 110  Bit Score: 164.18  E-value: 2.55e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  289 DVDLVVPDKDKTLNEGAIEPWIPTSSDFYPTLLKRVCEVYKINMDKPFKKLTERQRDILLYGSGDKEIEFTFTqRQGGTR 368
Cdd:pfam17755   1 DPDLVIPDPSLSLAEGAIAPWGKKRSSYYFQLLEALAKHYGFDLDTPFKDLPEEQQDIILYGSGEEIIVFYYS-RGGRTR 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 446585350  369 KRTMVFEGVVPNISRRFHESPSEYTREMMSK 399
Cdd:pfam17755  80 TYTKPFEGVIPNLERRYRETDSESVREELEK 110
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
464-575 1.40e-45

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: 161.72  E-value: 1.40e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 464 ISRLTFLNNVGLEYLTLNRASGTLSGGEAQRIRLATQIGSRLTGVLYVLDEPSIGLHQRDNDRLINTLKEMRDLGNTLIV 543
Cdd:cd03238   65 IDQLQFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVIL 144
                         90       100       110
                 ....*....|....*....|....*....|..
gi 446585350 544 VEHDDDTMRAADYLVDIGPGAGEHGGQIVSSG 575
Cdd:cd03238  145 IEHNLDVLSSADWIIDFGPGSGKSGGKVVFSG 176
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
612-902 3.39e-44

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: 157.87  E-value: 3.39e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 612 ISIRGARSNNLKGIDVDIPLSIMTVVTGVSGSGKSSLVNEVLYKSLAQKINKSkvkPGLYDKiegidqlDKIIDIDQspi 691
Cdd:cd03238    1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKARLISF---LPKFSR-------NKLIFIDQ--- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 692 grtprsnpatytgvfddirdvfaqtneakirgyqkgrfsfnvkggrceackgdgiikiemhflpdvyvpcevcdgkrynr 771
Cdd:cd03238      --------------------------------------------------------------------------------
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 772 etlevtykgkniadilemtveeatqffenipkikrkLQTLVDVGLGYVTLGQQATTLSGGEAQRVKLASELHKRSTGkSI 851
Cdd:cd03238   68 ------------------------------------LQFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPG-TL 110
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446585350 852 YILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHNLDVIKTADYIIDL 902
Cdd:cd03238  111 FILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDF 161
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
402-902 4.45e-44

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 174.25  E-value: 4.45e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  402 TELPCETCHGKRLSREALSVYVGGLNIGEVVEYSISQALNYYknidLSEqdqaianqilKEIISRLTFLNNVGLEYLTLN 481
Cdd:PRK00635  739 TSIPCPSCLGKRFLPQVLEVRYKGKNIADILEMTAYEAEKFF----LDE----------PSIHEKIHALCSLGLDYLPLG 804
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  482 RASGTLSGGEAQRIRLATQIGSRLTG-VLYVLDEPSIGLHQRDNDRLINTLKEMRDLGNTLIVVEHDDDTMRAADYLVDI 560
Cdd:PRK00635  805 RPLSSLSGGEIQRLKLAYELLAPSKKpTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLEL 884
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  561 GPGAGEHGGQIVSSGTPQKVMKdKKSLTGQ----YLSGKKRIDVPEYRRPASD--RKISIRGARSNNLKGIDVDIPLSIM 634
Cdd:PRK00635  885 GPEGGNLGGYLLASCSPEELIH-LHTPTAKalrpYLSSPQELPYLPDPSPKPPvpADITIKNAYQHNLKHIDLSLPRNAL 963
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  635 TVVTGVSGSGKSSLVNEVLYKS--------LAQKINKSKVKPGLYDKIEGIDQLDKIIDIDQSPIGRTPRSNPATYTGVF 706
Cdd:PRK00635  964 TAVTGPSASGKHSLVFDILYAAgniayaelFPPYIRQALIKKTPLPSVDKVTGLSPVIAIEKTSASKNSNHSVASALEIS 1043
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  707 DDIRDVFAQ-------------------------------------------------TNEAKIRGYQK----------- 726
Cdd:PRK00635 1044 NGLEKLFARlghpysplsgdalrkitpqtiaeellthytkgyvtitspipkeedlfiyLQEKLKEGFLKlyaneqfydld 1123
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  727 GRF-------------------------------------------------------------------------SFNV 733
Cdd:PRK00635 1124 EPLptslenpaiviqhtkiseknlssllssltlafslsssiclhieyagtslsltyrlgwqdssgnlypnittpllSRDH 1203
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  734 KGGRCEACKGDGII----------KIEMH--------FLPDVYV------------------------------------ 759
Cdd:PRK00635 1204 EEGLCPLCHGKGFIlkcsllphkeKIAHYtplslftlFFPNQDPkpvypllkelgipsialfqeldtlsfeslclgtqqh 1283
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  760 ---------------------------PCEVCDGKRYNRETLEVTYKGKNIADILemtvEEATQFFEN------------ 800
Cdd:PRK00635 1284 pglnallmeamlmeseeplppplisktPCNQCQGLGVYTYAHCVRIHNTSLSDIY----QEDVTFLKKflltihddeeps 1359
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  801 -IPKIKRKLQTLVDVGLGYVTLGQQATTLSGGEAQRVKLASelhKRSTGKS--IYILDEPTTGLHVDDISRLLKVLNRLV 877
Cdd:PRK00635 1360 iIQDLLNRLTFIDKVGLSYITLGQEQDTLSDGEHYRLHLAK---KISSNLTdiIYLLEDPLSGLHPQDAPTLLQLIKELV 1436
                         730       740
                  ....*....|....*....|....*
gi 446585350  878 ENGDTVVIIEHNLDVIKTADYIIDL 902
Cdd:PRK00635 1437 TNNNTVIATDRSGSLAEHADHLIHL 1461
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
6-121 1.44e-20

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: 92.29  E-value: 1.44e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350   6 IVVKGARAHNLKDIDIELPKNKLIVMTGLSGSGKSSLAFDTIYAEGQRRYveslstyarqFLGQMDKPDVDTIEGL---S 82
Cdd:cd03271    1 LTLKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPALARRL----------HLKKEQPGNHDRIEGLehiD 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446585350  83 PAISIDQKTTSKNPRSTVATVTEIYDYIRLLYARV--GKPY 121
Cdd:cd03271   71 KVIVIDQSPIGRTPRSNPATYTGVFDEIRELFCEVckGKRY 111
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
8-70 7.00e-18

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: 82.37  E-value: 7.00e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446585350   8 VKGARAHNLKDIDIELPKNKLIVMTGLSGSGKSSLAFDTIYAEGQRRYVESLSTYARQ---FLGQM 70
Cdd:cd03238    3 VSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKARLISFLPKFSRNkliFIDQL 68
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
472-562 3.57e-17

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: 79.71  E-value: 3.57e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 472 NVGLEYLTLNRASGTLSGGEAQRIRLATQIGSRLT--GVLYVLDEPSIGLHQRDNDRLINTLKEMRDLGNTLIVVEHDDD 549
Cdd:cd03227   63 IVAAVSAELIFTRLQLSGGEKELSALALILALASLkpRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPE 142
                         90
                 ....*....|...
gi 446585350 550 TMRAADYLVDIGP 562
Cdd:cd03227  143 LAELADKLIHIKK 155
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
401-594 1.94e-16

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 84.88  E-value: 1.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  401 MTELPCETCHGKRLSREALSVYVGGLNIGEVVEYSIsqalnyyknidlseQDQAIANQILKEIISRLTFLNNVGLEYLTL 480
Cdd:PRK00635 1628 LEKRPCPTCSGFRIQPLAQEVVYEGKHFGQLLQTPI--------------EEVAETFPFLKKIQKPLQALIDNGLGYLPL 1693
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  481 NRASGTLSGGEaqriRLATQIGSRL-----TGVLYVLDEPSIGLHQRDNDRLINTLKEMRDLGNTLIVVEHDDDTMRAAD 555
Cdd:PRK00635 1694 GQNLSSLSLSE----KIAIKIAKFLylppkHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALLKQAD 1769
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 446585350  556 YLVDIGPGAGEHGGQIVSSGTPQKVMKDKKSLTGQYLSG 594
Cdd:PRK00635 1770 YLIEMGPGSGKTGGKILFSGPPKDISASKDSLLKTYMCN 1808
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
470-941 1.23e-15

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: 81.10  E-value: 1.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 470 LNNVGLEYLtLNRASGTLSGGEAQRIRLATQIGSRltGVLYVLDEPSIGL---HQRDNDRLINTLKemRDLGNTLIVVEH 546
Cdd:COG1123  127 LEAVGLERR-LDRYPHQLSGGQRQRVAIAMALALD--PDLLIADEPTTALdvtTQAEILDLLRELQ--RERGTTVLLITH 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 547 D-DDTMRAADYLVDIgpgageHGGQIVSSGTPQKVMKDKKSLtGQYLSGKKRIDVPEYRRPASDRKISIRG------ARS 619
Cdd:COG1123  202 DlGVVAEIADRVVVM------DDGRIVEDGPPEEILAAPQAL-AAVPRLGAARGRAAPAAAAAEPLLEVRNlskrypVRG 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 620 NN----LKGIDVDIP----LSIMtvvtGVSGSGKSSLVnevlyKSLAqkinkskvkpGLYDKIEGidqldKIIdIDQSPI 691
Cdd:COG1123  275 KGgvraVDDVSLTLRrgetLGLV----GESGSGKSTLA-----RLLL----------GLLRPTSG-----SIL-FDGKDL 329
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 692 GRTPRSNPATYTG----VFddiRDVFAqtneakirgyqkgrfSFNvkggrceackgdgiikiemhflPdvyvpcevcdgk 767
Cdd:COG1123  330 TKLSRRSLRELRRrvqmVF---QDPYS---------------SLN----------------------P------------ 357
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 768 rynRETlevtykgknIADIlemtVEEATQFFENIPKIKRK---LQTLVDVGLGYVTLGQQATTLSGGEAQRVKLASELhk 844
Cdd:COG1123  358 ---RMT---------VGDI----IAEPLRLHGLLSRAERRervAELLERVGLPPDLADRYPHELSGGQRQRVAIARAL-- 419
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 845 rSTGKSIYILDEPTTGLhvdDIS---RLLKVLNRLV-ENGDTVVIIEHNLDVIKT-ADYIIDLgpeggsGGGTIVATGTP 919
Cdd:COG1123  420 -ALEPKLLILDEPTSAL---DVSvqaQILNLLRDLQrELGLTYLFISHDLAVVRYiADRVAVM------YDGRIVEDGPT 489
                        490       500
                 ....*....|....*....|...
gi 446585350 920 EDI-AQTKSSYTGKYLKEVLERD 941
Cdd:COG1123  490 EEVfANPQHPYTRALLAAVPSLD 512
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
828-902 4.08e-15

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: 73.82  E-value: 4.08e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446585350 828 LSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHNLDVIKTA-DYIIDL 902
Cdd:cd00267   81 LSGGQRQRVALARALLLNP---DLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAaDRVIVL 153
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
444-587 1.23e-14

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: 74.29  E-value: 1.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 444 KNIDLSEQD-QAIANQILKEiisrltflnnVGLEYLtLNRASGTLSGGEAQRIRLAtqigsrltGVL------YVLDEPS 516
Cdd:COG1122  102 ENLGLPREEiRERVEEALEL----------VGLEHL-ADRPPHELSGGQKQRVAIA--------GVLamepevLVLDEPT 162
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446585350 517 IGLHQRDNDRLINTLKEMRDLGNTLIVVEHD-DDTMRAADYLVDIgpgageHGGQIVSSGTPQKVMKDKKSL 587
Cdd:COG1122  163 AGLDPRGRRELLELLKRLNKEGKTVIIVTHDlDLVAELADRVIVL------DDGRIVADGTPREVFSDYELL 228
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
821-926 2.50e-14

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: 77.11  E-value: 2.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 821 LGQQATTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHVDDISRLLKVLNRLVEnGDTVVIIEHNLDVIKTADYII 900
Cdd:COG4988  467 LGEGGRGLSGGQAQRLALARALLRDA---PLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLAQADRIL 542
                         90       100
                 ....*....|....*....|....*.
gi 446585350 901 DLgpeggsGGGTIVATGTPEDIAQTK 926
Cdd:COG4988  543 VL------DDGRIVEQGTHEELLAKN 562
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
827-922 3.09e-14

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: 73.14  E-value: 3.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 827 TLSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLhvDDISR--LLKVLNRLVENGDTVVIIEHNLD-VIKTADYIIDLg 903
Cdd:COG1122  134 ELSGGQKQRVAIAGVL---AMEPEVLVLDEPTAGL--DPRGRreLLELLKRLNKEGKTVIIVTHDLDlVAELADRVIVL- 207
                         90
                 ....*....|....*....
gi 446585350 904 peggsGGGTIVATGTPEDI 922
Cdd:COG1122  208 -----DDGRIVADGTPREV 221
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
827-900 6.12e-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: 71.73  E-value: 6.12e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446585350 827 TLSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHNLD-VIKTADYII 900
Cdd:cd03225  134 TLSGGQKQRVAIAGVL---AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDlLLELADRVI 205
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
425-581 2.17e-13

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 71.20  E-value: 2.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 425 GLNIGEVVEYSISQALNYYKNidLSEQDQAIANQILKEiisrltflnnVGLEYLTlNRASGTLSGGEAQRIRLATQIGSR 504
Cdd:PRK11231  90 GITVRELVAYGRSPWLSLWGR--LSAEDNARVNQAMEQ----------TRINHLA-DRRLTDLSGGQRQRAFLAMVLAQD 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 505 LTGVLyvLDEPSIGL---HQRDndrLINTLKEMRDLGNTLIVVEHD-DDTMRAADYLVDIgpgageHGGQIVSSGTPQKV 580
Cdd:PRK11231 157 TPVVL--LDEPTTYLdinHQVE---LMRLMRELNTQGKTVVTVLHDlNQASRYCDHLVVL------ANGHVMAQGTPEEV 225

                 .
gi 446585350 581 M 581
Cdd:PRK11231 226 M 226
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
487-563 2.36e-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: 68.43  E-value: 2.36e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446585350 487 LSGGEAQRIRLATQIGSRLTgvLYVLDEPSIGLHQRDNDRLINTLKEMRDLGNTLIVVEHD-DDTMRAADYLVDIGPG 563
Cdd:cd00267   81 LSGGQRQRVALARALLLNPD--LLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDpELAELAADRVIVLKDG 156
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
818-902 3.21e-13

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: 68.54  E-value: 3.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 818 YVTLGQqattLSGGEAQRVKLASELHKRST-GKSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHNLDVIKTA 896
Cdd:cd03227   72 IFTRLQ----LSGGEKELSALALILALASLkPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELA 147

                 ....*.
gi 446585350 897 DYIIDL 902
Cdd:cd03227  148 DKLIHI 153
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
775-902 1.27e-12

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 67.92  E-value: 1.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 775 EVTYKGKNIADI------------------LEMTVEE----ATQFFENIPKIKRKLQTLVDVGLGYVTLGQQATTLSGGE 832
Cdd:COG4619   56 EIYLDGKPLSAMpppewrrqvayvpqepalWGGTVRDnlpfPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGE 135
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446585350 833 AQRVKLASELhkrSTGKSIYILDEPTTGLHVDDISRLLKVLNRLV-ENGDTVVIIEHNLDVIKT-ADYIIDL 902
Cdd:COG4619  136 RQRLALIRAL---LLQPDVLLLDEPTSALDPENTRRVEELLREYLaEEGRAVLWVSHDPEQIERvADRVLTL 204
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
788-924 5.29e-12

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 66.63  E-value: 5.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 788 EMTVEEATQFFENI-----PKIKRKLQTLVD-VGLGYVtLGQQATTLSGGEAQRVKLASEL-HKRStgksIYILDEPTTG 860
Cdd:COG1131   87 DLTVRENLRFFARLyglprKEARERIDELLElFGLTDA-ADRKVGTLSGGMKQRLGLALALlHDPE----LLILDEPTSG 161
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446585350 861 LHVDDISRLLKVLNRLVENGDTVVIIEHNLDVI-KTADY--IIDlgpeggsgGGTIVATGTPEDIAQ 924
Cdd:COG1131  162 LDPEARRELWELLRELAAEGKTVLLSTHYLEEAeRLCDRvaIID--------KGRIVADGTPDELKA 220
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
828-900 1.14e-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: 63.99  E-value: 1.14e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446585350 828 LSGGEAQRVKLASELHkrsTGKSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHNLD-VIKTADYII 900
Cdd:cd03216   83 LSVGERQMVEIARALA---RNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDeVFEIADRVT 153
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
814-923 1.24e-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: 65.54  E-value: 1.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 814 VGLGYVtLGQQATTLSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHNLDVI 893
Cdd:cd03219  131 VGLADL-ADRPAGELSYGQQRRLEIARAL---ATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVV 206
                         90       100       110
                 ....*....|....*....|....*....|.
gi 446585350 894 KT-ADYIIDLgpeggsGGGTIVATGTPEDIA 923
Cdd:cd03219  207 MSlADRVTVL------DQGRVIAEGTPDEVR 231
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
780-922 3.71e-11

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: 66.85  E-value: 3.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 780 GKNIADILE---MTVEEAtqffenipkIKRKLQTLVDVGLGYVtLGQQATTLSGGEAQRVKLASELhkrSTGKSIYILDE 856
Cdd:COG1123  102 GDQIAEALEnlgLSRAEA---------RARVLELLEAVGLERR-LDRYPHQLSGGQRQRVAIAMAL---ALDPDLLIADE 168
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 857 PTTGLHV---DDISRLLKVLNRlvENGDTVVIIEHNLDVI-KTADYIIDLgpeggsGGGTIVATGTPEDI 922
Cdd:COG1123  169 PTTALDVttqAEILDLLRELQR--ERGTTVLLITHDLGVVaEIADRVVVM------DDGRIVEDGPPEEI 230
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
797-900 3.83e-11

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: 63.71  E-value: 3.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 797 FFENIPKIKRK--LQTLVDVGLGYVtLGQQATTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHVDDISRLLKVLN 874
Cdd:cd03235  101 LFRRLSKADKAkvDEALERVGLSEL-ADRQIGELSGGQQQRVLLARALVQDP---DLLLLDEPFAGVDPKTQEDIYELLR 176
                         90       100
                 ....*....|....*....|....*..
gi 446585350 875 RLVENGDTVVIIEHNLD-VIKTADYII 900
Cdd:cd03235  177 ELRREGMTILVVTHDLGlVLEYFDRVL 203
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
808-902 9.58e-11

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: 65.39  E-value: 9.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  808 LQTLV-DVGLGYVT-LGQQATTLSGGEAQRVKLASELHKrstGKSIYILDEPTTGLHVDDISRLLKVLNRLVEnGDTVVI 885
Cdd:TIGR02857 437 LDEFVaALPQGLDTpIGEGGAGLSGGQAQRLALARAFLR---DAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLL 512
                          90
                  ....*....|....*..
gi 446585350  886 IEHNLDVIKTADYIIDL 902
Cdd:TIGR02857 513 VTHRLALAALADRIVVL 529
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
776-901 1.16e-10

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: 62.81  E-value: 1.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 776 VTYKGKNIADILEMTVE----EATQFFENIPKIKR------KLQTLVDvglgyvtlgQQATTLSGGEAQRVKLASELHKR 845
Cdd:cd03237   63 VSYKPQYIKADYEGTVRdllsSITKDFYTHPYFKTeiakplQIEQILD---------REVPELSGGELQRVAIAACLSKD 133
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446585350 846 StgkSIYILDEPTTGLHVDDISRLLKVLNRLVENGD-TVVIIEHnlDVIkTADYIID 901
Cdd:cd03237  134 A---DIYLLDEPSAYLDVEQRLMASKVIRRFAENNEkTAFVVEH--DII-MIDYLAD 184
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
461-558 1.45e-10

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: 61.71  E-value: 1.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 461 KEIISRLTF-LNNVGLEYLtLNRASGTLSGGEAQRIRLATQIGSRLTgvLYVLDEPSIGLHQRDNDRLINTLKEMRDLGN 539
Cdd:cd03225  109 EEIEERVEEaLELVGLEGL-RDRSPFTLSGGQKQRVAIAGVLAMDPD--ILLLDEPTAGLDPAGRRELLELLKKLKAEGK 185
                         90       100
                 ....*....|....*....|
gi 446585350 540 TLIVVEHD-DDTMRAADYLV 558
Cdd:cd03225  186 TIIIVTHDlDLLLELADRVI 205
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
827-922 1.51e-10

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 62.41  E-value: 1.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 827 TLSGGEAQRVKLASELHKRStgkSIYILDEPTTGL---HVDDISRLLKvlnRLVENGDTVVIIEHNLD-VIKTADYIIDL 902
Cdd:COG1121  139 ELSGGQQQRVLLARALAQDP---DLLLLDEPFAGVdaaTEEALYELLR---ELRREGKTILVVTHDLGaVREYFDRVLLL 212
                         90       100
                 ....*....|....*....|
gi 446585350 903 gpeggsgGGTIVATGTPEDI 922
Cdd:COG1121  213 -------NRGLVAHGPPEEV 225
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
473-585 1.55e-10

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: 62.45  E-value: 1.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 473 VGLEYLtLNRASGTLSGGEAQRIRLATQIGSRlTGVLyVLDEPSIGLHQRDNDRLINTLKEMRDLGNTLIVVEHD-DDTM 551
Cdd:cd03219  131 VGLADL-ADRPAGELSYGQQRRLEIARALATD-PKLL-LLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDmDVVM 207
                         90       100       110
                 ....*....|....*....|....*....|....
gi 446585350 552 RAADYLVDIgpgageHGGQIVSSGTPQKVMKDKK 585
Cdd:cd03219  208 SLADRVTVL------DQGRVIAEGTPDEVRNNPR 235
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
828-902 2.04e-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: 60.69  E-value: 2.04e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446585350 828 LSGGEAQRVKLASELHKRstgKSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHNLDVIKTADYIIDL 902
Cdd:cd03246   97 LSGGQRQRLGLARALYGN---PRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVL 168
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
816-929 3.49e-10

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: 64.08  E-value: 3.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 816 LGYVT-LGQQATTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLhvDDIS--RLLKVLNRLVeNGDTVVIIEHNLDV 892
Cdd:COG2274  599 MGYDTvVGEGGSNLSGGQRQRLAIARALLRNP---RILILDEATSAL--DAETeaIILENLRRLL-KGRTVIIIAHRLST 672
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446585350 893 IKTADYIIDLgpeggsGGGTIVATGTPEDIAQTKSSY 929
Cdd:COG2274  673 IRLADRIIVL------DKGRIVEDGTHEELLARKGLY 703
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
789-929 3.87e-10

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: 60.98  E-value: 3.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 789 MTVEEATQFF--ENIPKIKRKLQTLVDVGLGYVTLGQQA----TTLSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLH 862
Cdd:cd03261   92 LTVFENVAFPlrEHTRLSEEEIREIVLEKLEAVGLRGAEdlypAELSGGMKKRVALARAL---ALDPELLLYDEPTAGLD 168
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446585350 863 ---VDDISRLLKVLNRlvENGDTVVIIEHNLD-VIKTADYIIDLgpeggsGGGTIVATGTPEDIAQTKSSY 929
Cdd:cd03261  169 piaSGVIDDLIRSLKK--ELGLTSIMVTHDLDtAFAIADRIAVL------YDGKIVAEGTPEELRASDDPL 231
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
448-547 4.24e-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: 60.62  E-value: 4.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 448 LSEQDQAIANQILKEiisrltflnnVGLEYLtLNRASGTLSGGEAQRIRLATQIGSRltGVLYVLDEPSIGLHQRDNDRL 527
Cdd:cd03235  105 LSKADKAKVDEALER----------VGLSEL-ADRQIGELSGGQQQRVLLARALVQD--PDLLLLDEPFAGVDPKTQEDI 171
                         90       100
                 ....*....|....*....|
gi 446585350 528 INTLKEMRDLGNTLIVVEHD 547
Cdd:cd03235  172 YELLRELRREGMTILVVTHD 191
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
826-922 7.32e-10

ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];


Pssm-ID: 440737 [Multi-domain]  Cd Length: 254  Bit Score: 60.44  E-value: 7.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 826 TTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLhvdDIS---RLLKVLNRLV-ENGDTVVIIEHNLD-VIKTADYII 900
Cdd:COG1120  136 DELSGGERQRVLIARALAQEP---PLLLLDEPTSHL---DLAhqlEVLELLRRLArERGRTVVMVLHDLNlAARYADRLV 209
                         90       100
                 ....*....|....*....|..
gi 446585350 901 DLgpeggsGGGTIVATGTPEDI 922
Cdd:COG1120  210 LL------KDGRIVAQGPPEEV 225
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
445-584 7.77e-10

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: 62.47  E-value: 7.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 445 NIDLSEQD--QAIANQILKEIISRLtflnNVGLEYLTLNRASGtLSGGEAQRIRLAtqigsRL---TGVLYVLDEPSIGL 519
Cdd:COG4988  435 RPDASDEEleAALEAAGLDEFVAAL----PDGLDTPLGEGGRG-LSGGQAQRLALA-----RAllrDAPLLLLDEPTAHL 504
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446585350 520 HQRDNDRLINTLKEMRDlGNTLIVVEHDDDTMRAADYLVDIgpgageHGGQIVSSGTPQKVMKDK 584
Cdd:COG4988  505 DAETEAEILQALRRLAK-GRTVILITHRLALLAQADRILVL------DDGRIVEQGTHEELLAKN 562
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
775-900 1.12e-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: 58.56  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 775 EVTYKGKNIadilemtveeatqfFENIPKIKRKLQTLVDVGLGYVTL-GQQATTLSGGEAQRVKLASEL-HKRStgksIY 852
Cdd:cd03230   56 EIKVLGKDI--------------KKEPEEVKRRIGYLPEEPSLYENLtVRENLKLSGGMKQRLALAQALlHDPE----LL 117
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 446585350 853 ILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHNLDVI-KTADYII 900
Cdd:cd03230  118 ILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAeRLCDRVA 166
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
808-900 1.44e-09

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: 58.22  E-value: 1.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 808 LQTLVDVGLGYVtLGQQATTLSGGEAQRVKLASELHKRSTgksIYILDEPTTGLhvdDI---SRLLKVLNRLV-ENGDTV 883
Cdd:cd03214   79 PQALELLGLAHL-ADRPFNELSGGERQRVLLARALAQEPP---ILLLDEPTSHL---DIahqIELLELLRRLArERGKTV 151
                         90
                 ....*....|....*...
gi 446585350 884 VIIEHNLD-VIKTADYII 900
Cdd:cd03214  152 VMVLHDLNlAARYADRVI 169
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
480-582 1.71e-09

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 59.56  E-value: 1.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 480 LNRASGTLSGGEAQRIRLAT---QIGSRLT--GVLYVLDEPSIGL---HQRDNDRLINtlkEMRDLGNTLIVVEHD-DDT 550
Cdd:PRK03695 120 LGRSVNQLSGGEWQRVRLAAvvlQVWPDINpaGQLLLLDEPMNSLdvaQQAALDRLLS---ELCQQGIAVVMSSHDlNHT 196
                         90       100       110
                 ....*....|....*....|....*....|....
gi 446585350 551 MRAAD--YLVdigpgageHGGQIVSSGTPQKVMK 582
Cdd:PRK03695 197 LRHADrvWLL--------KQGKLLASGRRDEVLT 222
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
773-901 2.02e-09

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 61.36  E-value: 2.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 773 TLEVTYKGKNIADILEMTVEEatqFFENIPK----------IKRKLQtLVDVglgyvtLGQQATTLSGGEAQRVKLASEL 842
Cdd:PRK13409 399 ELKISYKPQYIKPDYDGTVED---LLRSITDdlgssyykseIIKPLQ-LERL------LDKNVKDLSGGELQRVAIAACL 468
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 843 HKRStgkSIYILDEPTTGLHVDDISRLLKVLNRLVENGD-TVVIIEHNLDVIktaDYIID 901
Cdd:PRK13409 469 SRDA---DLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREaTALVVDHDIYMI---DYISD 522
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
790-922 2.46e-09

energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 275313 [Multi-domain]  Cd Length: 268  Bit Score: 59.37  E-value: 2.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  790 TVEEATQF-FENI----PKIKRKLQT-LVDVGL-GYvtLGQQATTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLh 862
Cdd:TIGR04520  94 TVEDDVAFgLENLgvprEEMRKRVDEaLKLVGMeDF--RDREPHLLSGGQKQRVAIAGVLAMRP---DIIILDEATSML- 167
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446585350  863 vDDISR--LLKVLNRLV-ENGDTVVIIEHNLDVIKTADYIIDLgpeggsGGGTIVATGTPEDI 922
Cdd:TIGR04520 168 -DPKGRkeVLETIRKLNkEEGITVISITHDMEEAVLADRVIVM------NKGKIVAEGTPREI 223
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
827-902 2.79e-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: 58.04  E-value: 2.79e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446585350 827 TLSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHNLDVI-KTADYIIDL 902
Cdd:cd03226  126 SLSGGQKQRLAIAAAL---LSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLaKVCDRVLLL 199
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
444-602 3.11e-09

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 59.26  E-value: 3.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 444 KNIDLSEQDqaiANQILKEIISRltflnnVGLEYLTLNRASGTLSGGEAQRIRLAtqigsrltGVL------YVLDEPSI 517
Cdd:PRK13634 112 MNFGVSEED---AKQKAREMIEL------VGLPEELLARSPFELSGGQMRRVAIA--------GVLamepevLVLDEPTA 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 518 GLHQRDNdrlintlKEMRDL--------GNTLIVVEHD-DDTMRAADYLVDIgpgageHGGQIVSSGTPQKVMKDKKSLT 588
Cdd:PRK13634 175 GLDPKGR-------KEMMEMfyklhkekGLTTVLVTHSmEDAARYADQIVVM------HKGTVFLQGTPREIFADPDELE 241
                        170
                 ....*....|....
gi 446585350 589 GqylsgkKRIDVPE 602
Cdd:PRK13634 242 A------IGLDLPE 249
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
828-902 4.12e-09

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: 56.62  E-value: 4.12e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446585350 828 LSGGEAQRVKLASELHKRStgkSIYILDEPTTGLhvDDIS--RLLKVLNRLvENGDTVVIIEHNLDVIKTADYIIDL 902
Cdd:cd03228   97 LSGGQRQRIAIARALLRDP---PILILDEATSAL--DPETeaLILEALRAL-AKGKTVIVIAHRLSTIRDADRIIVL 167
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
452-575 6.33e-09

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: 56.29  E-value: 6.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 452 DQAIANQILKEIISRLTF----LNNVGLEYLtLNRASGTLSGGEAQRIRLATQIGsRLTGVLyVLDEPSIGL---HQrdn 524
Cdd:cd03214   60 GKDLASLSPKELARKIAYvpqaLELLGLAHL-ADRPFNELSGGERQRVLLARALA-QEPPIL-LLDEPTSHLdiaHQ--- 133
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446585350 525 DRLINTLKEM-RDLGNTLIVVEHD-DDTMRAADYLVDIgpgageHGGQIVSSG 575
Cdd:cd03214  134 IELLELLRRLaRERGKTVVMVLHDlNLAARYADRVILL------KDGRIVAQG 180
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
823-922 6.94e-09

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 59.08  E-value: 6.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 823 QQATTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHNLDV-IKTADYIID 901
Cdd:PRK09536 135 RPVTSLSGGERQRVLLARALAQAT---PVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLaARYCDELVL 211
                         90       100
                 ....*....|....*....|.
gi 446585350 902 LGPEGgsgggtIVATGTPEDI 922
Cdd:PRK09536 212 LADGR------VRAAGPPADV 226
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
772-901 7.74e-09

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: 59.41  E-value: 7.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 772 ETLEVTYKGKNIADILEMTVEEA----------TQFFENipKIKRKLqtlvdvGLGYVtLGQQATTLSGGEAQRVKLASE 841
Cdd:COG1245  399 EDLKISYKPQYISPDYDGTVEEFlrsantddfgSSYYKT--EIIKPL------GLEKL-LDKNVKDLSGGELQRVAIAAC 469
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446585350 842 LHKRStgkSIYILDEPTTGLHVDDISRLLKVLNRLVENGD-TVVIIEHNLDVIktaDYIID 901
Cdd:COG1245  470 LSRDA---DLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGkTAMVVDHDIYLI---DYISD 524
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
823-943 1.06e-08

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 57.33  E-value: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 823 QQATTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLhvdDISR---LLKVLNRLVENGDTVVIIEHNLD-VIKTADY 898
Cdd:PRK11231 134 RRLTDLSGGQRQRAFLAMVLAQDT---PVVLLDEPTTYL---DINHqveLMRLMRELNTQGKTVVTVLHDLNqASRYCDH 207
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 446585350 899 IIDLGPEGgsgggtIVATGTPEDIaqtkssYTGKYLKEVLERDKQ 943
Cdd:PRK11231 208 LVVLANGH------VMAQGTPEEV------MTPGLLRTVFDVEAE 240
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
821-924 1.15e-08

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: 56.29  E-value: 1.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 821 LGQQATTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLH---VDDISRLLKVLNRLvenGDTVVIIEHNLDVI-KTA 896
Cdd:cd03224  126 RKQLAGTLSGGEQQMLAIARALMSRP---KLLLLDEPSEGLApkiVEEIFEAIRELRDE---GVTILLVEQNARFAlEIA 199
                         90       100       110
                 ....*....|....*....|....*....|
gi 446585350 897 D--YIIDlgpeggsgGGTIVATGTPEDIAQ 924
Cdd:cd03224  200 DraYVLE--------RGRVVLEGTAAELLA 221
cbiO PRK13644
energy-coupling factor transporter ATPase;
790-922 1.16e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 57.30  E-value: 1.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 790 TVEEATQFF-ENIPKIKRKLQTLVDVGLGYVTLGQ----QATTLSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLHVD 864
Cdd:PRK13644  94 TVEEDLAFGpENLCLPPIEIRKRVDRALAEIGLEKyrhrSPKTLSGGQGQCVALAGIL---TMEPECLIFDEVTSMLDPD 170
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446585350 865 DISRLLKVLNRLVENGDTVVIIEHNLDVIKTADYIIDLGPEGgsgggtIVATGTPEDI 922
Cdd:PRK13644 171 SGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGK------IVLEGEPENV 222
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
811-930 1.31e-08

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];


Pssm-ID: 440741 [Multi-domain]  Cd Length: 248  Bit Score: 56.74  E-value: 1.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 811 LVDVGLGYVTLGQQATTLSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLhvdDIS---RLLKVLNRL-VENGDTVVII 886
Cdd:COG1124  122 LEQVGLPPSFLDRYPHQLSGGQRQRVAIARAL---ILEPELLLLDEPTSAL---DVSvqaEILNLLKDLrEERGLTYLFV 195
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446585350 887 EHNLDVIKT-ADYIIDLgpeggsGGGTIVATGTPEDI-AQTKSSYT 930
Cdd:COG1124  196 SHDLAVVAHlCDRVAVM------QNGRIVEELTVADLlAGPKHPYT 235
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
803-900 1.72e-08

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: 55.97  E-value: 1.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 803 KIKRKLQTLVDVGLGYVTLGQQATTLSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLHV---DDISRLLKVLNRlvEN 879
Cdd:cd03257  121 RKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARAL---ALNPKLLIADEPTSALDVsvqAQILDLLKKLQE--EL 195
                         90       100
                 ....*....|....*....|..
gi 446585350 880 GDTVVIIEHNLDVIK-TADYII 900
Cdd:cd03257  196 GLTLLFITHDLGVVAkIADRVA 217
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
473-582 1.95e-08

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 56.33  E-value: 1.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 473 VGLEYLTlNRASGTLSGGEAQRIRLATQIGSRLTGVLyvLDEPSIGL---HQRDNDRLINTLKEMRDLgnTLIVVEHD-D 548
Cdd:PRK10575 135 VGLKPLA-HRLVDSLSGGERQRAWIAMLVAQDSRCLL--LDEPTSALdiaHQVDVLALVHRLSQERGL--TVIAVLHDiN 209
                         90       100       110
                 ....*....|....*....|....*....|....
gi 446585350 549 DTMRAADYLVDIgpgageHGGQIVSSGTPQKVMK 582
Cdd:PRK10575 210 MAARYCDYLVAL------RGGEMIAQGTPAELMR 237
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
826-921 2.13e-08

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 56.32  E-value: 2.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 826 TTLSGGEAQRVKLA---SELHKRSTGKSIYILDEPTTGLhvdDIS---RLLKVLNRLV-ENGDTVVIIEHNLDV-IKTAD 897
Cdd:PRK13548 133 PQLSGGEQQRVQLArvlAQLWEPDGPPRWLLLDEPTSAL---DLAhqhHVLRLARQLAhERGLAVIVVLHDLNLaARYAD 209
                         90       100
                 ....*....|....*....|....
gi 446585350 898 YIIDLgpeggsGGGTIVATGTPED 921
Cdd:PRK13548 210 RIVLL------HQGRLVADGTPAE 227
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
817-929 2.36e-08

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: 55.70  E-value: 2.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 817 GYVT-LGQQATTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHVDDISRLLKVLNRLVeNGDTVVIIEHNLDVIKT 895
Cdd:cd03253  126 GYDTiVGERGLKLSGGEKQRVAIARAILKNP---PILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVN 201
                         90       100       110
                 ....*....|....*....|....*....|....
gi 446585350 896 ADYIIDLGPEGgsgggtIVATGTPEDIAQTKSSY 929
Cdd:cd03253  202 ADKIIVLKDGR------IVERGTHEELLAKGGLY 229
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
817-929 3.78e-08

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 57.10  E-value: 3.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 817 GYVT-LGQQATTLSGGEAQRVKLASELHKRStgkSIYILDEPTTglHVDDIS--RLLKVLNRLVENGdTVVIIEHNLDVI 893
Cdd:COG1132  465 GYDTvVGERGVNLSGGQRQRIAIARALLKDP---PILILDEATS--ALDTETeaLIQEALERLMKGR-TTIVIAHRLSTI 538
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446585350 894 KTADYIIDLgpeggsGGGTIVATGTPEDIAQTKSSY 929
Cdd:COG1132  539 RNADRILVL------DDGRIVEQGTHEELLARGGLY 568
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
821-890 4.16e-08

ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 55.23  E-value: 4.16e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446585350 821 LGQQATTLSGGEAQRVKLAS---ELHKR--STGKsIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHNL 890
Cdd:COG4138  120 LSRPLTQLSGGEWQRVRLAAvllQVWPTinPEGQ-LLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDL 193
cbiO PRK13641
energy-coupling factor transporter ATPase;
467-593 5.14e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 55.61  E-value: 5.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 467 LTFLNNVGLEYLTLNRASGTLSGGEAQRIRLAtqigsrltGVL------YVLDEPSIGLHQRDNDRLINTLKEMRDLGNT 540
Cdd:PRK13641 126 LKWLKKVGLSEDLISKSPFELSGGQMRRVAIA--------GVMayepeiLCLDEPAAGLDPEGRKEMMQLFKDYQKAGHT 197
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446585350 541 LIVVEH--DDDTMRAADYLVdigpgaGEHgGQIVSSGTPQKVMKDKKSLTGQYLS 593
Cdd:PRK13641 198 VILVTHnmDDVAEYADDVLV------LEH-GKLIKHASPKEIFSDKEWLKKHYLD 245
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
790-922 5.47e-08

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 55.41  E-value: 5.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 790 TVEEATQF-FEN--IPK---IKRKLQTLVDVGLGYVtLGQQATTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLhv 863
Cdd:PRK13635  98 TVQDDVAFgLENigVPReemVERVDQALRQVGMEDF-LNREPHRLSGGQKQRVAIAGVLALQP---DIIILDEATSML-- 171
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446585350 864 DDISR--LLKVLNRLVENGD-TVVIIEHNLDVIKTADYIIDLGPEGgsgggtIVATGTPEDI 922
Cdd:PRK13635 172 DPRGRreVLETVRQLKEQKGiTVLSITHDLDEAAQADRVIVMNKGE------ILEEGTPEEI 227
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
480-583 5.60e-08

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: 54.36  E-value: 5.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 480 LNRASGTLSGGEAQriRLAtqIGSRLTG--VLYVLDEPSIGLHQRDNDRLINTLKEMRDLGNTLIVVEHD-DDTMRAAD- 555
Cdd:cd03224  126 RKQLAGTLSGGEQQ--MLA--IARALMSrpKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNaRFALEIADr 201
                         90       100
                 ....*....|....*....|....*....
gi 446585350 556 -YLVDigpgagehGGQIVSSGTPQKVMKD 583
Cdd:cd03224  202 aYVLE--------RGRVVLEGTAAELLAD 222
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
828-929 6.53e-08

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: 54.60  E-value: 6.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 828 LSGGEAQRVKLAselhkRStgksI-----YIL-DEPTTGLH---VDDISRLLKVLNRlvENGDTVVIIEHNLD-VIKTAD 897
Cdd:COG1127  142 LSGGMRKRVALA-----RA----LaldpeILLyDEPTAGLDpitSAVIDELIRELRD--ELGLTSVVVTHDLDsAFAIAD 210
                         90       100       110
                 ....*....|....*....|....*....|..
gi 446585350 898 YIIDLgpeggsGGGTIVATGTPEDIAQTKSSY 929
Cdd:COG1127  211 RVAVL------ADGKIIAEGTPEELLASDDPW 236
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
803-930 8.40e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 54.76  E-value: 8.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 803 KIKRKL-QTLVDVGLgYVTLGQQATTLSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLHVDDISRLLKVLNRLVENGD 881
Cdd:PRK13648 118 EMHRRVsEALKQVDM-LERADYEPNALSGGQKQRVAIAGVL---ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHN 193
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 446585350 882 -TVVIIEHNLDVIKTADYIIDLgpeggsGGGTIVATGTPEDIAQTKSSYT 930
Cdd:PRK13648 194 iTIISITHDLSEAMEADHVIVM------NKGTVYKEGTPTEIFDHAEELT 237
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
775-899 8.83e-08

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


Pssm-ID: 213184 [Multi-domain]  Cd Length: 200  Bit Score: 53.30  E-value: 8.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 775 EVTYKGKniaDILEMTVEE--------ATQFFENIPKIKrklqtLVDVgLGYVTLGqqattLSGGEAQRVKLASELHKRS 846
Cdd:cd03217   58 EILFKGE---DITDLPPEErarlgiflAFQYPPEIPGVK-----NADF-LRYVNEG-----FSGGEKKRNEILQLLLLEP 123
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446585350 847 TgksIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHN---LDVIKtADYI 899
Cdd:cd03217  124 D---LAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYqrlLDYIK-PDRV 175
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
789-924 9.41e-08

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: 54.09  E-value: 9.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 789 MTVEEATQFFENIPKIKRK-LQTLVD-----VGLGYVtLGQQATTLSGGEAQRVKLASEL-HKRStgksIYILDEPTTGL 861
Cdd:COG4555   89 LTVRENIRYFAELYGLFDEeLKKRIEelielLGLEEF-LDRRVGELSTGMKKKVALARALvHDPK----VLLLDEPTNGL 163
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446585350 862 HVDDISRLLKVLNRLVENGDTVVIIEHNLDVI-KTADYIIDLgpeggsGGGTIVATGTPEDIAQ 924
Cdd:COG4555  164 DVMARRLLREILRALKKEGKTVLFSSHIMQEVeALCDRVVIL------HKGKVVAQGSLDELRE 221
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
788-902 1.18e-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: 53.26  E-value: 1.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 788 EMTVEE---ATQFFENIPK--IKRKLQTLVD-VGLGYVtLGQQATTLSGGEAQRVKLASELhkrSTGKSIYILDEPTTGL 861
Cdd:cd03255   96 DLTALEnveLPLLLAGVPKkeRRERAEELLErVGLGDR-LNHYPSELSGGQQQRVAIARAL---ANDPKIILADEPTGNL 171
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 446585350 862 ---HVDDISRLLKVLNRlvENGDTVVIIEHNLDVIKTADYIIDL 902
Cdd:cd03255  172 dseTGKEVMELLRELNK--EAGTTIVVVTHDPELAEYADRIIEL 213
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
816-902 1.29e-07

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: 53.64  E-value: 1.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 816 LGYVT-LGQQATTLSGGEAQRVKLASELHkrsTGKSIYILDEPTTGLHVDDISRLLKVLNRLVEnGDTVVIIEHNLDVIK 894
Cdd:cd03252  126 EGYDTiVGEQGAGLSGGQRQRIAIARALI---HNPRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVK 201

                 ....*...
gi 446585350 895 TADYIIDL 902
Cdd:cd03252  202 NADRIIVM 209
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
801-922 1.31e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 54.47  E-value: 1.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 801 IPKIKRKLQT---LVDVGLGYVTLGQQATTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHVDDISRLLKVLNRLV 877
Cdd:PRK13631 147 VKKSEAKKLAkfyLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQP---EILIFDEPTAGLDPKGEHEMMQLILDAK 223
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446585350 878 ENGDTVVIIEHNLD-VIKTADYIIDLGPEGgsgggtIVATGTPEDI 922
Cdd:PRK13631 224 ANNKTVFVITHTMEhVLEVADEVIVMDKGK------ILKTGTPYEI 263
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
451-584 1.52e-07

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 53.62  E-value: 1.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 451 QDQAIANQILKEiisrltflnnVGLEYLTlNRASGTLSGGEAQRIRLA---TQIGSRL--TGVLYvLDEPSIGL---HQr 522
Cdd:PRK13548 110 EDDALVAAALAQ----------VDLAHLA-GRDYPQLSGGEQQRVQLArvlAQLWEPDgpPRWLL-LDEPTSALdlaHQ- 176
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446585350 523 dndrlINTLKEMRDL----GNTLIVVEHD-DDTMRAADYLVDIgpgageHGGQIVSSGTPQKVMKDK 584
Cdd:PRK13548 177 -----HHVLRLARQLaherGLAVIVVLHDlNLAARYADRIVLL------HQGRLVADGTPAEVLTPE 232
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
822-922 1.55e-07

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 53.84  E-value: 1.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 822 GQQATTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGL---HVDDISRLLKVLNRlvENGDTVVIIEHNLD-VIKTAD 897
Cdd:PRK10253 138 DQSVDTLSGGQRQRAWIAMVLAQET---AIMLLDEPTTWLdisHQIDLLELLSELNR--EKGYTLAAVLHDLNqACRYAS 212
                         90       100
                 ....*....|....*....|....*
gi 446585350 898 YIIDLGPEGgsgggtIVATGTPEDI 922
Cdd:PRK10253 213 HLIALREGK------IVAQGAPKEI 231
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
822-902 1.86e-07

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: 52.47  E-value: 1.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 822 GQQATTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGL--HVddiSRLL--KVLNRLVENGDTVVIIEHNLDVIKTAD 897
Cdd:cd03250  122 GEKGINLSGGQKQRISLARAVYSDA---DIYLLDDPLSAVdaHV---GRHIfeNCILGLLLNNKTRILVTHQLQLLPHAD 195

                 ....*
gi 446585350 898 YIIDL 902
Cdd:cd03250  196 QIVVL 200
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
461-582 1.88e-07

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: 52.89  E-value: 1.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 461 KEIISRLT--FLNNVGLEYlTLNRASGTLSGGEAQRIRLATQIGSRLTGVLYvlDEPSIGLH---QRDNDRLINTLKEMr 535
Cdd:cd03261  110 EEEIREIVleKLEAVGLRG-AEDLYPAELSGGMKKRVALARALALDPELLLY--DEPTAGLDpiaSGVIDDLIRSLKKE- 185
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446585350 536 dLGNTLIVVEHD-DDTMRAADYLVDIgpgageHGGQIVSSGTPQKVMK 582
Cdd:cd03261  186 -LGLTSIMVTHDlDTAFAIADRIAVL------YDGKIVAEGTPEELRA 226
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
765-922 1.94e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 53.46  E-value: 1.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 765 DGKRYNRETLevTYKGKNIADILE--------MTVEEATQF-FEN--IP--KIKRKLQTLVD-VGLGYVtLGQQATTLSG 830
Cdd:PRK13632  69 DGITISKENL--KEIRKKIGIIFQnpdnqfigATVEDDIAFgLENkkVPpkKMKDIIDDLAKkVGMEDY-LDKEPQNLSG 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 831 GEAQRVKLASELhkrSTGKSIYILDEPTTGLHVDDISRLLKVLNRLVENGD-TVVIIEHNLDVIKTADYIIDLGPEGgsg 909
Cdd:PRK13632 146 GQKQRVAIASVL---ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAILADKVIVFSEGK--- 219
                        170
                 ....*....|...
gi 446585350 910 ggtIVATGTPEDI 922
Cdd:PRK13632 220 ---LIAQGKPKEI 229
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
485-582 2.07e-07

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: 54.84  E-value: 2.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 485 GTLSGGEAQRIRLAtqigsRltgVLY------VLDEPSIGLHQRDNDRLINTLKEMRDlGNTLIVVEHDDDTMRAADYLV 558
Cdd:COG2274  610 SNLSGGQRQRLAIA-----R---ALLrnprilILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIRLADRII 680
                         90       100
                 ....*....|....*....|....
gi 446585350 559 DIgpgageHGGQIVSSGTPQKVMK 582
Cdd:COG2274  681 VL------DKGRIVEDGTHEELLA 698
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
805-922 2.23e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 53.49  E-value: 2.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 805 KRKLQTLVD-VGLGYVTLGQQATTLSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLhvDDISR--LLKVLNRL-VENG 880
Cdd:PRK13634 122 KQKAREMIElVGLPEELLARSPFELSGGQMRRVAIAGVL---AMEPEVLVLDEPTAGL--DPKGRkeMMEMFYKLhKEKG 196
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446585350 881 DTVVIIEHNL-DVIKTADYIIDLGPEggsgggTIVATGTPEDI 922
Cdd:PRK13634 197 LTTVLVTHSMeDAARYADQIVVMHKG------TVFLQGTPREI 233
cbiO PRK13637
energy-coupling factor transporter ATPase;
444-587 2.68e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 53.13  E-value: 2.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 444 KNIDLSEQDqaIANQILKEIisrltflNNVGLEYLTL-NRASGTLSGGEAQRIRLATQIGSRLTgVLyVLDEPSIGLHQR 522
Cdd:PRK13637 110 INLGLSEEE--IENRVKRAM-------NIVGLDYEDYkDKSPFELSGGQKRRVAIAGVVAMEPK-IL-ILDEPTAGLDPK 178
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446585350 523 DNDRLINTLKEMRD-LGNTLIVVEHD-DDTMRAADYLVDIgpgageHGGQIVSSGTPQKVMKDKKSL 587
Cdd:PRK13637 179 GRDEILNKIKELHKeYNMTIILVSHSmEDVAKLADRIIVM------NKGKCELQGTPREVFKEVETL 239
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
487-560 2.73e-07

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: 54.21  E-value: 2.73e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446585350  487 LSGGEAQRIRLAtQIGSRLTGVLyVLDEPSIGLHQRDNDRLINTLKEMRDlGNTLIVVEHDDDTMRAADYLVDI 560
Cdd:TIGR02857 459 LSGGQAQRLALA-RAFLRDAPLL-LLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAALADRIVVL 529
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
440-586 3.08e-07

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: 52.34  E-value: 3.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 440 LNYYKNIDLSEQDQAIAN-QILKEIISRLTFLnnvGLEYLtLNRASGTLSGGEAQRIRLATQIgsRLTGVLYVLDEPSIG 518
Cdd:cd03299   86 MTVYKNIAYGLKKRKVDKkEIERKVLEIAEML---GIDHL-LNRKPETLSGGEQQRVAIARAL--VVNPKILLLDEPFSA 159
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 519 LHQRDNDRLINTLKEMRD-LGNTLIVVEHDDDTMRA-ADYLVDIgpgageHGGQIVSSGTPQKVMKDKKS 586
Cdd:cd03299  160 LDVRTKEKLREELKKIRKeFGVTVLHVTHDFEEAWAlADKVAIM------LNGKLIQVGKPEEVFKKPKN 223
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
817-929 3.14e-07

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: 52.54  E-value: 3.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 817 GYVTL-GQQATTLSGGEAQRVKLASELHKRSTgksIYILDEPTTGLhvDDISRLL--KVLNRLVEnGDTVVIIEHNLDVI 893
Cdd:cd03249  128 GYDTLvGERGSQLSGGQKQRIAIARALLRNPK---ILLLDEATSAL--DAESEKLvqEALDRAMK-GRTTIVIAHRLSTI 201
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446585350 894 KTADYIIDLGPEGgsgggtIVATGTPEDIAQTKSSY 929
Cdd:cd03249  202 RNADLIAVLQNGQ------VVEQGTHDELMAQKGVY 231
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
828-922 3.32e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 52.88  E-value: 3.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 828 LSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLHVDDISRLLKVLNRLVEN-GDTVVIIEHNLDVI-KTADYIIDLgpe 905
Cdd:PRK13652 138 LSGGEKKRVAIAGVI---AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVpEMADYIYVM--- 211
                         90
                 ....*....|....*..
gi 446585350 906 ggsGGGTIVATGTPEDI 922
Cdd:PRK13652 212 ---DKGRIVAYGTVEEI 225
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
775-902 3.63e-07

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: 51.71  E-value: 3.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 775 EVTYKGKNIAD------------------ILEMTVEE----ATQFFENIPKIKRKLQTLVDVGLGYVtLGQQATTLSGGE 832
Cdd:COG4133   58 EVLWNGEPIRDaredyrrrlaylghadglKPELTVREnlrfWAALYGLRADREAIDEALEAVGLAGL-ADLPVRQLSAGQ 136
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 833 AQRVKLASELhkrSTGKSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHNLDVIkTADYIIDL 902
Cdd:COG4133  137 KRRVALARLL---LSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLEL-AAARVLDL 202
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
828-900 3.83e-07

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: 51.03  E-value: 3.83e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446585350 828 LSGGEAQRVKLASELHKRstgKSIYILDEPTTGLhvDDISR--LLKVLNRLVEN-GDTVVIIEHNLDVIKT-ADYII 900
Cdd:cd03229  101 LSGGQQQRVALARALAMD---PDVLLLDEPTSAL--DPITRreVRALLKSLQAQlGITVVLVTHDLDEAARlADRVV 172
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
793-930 3.93e-07

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: 52.23  E-value: 3.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 793 EATQFFENIPKikrklqtlvdvglGYVT-LGQQATTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHVDDISRLLK 871
Cdd:cd03251  116 NAHEFIMELPE-------------GYDTvIGERGVKLSGGQRQRIAIARALLKDP---PILILDEATSALDTESERLVQA 179
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446585350 872 VLNRLVENgDTVVIIEHNLDVIKTADYIIDLgpeggsGGGTIVATGTPEDIAQTKSSYT 930
Cdd:cd03251  180 ALERLMKN-RTTFVIAHRLSTIENADRIVVL------EDGKIVERGTHEELLAQGGVYA 231
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
821-902 4.16e-07

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 53.63  E-value: 4.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 821 LGQQATTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLhvdDIS---RLLKVLNRLVENGDTVVIIEHNLDVIktaD 897
Cdd:COG1245  206 LDRDISELSGGELQRVAIAAALLRDA---DFYFFDEPSSYL---DIYqrlNVARLIRELAEEGKYVLVVEHDLAIL---D 276

                 ....*
gi 446585350 898 YIIDL 902
Cdd:COG1245  277 YLADY 281
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
815-899 5.41e-07

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 53.31  E-value: 5.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 815 GLGYvTLGQQATTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHVDDISRLLKVLNRLVeNGDTVVIIEHNLDVIK 894
Cdd:PRK11174 474 GLDT-PIGDQAAGLSVGQAQRLALARALLQPC---QLLLLDEPTASLDAHSEQLVMQALNAAS-RRQTTLMVTHQLEDLA 548

                 ....*
gi 446585350 895 TADYI 899
Cdd:PRK11174 549 QWDQI 553
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
485-582 5.98e-07

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: 53.21  E-value: 5.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 485 GTLSGGEAQRIRLAtqigsR-LTG--VLYVLDEPSIGLhqrDND---RLINTLKEMRDLGNTLIVVEHDDDTMRAADYLV 558
Cdd:COG4618  466 ARLSGGQRQRIGLA-----RaLYGdpRLVVLDEPNSNL---DDEgeaALAAAIRALKARGATVVVITHRPSLLAAVDKLL 537
                         90       100
                 ....*....|....*....|....
gi 446585350 559 DIgpgageHGGQIVSSGTPQKVMK 582
Cdd:COG4618  538 VL------RDGRVQAFGPRDEVLA 555
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
469-563 6.31e-07

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 50.97  E-value: 6.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 469 FLNNVGLEYLTLNRASGTLSGGEAQRIRL--ATQIGSRltgVLyVLDEPSIGLHQrDNDRLINTL--KEMRDLGNTLIVV 544
Cdd:COG4619  113 LLERLGLPPDILDKPVERLSGGERQRLALirALLLQPD---VL-LLDEPTSALDP-ENTRRVEELlrEYLAEEGRAVLWV 187
                         90       100
                 ....*....|....*....|
gi 446585350 545 EHDDD-TMRAADYLVDIGPG 563
Cdd:COG4619  188 SHDPEqIERVADRVLTLEAG 207
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
805-891 6.36e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 52.40  E-value: 6.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 805 KRKLQTLVDVGLGYVTLGQQATTLSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVV 884
Cdd:PRK13651 143 KRAAKYIELVGLDESYLQRSPFELSGGQKRRVALAGIL---AMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTII 219

                 ....*..
gi 446585350 885 IIEHNLD 891
Cdd:PRK13651 220 LVTHDLD 226
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
469-600 8.35e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 52.16  E-value: 8.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 469 FLNNVGLEYLTLNRASGTLSGGEAQRIRLAtqigsrltGVL------YVLDEPSIGLHQRDNDRLINTLKEMRDLGNTLI 542
Cdd:PRK13631 159 YLNKMGLDDSYLERSPFGLSGGQKRRVAIA--------GILaiqpeiLIFDEPTAGLDPKGEHEMMQLILDAKANNKTVF 230
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446585350 543 VVEHD-DDTMRAADYLVDIGPGagehggQIVSSGTPQKVMKDKKSLTGQYLSGKKRIDV 600
Cdd:PRK13631 231 VITHTmEHVLEVADEVIVMDKG------KILKTGTPYEIFTDQHIINSTSIQVPRVIQV 283
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
445-583 8.37e-07

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 52.92  E-value: 8.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 445 NIDLSEQ--DQAIANQILKEIISRLTflnnVGLEYLTLNRASGtLSGGEAQRIRLATQIGSrlTGVLYVLDEPSIGLHQR 522
Cdd:PRK11174 447 NPDASDEqlQQALENAWVSEFLPLLP----QGLDTPIGDQAAG-LSVGQAQRLALARALLQ--PCQLLLLDEPTASLDAH 519
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446585350 523 DNDRLINTLKEMRdLGNTLIVVEHDDDTMRAADYLVDIgpgageHGGQIVSSGTPQKVMKD 583
Cdd:PRK11174 520 SEQLVMQALNAAS-RRQTTLMVTHQLEDLAQWDQIWVM------QDGQIVQQGDYAELSQA 573
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
805-939 8.38e-07

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 51.51  E-value: 8.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 805 KRKLQTLVDVGLGYVTLGQQATTLSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVV 884
Cdd:PRK10619 130 ERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARAL---AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMV 206
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446585350 885 IIEHNLDVIK-TADYIIDLGPEGgsgggtIVATGTPEDI-AQTKSSYTGKYLKEVLE 939
Cdd:PRK10619 207 VVTHEMGFARhVSSHVIFLHQGK------IEEEGAPEQLfGNPQSPRLQQFLKGSLK 257
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
824-901 8.73e-07

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


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 50.26  E-value: 8.73e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446585350 824 QATTLSGGEAQRVKLASELHKRSTgksIYILDEPTTGLHVDDISRLLKVLNRLVENGD-TVVIIEHNLDVIktaDYIID 901
Cdd:cd03222   68 QYIDLSGGELQRVAIAAALLRNAT---FYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVL---DYLSD 140
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
811-902 9.23e-07

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 50.81  E-value: 9.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 811 LVDVGLGYVtLGQQATTLSGGEAQRVKLAselhkRS--TGKSIYILDEPT------TGlhvDDISRLLKVLNRlvENGDT 882
Cdd:COG1136  129 LERVGLGDR-LDHRPSQLSGGQQQRVAIA-----RAlvNRPKLILADEPTgnldskTG---EEVLELLRELNR--ELGTT 197
                         90       100
                 ....*....|....*....|
gi 446585350 883 VVIIEHNLDVIKTADYIIDL 902
Cdd:COG1136  198 IVMVTHDPELAARADRVIRL 217
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
828-888 9.48e-07

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: 50.24  E-value: 9.48e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446585350 828 LSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLhvDDIS--RLLKVLNRLVENGDTVVIIEH 888
Cdd:cd03213  112 LSGGERKRVSIALEL---VSNPSLLFLDEPTSGL--DSSSalQVMSLLRRLADTGRTIICSIH 169
cbiO PRK13643
energy-coupling factor transporter ATPase;
814-924 1.11e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 51.27  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 814 VGLGYVTLGQQATTLSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHNL-DV 892
Cdd:PRK13643 131 VGLADEFWEKSPFELSGGQMRRVAIAGIL---AMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMdDV 207
                         90       100       110
                 ....*....|....*....|....*....|..
gi 446585350 893 IKTADYIIDLGPEGgsgggtIVATGTPEDIAQ 924
Cdd:PRK13643 208 ADYADYVYLLEKGH------IISCGTPSDVFQ 233
cbiO PRK13645
energy-coupling factor transporter ATPase;
482-602 1.11e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 51.55  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 482 RASGTLSGGEAQRIRLATQIGsrLTGVLYVLDEPSIGLHQRDNDRLINTLKEM-RDLGNTLIVVEHD-DDTMRAADYLVD 559
Cdd:PRK13645 146 RSPFELSGGQKRRVALAGIIA--MDGNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNmDQVLRIADEVIV 223
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446585350 560 IgpgageHGGQIVSSGTPQKVMKDKKSLTgqylsgKKRIDVPE 602
Cdd:PRK13645 224 M------HEGKVISIGSPFEIFSNQELLT------KIEIDPPK 254
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
789-888 1.19e-06

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 52.36  E-value: 1.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  789 MTVEEATQFF------ENIPKIKRKL---QTLVDVGLG-----YVTLGQQATTLSGGEAQRVKLASELhkrSTGKSIYIL 854
Cdd:TIGR00955 114 LTVREHLMFQahlrmpRRVTKKEKRErvdEVLQALGLRkcantRIGVPGRVKGLSGGERKRLAFASEL---LTDPPLLFC 190
                          90       100       110
                  ....*....|....*....|....*....|....
gi 446585350  855 DEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEH 888
Cdd:TIGR00955 191 DEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
828-922 1.19e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 51.23  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 828 LSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHNLDVIKT-ADYIIDLGPEG 906
Cdd:PRK13639 138 LSGGQKKRVAIAGILAMKP---EIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVyADKVYVMSDGK 214
                         90
                 ....*....|....*.
gi 446585350 907 gsgggtIVATGTPEDI 922
Cdd:PRK13639 215 ------IIKEGTPKEV 224
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
826-926 1.33e-06

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 50.88  E-value: 1.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 826 TTLSGGEAQRVKLASEL----HKRSTGKSIYILDEPTTGLhvdDIS---RLLKVLNRLVENGDTVVIIEH--NLdVIKTA 896
Cdd:COG4559  132 QTLSGGEQQRVQLARVLaqlwEPVDGGPRWLFLDEPTSAL---DLAhqhAVLRLARQLARRGGGVVAVLHdlNL-AAQYA 207
                         90       100       110
                 ....*....|....*....|....*....|
gi 446585350 897 DYIIDLgpeggsGGGTIVATGTPEDIAQTK 926
Cdd:COG4559  208 DRILLL------HQGRLVAQGTPEEVLTDE 231
cbiO PRK13640
energy-coupling factor transporter ATPase;
790-922 2.06e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 50.57  E-value: 2.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 790 TVEEATQF-FENIPKIKRKLQTLV-----DVG-LGYVTlgQQATTLSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLH 862
Cdd:PRK13640 101 TVGDDVAFgLENRAVPRPEMIKIVrdvlaDVGmLDYID--SEPANLSGGQKQRVAIAGIL---AVEPKIIILDESTSMLD 175
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446585350 863 VDDISRLLKVLNRL-VENGDTVVIIEHNLDVIKTADYIIDLGPEGgsgggtIVATGTPEDI 922
Cdd:PRK13640 176 PAGKEQILKLIRKLkKKNNLTVISITHDIDEANMADQVLVLDDGK------LLAQGSPVEI 230
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
485-586 2.17e-06

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 51.65  E-value: 2.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 485 GTLSGGEAQRIRLATQIGSrlTGVLYVLDEPSIGLHQRDNDRLINTLKEMRDLGNTLIVVEHDDDTMRAADYLVDIgpga 564
Cdd:PRK10535 143 SQLSGGQQQRVSIARALMN--GGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEI---- 216
                         90       100
                 ....*....|....*....|..
gi 446585350 565 geHGGQIVSSGTPQKVMKDKKS 586
Cdd:PRK10535 217 --RDGEIVRNPPAQEKVNVAGG 236
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
821-890 2.21e-06

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 49.93  E-value: 2.21e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446585350 821 LGQQATTLSGGEAQRVKLA-------SELHKRSTgksIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHNL 890
Cdd:PRK03695 120 LGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQ---LLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDL 193
cbiO PRK13643
energy-coupling factor transporter ATPase;
428-596 2.74e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 50.12  E-value: 2.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 428 IGEVVEYSISQAL--NYYKNIDLSEQDQAIANQILKEIISRLtfLNNVGLEYLTLNRASGTLSGGEAQRIRLATQIGsrL 505
Cdd:PRK13643  86 VGVVFQFPESQLFeeTVLKDVAFGPQNFGIPKEKAEKIAAEK--LEMVGLADEFWEKSPFELSGGQMRRVAIAGILA--M 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 506 TGVLYVLDEPSIGLHQRDNDRLINTLKEMRDLGNTLIVVEH-DDDTMRAADYLVDIgpgageHGGQIVSSGTPQKVMKDK 584
Cdd:PRK13643 162 EPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHlMDDVADYADYVYLL------EKGHIISCGTPSDVFQEV 235
                        170
                 ....*....|..
gi 446585350 585 KSLTGQYLSGKK 596
Cdd:PRK13643 236 DFLKAHELGVPK 247
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
622-859 2.88e-06

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: 48.03  E-value: 2.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  622 LKGIDVDIPLSIMTVVTGVSGSGKSSLVnevlyKSLAqkinkskvkpGLYDKIEGIDQLDKIiDIDQSPIGRTPRSnpat 701
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLL-----KLIA----------GLLSPTEGTILLDGQ-DLTDDERKSLRKE---- 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  702 ytgvfddIRDVFAqtneakirgyqkgrfsfnvkggrceackgdgiikiEMHFLPDVYVpcevcdgkrynRETL-EVTYKG 780
Cdd:pfam00005  61 -------IGYVFQ-----------------------------------DPQLFPRLTV-----------RENLrLGLLLK 87
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446585350  781 KNIADILEMTVEEATQFFENIPKIKRKLqtlvdvglgyvtlGQQATTLSGGEAQRVKLASELHKRSTgksIYILDEPTT 859
Cdd:pfam00005  88 GLSKREKDARAEEALEKLGLGDLADRPV-------------GERPGTLSGGQRQRVAIARALLTKPK---LLLLDEPTA 150
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
487-619 2.96e-06

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 49.76  E-value: 2.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 487 LSGGEAQRIRLATQIGsrLTGVLYVLDEPSIGLHQRDNDRLINTLKEMRD-LGNTLIVVEHD-DDTMRAADYLVDIgpgA 564
Cdd:PRK11831 144 LSGGMARRAALARAIA--LEPDLIMFDEPFVGQDPITMGVLVKLISELNSaLGVTCVVVSHDvPEVLSIADHAYIV---A 218
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446585350 565 GEHggqIVSSGTPQKVMKDKKSLTGQYLSGKKRIDVPeYRRPASDRKISIRGARS 619
Cdd:PRK11831 219 DKK---IVAHGSAQALQANPDPRVRQFLDGIADGPVP-FRYPAGDYHADLLGGGS 269
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
828-894 3.08e-06

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: 49.50  E-value: 3.08e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 828 LSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLH---VDDISRLLKVLNRlvENGDTVVIIEHNLDVIK 894
Cdd:cd03258  141 LSGGQKQRVGIARAL---ANNPKVLLCDEATSALDpetTQSILALLRDINR--ELGLTIVLITHEMEVVK 205
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
789-929 3.24e-06

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: 49.26  E-value: 3.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 789 MTVEEATQF-----FENIPKIKRK-LQTLVDVGLGYVtLGQQATTLSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLH 862
Cdd:cd03299   86 MTVYKNIAYglkkrKVDKKEIERKvLEIAEMLGIDHL-LNRKPETLSGGEQQRVAIARAL---VVNPKILLLDEPFSALD 161
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446585350 863 VDDISRLLKVLNRLVENGDTVVI-IEHNLDVIKT-ADYIIDLGPEGgsgggtIVATGTPEDIAQTKSSY 929
Cdd:cd03299  162 VRTKEKLREELKKIRKEFGVTVLhVTHDFEEAWAlADKVAIMLNGK------LIQVGKPEEVFKKPKNE 224
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
786-900 3.42e-06

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: 49.25  E-value: 3.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 786 ILEMTVEEATQFFENIPKIKRK-------LQTLVDV-GLGYVT-LGQQATTLSGGEAQRVKLASELHKRStgkSIYILDE 856
Cdd:cd03290   90 LLNATVEENITFGSPFNKQRYKavtdacsLQPDIDLlPFGDQTeIGERGINLSGGQRQRICVARALYQNT---NIVFLDD 166
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446585350 857 PTTGLHVDDISRLLK--VLNRLVENGDTVVIIEHNLDVIKTADYII 900
Cdd:cd03290  167 PFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPHADWII 212
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
482-547 3.97e-06

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 49.50  E-value: 3.97e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446585350 482 RASGTLSGGEAQRIRLATQIGSRltGVLYVLDEPSIGLHQRDNDRLINTLKEMRDLGNTLIVVEHD 547
Cdd:PRK15056 138 RQIGELSGGQKKRVFLARAIAQQ--GQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHN 201
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
826-892 4.40e-06

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 49.15  E-value: 4.40e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446585350 826 TTLSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLHVDDISRLLKVLNRLV-ENGDTVVIIEHNLDV 892
Cdd:PRK11701 150 TTFSGGMQQRLQIARNL---VTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVrELGLAVVIVTHDLAV 214
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
796-901 4.53e-06

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 49.29  E-value: 4.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 796 QFFENIPK---------IKRK-----LQTLVDV-GLGYVtLGQQATTLSGGEAQRVKLASELHKRSTgksIYILDEPTTG 860
Cdd:cd03236   94 QYVDLIPKavkgkvgelLKKKdergkLDELVDQlELRHV-LDRNIDQLSGGELQRVAIAAALARDAD---FYFFDEPSSY 169
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446585350 861 LHVDDISRLLKVLNRLVENGDTVVIIEHNLDVIktaDYIID 901
Cdd:cd03236  170 LDIKQRLNAARLIRELAEDDNYVLVVEHDLAVL---DYLSD 207
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
487-548 5.32e-06

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 48.62  E-value: 5.32e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446585350 487 LSGGEAQRIRLATQIGSRlTGVLYVlDEPSIGLHQRDNDRLINTLKEM-RDLGNTLIVVEHDD 548
Cdd:PRK10584 147 LSGGEQQRVALARAFNGR-PDVLFA-DEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDL 207
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
828-900 5.55e-06

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: 49.28  E-value: 5.55e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446585350 828 LSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLHV---DDISRLLKVLNRlvENGDTVVIIEHNLDVIK-TADYII 900
Cdd:COG0444  151 LSGGMRQRVMIARAL---ALEPKLLIADEPTTALDVtiqAQILNLLKDLQR--ELGLAILFITHDLGVVAeIADRVA 222
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
821-902 5.97e-06

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 50.19  E-value: 5.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 821 LGQQATTLSGGEAQRVKLASELHKRSTgksIYILDEPTTGLHVDDISRLLKVLNRLVENgDTVVIIEHNLDVIktaDYII 900
Cdd:PRK13409 206 LDRDISELSGGELQRVAIAAALLRDAD---FYFFDEPTSYLDIRQRLNVARLIRELAEG-KYVLVVEHDLAVL---DYLA 278

                 ..
gi 446585350 901 DL 902
Cdd:PRK13409 279 DN 280
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
775-900 6.10e-06

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: 48.33  E-value: 6.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 775 EVTYKGKNIADILE----------MTVEEATQF----FENI---PKI-----KRKLQTLVDVGLGYVTLG------QQAT 826
Cdd:cd03260   61 EVLLDGKDIYDLDVdvlelrrrvgMVFQKPNPFpgsiYDNVaygLRLhgiklKEELDERVEEALRKAALWdevkdrLHAL 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 827 TLSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLhvDDIS-----RLLKVLNRLVengdTVVIIEHNL-DVIKTADYII 900
Cdd:cd03260  141 GLSGGQQQRLCLARAL---ANEPEVLLLDEPTSAL--DPIStakieELIAELKKEY----TIVIVTHNMqQAARVADRTA 211
cbiO PRK13649
energy-coupling factor transporter ATPase;
805-924 8.73e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 48.59  E-value: 8.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 805 KRKLQTLVDVGLGYVTLGQQATTLSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVV 884
Cdd:PRK13649 123 ALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGIL---AMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIV 199
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446585350 885 IIEHNL-DVIKTADYIIDLGPEGgsgggtIVATGTPEDIAQ 924
Cdd:PRK13649 200 LVTHLMdDVANYADFVYVLEKGK------LVLSGKPKDIFQ 234
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
805-902 8.90e-06

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 49.72  E-value: 8.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 805 KRKLQTLVDVGLGYvTLGQQATTLSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVV 884
Cdd:PRK10535 123 LRAQELLQRLGLED-RVEYQPSQLSGGQQQRVSIARAL---MNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVI 198
                         90
                 ....*....|....*...
gi 446585350 885 IIEHNLDVIKTADYIIDL 902
Cdd:PRK10535 199 IVTHDPQVAAQAERVIEI 216
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
827-893 9.19e-06

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: 48.16  E-value: 9.19e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446585350 827 TLSGGEAQRVKLAselhkRS--TGKSIYILDEPTTGLhvDDISR--LLKVLNRLVENGDTVVI-IEHNLDVI 893
Cdd:COG1119  142 TLSQGEQRRVLIA-----RAlvKDPELLILDEPTAGL--DLGARelLLALLDKLAAEGAPTLVlVTHHVEEI 206
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
801-900 1.20e-05

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 49.25  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 801 IPKIKRKLQTLVdvglgyvtlGQQATTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHVDDISRLLKVLNRLVENg 880
Cdd:PRK11176 463 INKMDNGLDTVI---------GENGVLLSGGQRQRIAIARALLRDS---PILILDEATSALDTESERAIQAALDELQKN- 529
                         90       100
                 ....*....|....*....|
gi 446585350 881 DTVVIIEHNLDVIKTADYII 900
Cdd:PRK11176 530 RTSLVIAHRLSTIEKADEIL 549
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
827-899 1.21e-05

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 48.86  E-value: 1.21e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446585350 827 TLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHNLD-VIKTADYI 899
Cdd:COG1129  140 DLSVAQQQLVEIARALSRDA---RVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDeVFEIADRV 210
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
821-900 1.22e-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: 46.92  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 821 LGQQattLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHVDDISRLLKVLNRLVENgDTVVIIEHNLDVIKTADYII 900
Cdd:cd03247   95 LGRR---FSGGERQRLALARILLQDA---PIVLLDEPTVGLDPITERQLLSLIFEVLKD-KTLIWITHHLTGIEHMDKIL 167
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
817-899 1.33e-05

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: 48.98  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 817 GYVT-LGQQATTLSGGEAQRVKLASELHkrstGK-SIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHNLDVIK 894
Cdd:COG4618  456 GYDTrIGEGGARLSGGQRQRIGLARALY----GDpRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLA 531

                 ....*
gi 446585350 895 TADYI 899
Cdd:COG4618  532 AVDKL 536
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
470-592 1.48e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 47.76  E-value: 1.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 470 LNNVGLEYLTlNRASGTLSGGEAQRIRLAtqigsrltGVL------YVLDEPSIGLHQRDNDRLINTLKEMRDLGNTLIV 543
Cdd:PRK13639 122 LKAVGMEGFE-NKPPHHLSGGQKKRVAIA--------GILamkpeiIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIII 192
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446585350 544 VEHDddtmraadylVDIGPGAGE-----HGGQIVSSGTPQKVMKDKKSLTGQYL 592
Cdd:PRK13639 193 STHD----------VDLVPVYADkvyvmSDGKIIKEGTPKEVFSDIETIRKANL 236
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
467-547 1.52e-05

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 47.50  E-value: 1.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 467 LTFLNNVGLEYLTLNRASgTLSGGEAQRIRLATQIGSRLTGVLyvLDEPSIGLHQRDNDRLINTLKEM-RDLGNTLIVVE 545
Cdd:PRK11629 127 LEMLAAVGLEHRANHRPS-ELSGGERQRVAIARALVNNPRLVL--ADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVT 203

                 ..
gi 446585350 546 HD 547
Cdd:PRK11629 204 HD 205
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
819-900 1.62e-05

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: 46.27  E-value: 1.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 819 VTLGQQattLSGGEAQRVKLASELHkrsTGKSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHNLD-VIKTAD 897
Cdd:cd03215   99 IALSSL---LSGGNQQKVVLARWLA---RDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDeLLGLCD 172

                 ...
gi 446585350 898 YII 900
Cdd:cd03215  173 RIL 175
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
827-899 1.66e-05

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 48.48  E-value: 1.66e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446585350 827 TLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHNLDVIKT-ADYI 899
Cdd:COG3845  141 DLSVGEQQRVEILKALYRGA---RILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAiADRV 211
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
820-932 1.68e-05

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 47.20  E-value: 1.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 820 TLGQqatTLSGGEAQRVKLASELhkrSTGKSIYILDEPTTGlhVDDISRL--LKVLNRLVENGDTVVIIEHN----LDVI 893
Cdd:PRK10895 133 SMGQ---SLSGGERRRVEIARAL---AANPKFILLDEPFAG--VDPISVIdiKRIIEHLRDSGLGVLITDHNvretLAVC 204
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446585350 894 KTAdYIIDlgpeggsgGGTIVATGTPEDI---AQTKSSYTGK 932
Cdd:PRK10895 205 ERA-YIVS--------QGHLIAHGTPTEIlqdEHVKRVYLGE 237
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
428-569 1.73e-05

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: 46.90  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 428 IGEVV-EYSISQALNYYKNID--LSEQDQAIANQILKEIISRLtflnnvGLEYLtLNRASGTLSGGEAQRIRLATQIGSR 504
Cdd:cd03297   77 IGLVFqQYALFPHLNVRENLAfgLKRKRNREDRISVDELLDLL------GLDHL-LNRYPAQLSGGEKQRVALARALAAQ 149
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446585350 505 LTgvLYVLDEPSIGLHQRDNDRLINTLKEM-RDLGNTLIVVEHDDDTM-RAADYLVDIGPGAGEHGG 569
Cdd:cd03297  150 PE--LLLLDEPFSALDRALRLQLLPELKQIkKNLNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
481-581 1.85e-05

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 48.30  E-value: 1.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 481 NRASGTLSGGEAQRIRLATQIgSRLTGVLyVLDEPSIGLhqrDNDRLINTLKEMRDL---GNTLIVVEHD-DDTMRAADY 556
Cdd:PRK09536 134 DRPVTSLSGGERQRVLLARAL-AQATPVL-LLDEPTASL---DINHQVRTLELVRRLvddGKTAVAAIHDlDLAARYCDE 208
                         90       100
                 ....*....|....*....|....*
gi 446585350 557 LVDIGpgagehGGQIVSSGTPQKVM 581
Cdd:PRK09536 209 LVLLA------DGRVRAAGPPADVL 227
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
817-900 1.90e-05

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 48.42  E-value: 1.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 817 GYVTL-GQQATTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHVDDISRLLKVLNRLVEnGDTVVIIEHNLDVIKT 895
Cdd:PRK13657 460 GYDTVvGERGRQLSGGERQRLAIARALLKDP---PILILDEATSALDVETEAKVKAALDELMK-GRTTFIIAHRLSTVRN 535

                 ....*
gi 446585350 896 ADYII 900
Cdd:PRK13657 536 ADRIL 540
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
432-583 1.98e-05

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: 48.36  E-value: 1.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 432 VEYSISQALNYYKNIDLSEQDQAIAnQILKEiisrltflnnVGLEYLTLNRASGTLSGGEAQRI---R-LATQigSRltg 507
Cdd:COG1123  361 VGDIIAEPLRLHGLLSRAERRERVA-ELLER----------VGLPPDLADRYPHELSGGQRQRVaiaRaLALE--PK--- 424
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 508 vLYVLDEPSIGL---HQRdndRLINTLKEMRD-LGNTLIVVEHDDDTMRA-ADYLVDIgpgageHGGQIVSSGTPQKVMK 582
Cdd:COG1123  425 -LLILDEPTSALdvsVQA---QILNLLRDLQReLGLTYLFISHDLAVVRYiADRVAVM------YDGRIVEDGPTEEVFA 494

                 .
gi 446585350 583 D 583
Cdd:COG1123  495 N 495
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
798-898 2.00e-05

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 46.97  E-value: 2.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 798 FENI-------PKIKRKLQTLVDVGLGYVTLGQQA----TTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHVDDI 866
Cdd:COG2884   97 YENValplrvtGKSRKEIRRRVREVLDLVGLSDKAkalpHELSGGEQQRVAIARALVNRP---ELLLADEPTGNLDPETS 173
                         90       100       110
                 ....*....|....*....|....*....|..
gi 446585350 867 SRLLKVLNRLVENGDTVVIIEHNLDVIKTADY 898
Cdd:COG2884  174 WEIMELLEEINRRGTTVLIATHDLELVDRMPK 205
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
428-601 2.17e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 47.29  E-value: 2.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 428 IGEVVEYSISQALNYyKNIDLSEqdqaianqiLKEIISRLTflNNVGLEYLtLNRASGTLSGGEAQRIRLATQIGsrLTG 507
Cdd:PRK13632  97 IGATVEDDIAFGLEN-KKVPPKK---------MKDIIDDLA--KKVGMEDY-LDKEPQNLSGGQKQRVAIASVLA--LNP 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 508 VLYVLDEPSIGLHQRDNDRLINTLKEMRDLGN-TLIVVEHDDDTMRAADYLVDIGpgagehGGQIVSSGTPQKVMKDKKS 586
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAILADKVIVFS------EGKLIAQGKPKEILNNKEI 235
                        170
                 ....*....|....*
gi 446585350 587 LTgqylsgKKRIDVP 601
Cdd:PRK13632 236 LE------KAKIDSP 244
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
460-560 3.01e-05

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: 46.59  E-value: 3.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 460 LKEIISRLTfLNNVgleyltLNRASGTLSGGEAQRIRLATQIGSRLTgvLYVLDEPS--IGLHQRDN-DRLIntlKEMRD 536
Cdd:cd03236  120 LDELVDQLE-LRHV------LDRNIDQLSGGELQRVAIAAALARDAD--FYFFDEPSsyLDIKQRLNaARLI---RELAE 187
                         90       100
                 ....*....|....*....|....
gi 446585350 537 LGNTLIVVEHDddtMRAADYLVDI 560
Cdd:cd03236  188 DDNYVLVVEHD---LAVLDYLSDY 208
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
487-564 3.03e-05

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: 45.29  E-value: 3.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 487 LSGGEAQRIRLAtqigsRltgVLY------VLDEPSIGLHQrDNDRLIN-TLKEMRDLGNTLIVVEHDDDTMRAADYLVD 559
Cdd:cd03246   97 LSGGQRQRLGLA-----R---ALYgnprilVLDEPNSHLDV-EGERALNqAIAALKAAGATRIVIAHRPETLASADRILV 167

                 ....*
gi 446585350 560 IGPGA 564
Cdd:cd03246  168 LEDGR 172
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
805-891 3.05e-05

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 46.54  E-value: 3.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 805 KRKLQTLVDVGLGYVTlGQQATTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHVDDISRLLKVLNRLVEN-GDTV 883
Cdd:PRK09984 131 QRALQALTRVGMVHFA-HQRVSTLSGGQQQRVAIARALMQQA---KVILADEPIASLDPESARIVMDTLRDINQNdGITV 206

                 ....*...
gi 446585350 884 VIIEHNLD 891
Cdd:PRK09984 207 VVTLHQVD 214
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
828-895 3.06e-05

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: 46.25  E-value: 3.06e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446585350 828 LSGGEAQRVKLASELHKRSTgksIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHNLDVIKT 895
Cdd:cd03292  137 LSGGEQQRVAIARAIVNSPT---ILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDT 201
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
465-558 3.23e-05

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: 45.64  E-value: 3.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 465 SRLTFLNNVGLeyltlnrasgTLSGGEAQRIRLATQIGSRlTGVLyVLDEPSIGLHQRDNDRLINTLKEMRD-LGNTLIV 543
Cdd:cd03229   89 PHLTVLENIAL----------GLSGGQQQRVALARALAMD-PDVL-LLDEPTSALDPITRREVRALLKSLQAqLGITVVL 156
                         90
                 ....*....|....*.
gi 446585350 544 VEHD-DDTMRAADYLV 558
Cdd:cd03229  157 VTHDlDEAARLADRVV 172
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
10-53 3.31e-05

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 45.04  E-value: 3.31e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 446585350  10 GARAHNLKDIDIELPKNKLIVMTGLSGSGKSSLAFDTIYAEGQR 53
Cdd:cd03227    5 GRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGA 48
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
789-891 3.80e-05

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: 45.75  E-value: 3.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 789 MTVEE----ATQFFENIPKIKRKLQTLVDVGLGYVtLGQQATTLSGGEAQRVKLASELHKRSTgksIYILDEPTTGLhvD 864
Cdd:cd03297   90 LNVREnlafGLKRKRNREDRISVDELLDLLGLDHL-LNRYPAQLSGGEKQRVALARALAAQPE---LLLLDEPFSAL--D 163
                         90       100       110
                 ....*....|....*....|....*....|
gi 446585350 865 DISR--LLKVLNRLVEN-GDTVVIIEHNLD 891
Cdd:cd03297  164 RALRlqLLPELKQIKKNlNIPVIFVTHDLS 193
hmuV PRK13547
heme ABC transporter ATP-binding protein;
821-924 3.80e-05

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 46.36  E-value: 3.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 821 LGQQATTLSGGEAQRVKLASEL------HKRSTGKSIYILDEPTTGLHVDDISRLLKVLNRLVENGDT-VVIIEHNLDV- 892
Cdd:PRK13547 139 VGRDVTTLSGGELARVQFARVLaqlwppHDAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLa 218
                         90       100       110
                 ....*....|....*....|....*....|..
gi 446585350 893 IKTADYIIDLgpeggsGGGTIVATGTPEDIAQ 924
Cdd:PRK13547 219 ARHADRIAML------ADGAIVAHGAPADVLT 244
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
826-902 3.83e-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: 45.89  E-value: 3.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 826 TTLSGGEAQRVKLASELHKRstgKSIYILDEPTTGLhvDDISRlLKVLNRLVE---NGDTVVIIEHNLDVIKT-ADYIID 901
Cdd:COG4778  151 ATFSGGEQQRVNIARGFIAD---PPLLLLDEPTASL--DAANR-AVVVELIEEakaRGTAIIGIFHDEEVREAvADRVVD 224

                 .
gi 446585350 902 L 902
Cdd:COG4778  225 V 225
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
789-888 4.07e-05

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: 45.56  E-value: 4.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 789 MTVEEATQFFENIPKIKRKLQTLVDVGLGYVTlGQQATTLSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLHVDDISR 868
Cdd:cd03231   88 LSVLENLRFWHADHSDEQVEEALARVGLNGFE-DRPVAQLSAGQQRRVALARLL---LSGRPLWILDEPTTALDKAGVAR 163
                         90       100
                 ....*....|....*....|
gi 446585350 869 LLKVLNRLVENGDTVVIIEH 888
Cdd:cd03231  164 FAEAMAGHCARGGMVVLTTH 183
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
823-893 4.91e-05

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 46.15  E-value: 4.91e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446585350 823 QQATTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHNLDVI 893
Cdd:PRK13638 132 QPIQCLSHGQKKRVAIAGALVLQA---RYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLI 199
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
804-902 5.01e-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: 45.64  E-value: 5.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 804 IKRKLQTLVDVGL-GYVTlgQQATTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLhvDDIS-----RLLKVLNRlv 877
Cdd:cd03256  122 KQRALAALERVGLlDKAY--QRADQLSGGQQQRVAIARALMQQP---KLILADEPVASL--DPASsrqvmDLLKRINR-- 192
                         90       100
                 ....*....|....*....|....*.
gi 446585350 878 ENGDTVVIIEHNLDVIKT-ADYIIDL 902
Cdd:cd03256  193 EEGITVIVSLHQVDLAREyADRIVGL 218
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
828-902 5.69e-05

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: 43.98  E-value: 5.69e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446585350 828 LSGGEAQRVKLASELhkrSTGKSIYILDEPTTglHVDDISRLLkVLNRLVENGDTVVIIEHNLDVI-KTADYIIDL 902
Cdd:cd03221   71 LSGGEKMRLALAKLL---LENPNLLLLDEPTN--HLDLESIEA-LEEALKEYPGTVILVSHDRYFLdQVATKIIEL 140
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
805-900 5.73e-05

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 46.03  E-value: 5.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 805 KRKLQTLVDVGLGYVTLGQ----QATTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHVDDISRLLKVLNRLVENG 880
Cdd:PRK15056 116 KKRDRQIVTAALARVDMVEfrhrQIGELSGGQKKRVFLARAIAQQG---QVILLDEPFTGVDVKTEARIISLLRELRDEG 192
                         90       100
                 ....*....|....*....|.
gi 446585350 881 DTVVIIEHNL-DVIKTADYII 900
Cdd:PRK15056 193 KTMLVSTHNLgSVTEFCDYTV 213
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
788-888 5.95e-05

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: 45.34  E-value: 5.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 788 EMTVEEATQFFENIP-------KIKRKLqtLVDVGLGYVTLGQQATT----LSGGEAQRVKLASELhkrSTGKSIYILDE 856
Cdd:cd03234   95 GLTVRETLTYTAILRlprkssdAIRKKR--VEDVLLRDLALTRIGGNlvkgISGGERRRVSIAVQL---LWDPKVLILDE 169
                         90       100       110
                 ....*....|....*....|....*....|..
gi 446585350 857 PTTGLHVDDISRLLKVLNRLVENGDTVVIIEH 888
Cdd:cd03234  170 PTSGLDSFTALNLVSTLSQLARRNRIVILTIH 201
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
788-900 6.07e-05

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: 45.29  E-value: 6.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 788 EMTVEEATQFFENIPKIKRKL--QTLVDVGLGYVTlGQQATTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHVDD 865
Cdd:cd03268   86 NLTARENLRLLARLLGIRKKRidEVLDVVGLKDSA-KKKVKGFSLGMKQRLGIALALLGNP---DLLILDEPTNGLDPDG 161
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446585350 866 ISRLLKVLNRLVENGDTVVIIEHNL-DVIKTADYII 900
Cdd:cd03268  162 IKELRELILSLRDQGITVLISSHLLsEIQKVADRIG 197
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
440-555 6.13e-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: 45.20  E-value: 6.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 440 LNYYKNIDLSEQDQAIANQILKEIISRLTFLnnVGLEYLtLNRASGTLSGGEAQRIRLATQIGSRlTGVLyVLDEPSIGL 519
Cdd:cd03259   87 LTVAENIAFGLKLRGVPKAEIRARVRELLEL--VGLEGL-LNRYPHELSGGQQQRVALARALARE-PSLL-LLDEPLSAL 161
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446585350 520 HQRDNDRLINTLKEM-RDLGNTLIVVEHD-DDTMRAAD 555
Cdd:cd03259  162 DAKLREELREELKELqRELGITTIYVTHDqEEALALAD 199
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
470-582 6.27e-05

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 45.78  E-value: 6.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 470 LNNVGLEYLtLNRASGTLSGGEAQRIRLATQIGSRLTgvLYVLDEPSIGLHQRDNDRLINTLKEMRDLGN-TLIVVEHDD 548
Cdd:PRK13635 125 LRQVGMEDF-LNREPHRLSGGQKQRVAIAGVLALQPD--IIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDL 201
                         90       100       110
                 ....*....|....*....|....*....|....
gi 446585350 549 DTMRAADYLVDIgpgageHGGQIVSSGTPQKVMK 582
Cdd:PRK13635 202 DEAAQADRVIVM------NKGEILEEGTPEEIFK 229
cbiO PRK13649
energy-coupling factor transporter ATPase;
470-583 6.54e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 45.89  E-value: 6.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 470 LNNVGLEYLTLNRASGTLSGGEAQRIRLATqIGSRLTGVLyVLDEPSIGLHQRDNDRLINTLKEMRDLGNTLIVVEH-DD 548
Cdd:PRK13649 129 LALVGISESLFEKNPFELSGGQMRRVAIAG-ILAMEPKIL-VLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHlMD 206
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446585350 549 DTMRAADYLVDIgpgageHGGQIVSSGTPQKVMKD 583
Cdd:PRK13649 207 DVANYADFVYVL------EKGKLVLSGKPKDIFQD 235
PLN03211 PLN03211
ABC transporter G-25; Provisional
828-888 6.99e-05

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 46.80  E-value: 6.99e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446585350 828 LSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEH 888
Cdd:PLN03211 207 ISGGERKRVSIAHEM---LINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
cbiO PRK13637
energy-coupling factor transporter ATPase;
814-900 7.44e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 45.81  E-value: 7.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 814 VGLGYVTLGQQAT-TLSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLHV---DDISRLLKVLNRlvENGDTVVIIEHN 889
Cdd:PRK13637 130 VGLDYEDYKDKSPfELSGGQKRRVAIAGVV---AMEPKILILDEPTAGLDPkgrDEILNKIKELHK--EYNMTIILVSHS 204
                         90
                 ....*....|..
gi 446585350 890 L-DVIKTADYII 900
Cdd:PRK13637 205 MeDVAKLADRII 216
cbiO PRK13646
energy-coupling factor transporter ATPase;
487-602 8.09e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 45.54  E-value: 8.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 487 LSGGEAQRIRLATQIGsrLTGVLYVLDEPSIGLHQRDNDRLINTLKEMR-DLGNTLIVVEHD-DDTMRAADYLVDIgpga 564
Cdd:PRK13646 146 MSGGQMRKIAIVSILA--MNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDmNEVARYADEVIVM---- 219
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446585350 565 geHGGQIVSSGTPQKVMKDKKSLTgqylsgKKRIDVPE 602
Cdd:PRK13646 220 --KEGSIVSQTSPKELFKDKKKLA------DWHIGLPE 249
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
487-636 8.19e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 45.46  E-value: 8.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 487 LSGGEAQRIRLATQIGSRLTGVlyVLDEPSIGLHQRDNDRLINTLKEM-RDLGNTLIVVEHDDDTMRAADYLVDIgpgag 565
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPECI--IFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVEADRIIVM----- 217
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446585350 566 eHGGQIVSSGTPQKVMKDKKSLtgqylsgkKRI--DVPEYRRPASDrkisirgarsnnLKGIDVDIPLSIMTV 636
Cdd:PRK13633 218 -DSGKVVMEGTPKEIFKEVEMM--------KKIglDVPQVTELAYE------------LKKEGVDIPSDILTI 269
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
816-888 8.68e-05

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 45.08  E-value: 8.68e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446585350 816 LGYVTLGQQA----TTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEH 888
Cdd:PRK09493 121 LAKVGLAERAhhypSELSGGQQQRVAIARALAVKP---KLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTH 194
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
634-893 8.94e-05

AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.


Pssm-ID: 433102 [Multi-domain]  Cd Length: 303  Bit Score: 45.46  E-value: 8.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  634 MTVVTGVSGSGKSSLVnEVLY--KSLAQKINKSKVKPGLYDKIEGIDQL------------------------DKIIDID 687
Cdd:pfam13304   1 INVLIGPNGSGKSNLL-EALRflADFDALVIGLTDERSRNGGIGGIPSLlngidpkepiefeisefledgvryRYGLDLE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  688 QSPIGRTPRSNPATYTGVFDDIRDVFAQTNE--AKIRGYQKGRFSF--------NVKGGRCEACKGDGI-----IKIEMH 752
Cdd:pfam13304  80 REDVEEKLSSKPTLLEKRLLLREDSEEREPKfpPEAEELRLGLDVEerielslsELSDLISGLLLLSIIsplsfLLLLDE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  753 FLPDVYVPCEVcDGKRY-----NRETLEVTYKGKNIADILEMTVEEATQF-FENIPKIKRKLQTLVDVGLGYvtlGQQAT 826
Cdd:pfam13304 160 GLLLEDWAVLD-LAADLalfpdLKELLQRLVRGLKLADLNLSDLGEGIEKsLLVDDRLRERGLILLENGGGG---ELPAF 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446585350  827 TLSGGEAQRVKLASELHKRSTGKSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHNLDVI 893
Cdd:pfam13304 236 ELSDGTKRLLALLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLLL 302
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
487-558 1.02e-04

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: 43.91  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 487 LSGGEAQRIRLA------TQIgsrltgvlYVLDEPSIGLhqrDND---RLINTLKEMRDlGNTLIVVEHDDDTMRAADYL 557
Cdd:cd03228   97 LSGGQRQRIAIArallrdPPI--------LILDEATSAL---DPEteaLILEALRALAK-GKTVIVIAHRLSTIRDADRI 164

                 .
gi 446585350 558 V 558
Cdd:cd03228  165 I 165
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
828-894 1.16e-04

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 45.85  E-value: 1.16e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446585350 828 LSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLHVDDISRLLKVLNRLV-ENGDTVVIIEHNLDVIK 894
Cdd:PRK15134 157 LSGGERQRVMIAMAL---LTRPELLIADEPTTALDVSVQAQILQLLRELQqELNMGLLFITHNLSIVR 221
cbiO PRK13646
energy-coupling factor transporter ATPase;
784-927 1.21e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 45.16  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 784 ADILEMTVEEATQF----FE-NIPKIK-RKLQTLVDVGLGYVTLGQQATTLSGGEAQRVKLASELhkrSTGKSIYILDEP 857
Cdd:PRK13646  96 SQLFEDTVEREIIFgpknFKmNLDEVKnYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSIL---AMNPDIIVLDEP 172
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446585350 858 TTGL---HVDDISRLLKVLNrlVENGDTVVIIEHNL-DVIKTADYIIDLgpeggsGGGTIVATGTPEDIAQTKS 927
Cdd:PRK13646 173 TAGLdpqSKRQVMRLLKSLQ--TDENKTIILVSHDMnEVARYADEVIVM------KEGSIVSQTSPKELFKDKK 238
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
772-902 1.27e-04

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 46.18  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  772 ETLEVTYKGKNIADILEMTVEEATQFFENIPKIKRKLQTLVdvglgyvtlGQQATTLSGGEAQRVKLASELHKRStgkSI 851
Cdd:PTZ00265  533 ELIEMRKNYQTIKDSEVVDVSKKVLIHDFVSALPDKYETLV---------GSNASKLSGGQKQRISIARAIIRNP---KI 600
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446585350  852 YILDEPTTGLhvDDISRLL--KVLNRLVENGDTV-VIIEHNLDVIKTADYIIDL 902
Cdd:PTZ00265  601 LILDEATSSL--DNKSEYLvqKTINNLKGNENRItIIIAHRLSTIRYANTIFVL 652
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
485-567 1.31e-04

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: 44.14  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 485 GTLSGGE------AQRIRLATQIGSRLtGVLyVLDEPSIGL-HQRDNDRLINTLKEMRDLGN-TLIVVEHDDDTMRAADY 556
Cdd:cd03240  114 GRCSGGEkvlaslIIRLALAETFGSNC-GIL-ALDEPTTNLdEENIEESLAEIIEERKSQKNfQLIVITHDEELVDAADH 191
                         90
                 ....*....|.
gi 446585350 557 LVDIGPGAGEH 567
Cdd:cd03240  192 IYRVEKDGRQK 202
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
789-886 1.42e-04

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: 44.11  E-value: 1.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 789 MTVEEATQFF---ENIPKIKRK---LQTLVDVGLGYVtLGQQATTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLh 862
Cdd:cd03264   87 FTVREFLDYIawlKGIPSKEVKarvDEVLELVNLGDR-AKKKIGSLSGGMRRRVGIAQALVGDP---SILIVDEPTAGL- 161
                         90       100
                 ....*....|....*....|....
gi 446585350 863 vdDISRLLKVLNRLVENGDTVVII 886
Cdd:cd03264  162 --DPEERIRFRNLLSELGEDRIVI 183
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
456-592 1.57e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 44.69  E-value: 1.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 456 ANQILKEIISRltflnnVGLEYLTLNRASGTLSGGEAQRIRLAtqigsrltGVL------YVLDEPSIGLHQRDNDRLIN 529
Cdd:PRK13651 141 AKKRAAKYIEL------VGLDESYLQRSPFELSGGQKRRVALA--------GILamepdfLVFDEPTAGLDPQGVKEILE 206
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446585350 530 TLKEMRDLGNTLIVVEHDDD-----TMRAADYlvdigpgageHGGQIVSSGTPQKVMKDKKSLTGQYL 592
Cdd:PRK13651 207 IFDNLNKQGKTIILVTHDLDnvlewTKRTIFF----------KDGKIIKDGDTYDILSDNKFLIENNM 264
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
427-577 1.67e-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: 43.90  E-value: 1.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 427 NIGEVVEY-SISQALNYYKNIDLSEQDQAIANQILKEIISRLtflnnvgLEYLTL----NRASGTLSGGEAQRIRLATQI 501
Cdd:cd03265   74 RIGIVFQDlSVDDELTGWENLYIHARLYGVPGAERRERIDEL-------LDFVGLleaaDRLVKTYSGGMRRRLEIARSL 146
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446585350 502 GSRlTGVLYvLDEPSIGLHQRDNDRLINTLKEM-RDLGNTLIVVEHDddtMRAADYLVDigPGAGEHGGQIVSSGTP 577
Cdd:cd03265  147 VHR-PEVLF-LDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHY---MEEAEQLCD--RVAIIDHGRIIAEGTP 216
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
440-552 1.79e-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: 43.94  E-value: 1.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 440 LNYYKNIdlseqdqAIANQIL----KEIISRLT-FLNNVGLEYLTLNRASGtLSGGEAQRIRLATQIGSRLTgvLYVLDE 514
Cdd:cd03292   93 RNVYENV-------AFALEVTgvppREIRKRVPaALELVGLSHKHRALPAE-LSGGEQQRVAIARAIVNSPT--ILIADE 162
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446585350 515 PSIGLHQRDNDRLINTLKEMRDLGNTLIVVEHDD---DTMR 552
Cdd:cd03292  163 PTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKelvDTTR 203
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
816-888 1.81e-04

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: 43.96  E-value: 1.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 816 LGYVTLGQQAT----TLSGGEAQRVKLAselhkR--STGKSIYILDEPT------TGLHVDDisrLLKVLNRlvENGDTV 883
Cdd:COG4181  131 LERVGLGHRLDhypaQLSGGEQQRVALA-----RafATEPAILFADEPTgnldaaTGEQIID---LLFELNR--ERGTTL 200

                 ....*
gi 446585350 884 VIIEH 888
Cdd:COG4181  201 VLVTH 205
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
802-902 1.81e-04

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 43.93  E-value: 1.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 802 PKIKRKLQTLVDVGLGYVTLGQQATTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHVDDISRLLKVLNRLV-ENG 880
Cdd:PRK10247 112 PDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMP---KVLLLDEITSALDESNKHNVNEIIHRYVrEQN 188
                         90       100
                 ....*....|....*....|..
gi 446585350 881 DTVVIIEHNLDVIKTADYIIDL 902
Cdd:PRK10247 189 IAVLWVTHDKDEINHADKVITL 210
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
487-560 1.84e-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: 1.84e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446585350 487 LSGGEAQRIRLATQIGSrlTGVLYVLDEPSIGLhqrDNDRLINTLKEMRDL----GNTLIVVEHDddtMRAADYLVDI 560
Cdd:cd03222   72 LSGGELQRVAIAAALLR--NATFYLFDEPSAYL---DIEQRLNAARAIRRLseegKKTALVVEHD---LAVLDYLSDR 141
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
432-563 1.86e-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: 43.64  E-value: 1.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 432 VEYSISQALNyyKNIDLSEQDQaianQILKEIISRltflnnVGLEYLtLNRASGTLSGGEAQRIRLATQIgSRLTGVLyV 511
Cdd:cd03298   87 VEQNVGLGLS--PGLKLTAEDR----QAIEVALAR------VGLAGL-EKRLPGELSGGERQRVALARVL-VRDKPVL-L 151
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446585350 512 LDEPSIGLHQ-RDNDRLINTLKEMRDLGNTLIVVEHD-DDTMRAADYLVDIGPG 563
Cdd:cd03298  152 LDEPFAALDPaLRAEMLDLVLDLHAETKMTVLMVTHQpEDAKRLAQRVVFLDNG 205
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
789-922 2.02e-04

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: 43.83  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 789 MTVEEatqffeNI---PKI---------KRKLQTLVDVGLGYVTLGQQ-ATTLSGGEAQRVKLASELhkrSTGKSIYILD 855
Cdd:cd03295   90 MTVEE------NIalvPKLlkwpkekirERADELLALVGLDPAEFADRyPHELSGGQQQRVGVARAL---AADPPLLLMD 160
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446585350 856 EPTTGLhvDDISRL-----LKVLNRLVenGDTVVIIEHNLD-VIKTADYIIDLgpeggsGGGTIVATGTPEDI 922
Cdd:cd03295  161 EPFGAL--DPITRDqlqeeFKRLQQEL--GKTIVFVTHDIDeAFRLADRIAIM------KNGEIVQVGTPDEI 223
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
448-559 2.15e-04

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: 43.65  E-value: 2.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 448 LSEQDQAIANQILKEIISRLtfLNNVGLEYLTLNRASGTLSGGEAQRIRLAtqigsR---LTGVLYVLDEPSIGLHQRDN 524
Cdd:cd03257  109 LRIHGKLSKKEARKEAVLLL--LVGVGLPEEVLNRYPHELSGGQRQRVAIA-----RalaLNPKLLIADEPTSALDVSVQ 181
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446585350 525 DRLINTLKEMRD-LGNTLIVVEHDddtMRAADYLVD 559
Cdd:cd03257  182 AQILDLLKKLQEeLGLTLLFITHD---LGVVAKIAD 214
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
486-581 2.35e-04

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 44.21  E-value: 2.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 486 TLSGGEAQRIRLATQIGSRLTGVLyvLDEPSIGL---HQRDndrLINTLKEM-RDLGNTLIVVEHD-DDTMRAADYLVDI 560
Cdd:PRK10253 143 TLSGGQRQRAWIAMVLAQETAIML--LDEPTTWLdisHQID---LLELLSELnREKGYTLAAVLHDlNQACRYASHLIAL 217
                         90       100
                 ....*....|....*....|.
gi 446585350 561 gpgageHGGQIVSSGTPQKVM 581
Cdd:PRK10253 218 ------REGKIVAQGAPKEIV 232
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
470-571 2.36e-04

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: 43.63  E-value: 2.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 470 LNNVGLEYLtLNRASGTLSGGEAQRIRLAtqigsR--LTGVLYVL-DEPSIGLHQRDNDRLINTLKEM-RDLGNTLIVVE 545
Cdd:cd03255  125 LERVGLGDR-LNHYPSELSGGQQQRVAIA-----RalANDPKIILaDEPTGNLDSETGKEVMELLRELnKEAGTTIVVVT 198
                         90       100
                 ....*....|....*....|....*.
gi 446585350 546 HDDDTMRAADYLVDIgpgageHGGQI 571
Cdd:cd03255  199 HDPELAEYADRIIEL------RDGKI 218
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
16-42 2.37e-04

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: 43.23  E-value: 2.37e-04
                         10        20
                 ....*....|....*....|....*..
gi 446585350  16 LKDIDIELPKNKLIVMTGLSGSGKSSL 42
Cdd:cd03250   21 LKDINLEVPKGELVAIVGPVGSGKSSL 47
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
470-580 2.46e-04

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: 43.87  E-value: 2.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 470 LNNVGLEYLTlNRASGTLSGGEAQRIRLATQIGSRlTGVLyVLDEPSIGLHQRDNDRLINTLKEMRD-LGNTLIVVEHD- 547
Cdd:cd03296  121 LKLVQLDWLA-DRYPAQLSGGQRQRVALARALAVE-PKVL-LLDEPFGALDAKVRKELRRWLRRLHDeLHVTTVFVTHDq 197
                         90       100       110
                 ....*....|....*....|....*....|...
gi 446585350 548 DDTMRAADYLVDIgpgageHGGQIVSSGTPQKV 580
Cdd:cd03296  198 EEALEVADRVVVM------NKGRIEQVGTPDEV 224
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
768-897 2.52e-04

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 43.71  E-value: 2.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 768 RYNRETLEVTYKGKNIadILEMTVEEATQ---FFENIPKIKRKLQTLVDV-GLGYVTLGQQATTLSGGEAQRVKLASELH 843
Cdd:PRK11614  76 KIMREAVAIVPEGRRV--FSRMTVEENLAmggFFAERDQFQERIKWVYELfPRLHERRIQRAGTMSGGEQQMLAIGRALM 153
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446585350 844 KRStgkSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHNLD-VIKTAD 897
Cdd:PRK11614 154 SQP---RLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANqALKLAD 205
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
816-902 2.59e-04

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: 43.61  E-value: 2.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 816 LGYVT-LGQQATTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHVDDISRLLKVLNRLVENgDTVVIIEHNLDVIK 894
Cdd:cd03248  138 SGYDTeVGEKGSQLSGGQKQRVAIARALIRNP---QVLILDEATSALDAESEQQVQQALYDWPER-RTVLVIAHRLSTVE 213

                 ....*...
gi 446585350 895 TADYIIDL 902
Cdd:cd03248  214 RADQILVL 221
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
827-900 2.70e-04

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: 43.29  E-value: 2.70e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446585350 827 TLSGGEAQRVKLASELHKRstgKSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHNLDVI-KTADYII 900
Cdd:cd03262  135 QLSGGQQQRVAIARALAMN---PKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFArEVADRVI 206
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
808-890 3.38e-04

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 44.43  E-value: 3.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 808 LQTLVDVGLGYVT---------LGQQATTLSGGEAQRVKLASE-LHKrstgKSIYILDEPTTGLHVDDISRLLKVLNRLV 877
Cdd:PRK11160 447 IEVLQQVGLEKLLeddkglnawLGEGGRQLSGGEQRRLGIARAlLHD----APLLLLDEPTEGLDAETERQILELLAEHA 522
                         90
                 ....*....|...
gi 446585350 878 ENgDTVVIIEHNL 890
Cdd:PRK11160 523 QN-KTVLMITHRL 534
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
820-886 3.40e-04

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 44.24  E-value: 3.40e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446585350 820 TLGQQATTLSGGEAQRVKLASELHkrsTGKSIYILDEPTTGlhVD-----DISRLlkvLNRLVENGDTVVII 886
Cdd:COG1129  387 SPEQPVGNLSGGNQQKVVLAKWLA---TDPKVLILDEPTRG--IDvgakaEIYRL---IRELAAEGKAVIVI 450
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
412-572 3.57e-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: 43.26  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  412 KRLSREALSVY---VGGLNIGEVVEYSISQALNYYKNIDLSEQdQAIANQILKEiisrltflnnVGLEYLTLNRASGTLS 488
Cdd:TIGR02769  84 RAFRRDVQLVFqdsPSAVNPRMTVRQIIGEPLRHLTSLDESEQ-KARIAELLDM----------VGLRSEDADKLPRQLS 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  489 GGEAQRIRLATQIGsrLTGVLYVLDEPSIGLHQRDNDRLINTLKEMR-DLGNTLIVVEHDddtMRAADYLVDigPGAGEH 567
Cdd:TIGR02769 153 GGQLQRINIARALA--VKPKLIVLDEAVSNLDMVLQAVILELLRKLQqAFGTAYLFITHD---LRLVQSFCQ--RVAVMD 225

                  ....*
gi 446585350  568 GGQIV 572
Cdd:TIGR02769 226 KGQIV 230
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
821-900 3.58e-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: 42.96  E-value: 3.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 821 LGQQATTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLhvDDIS--RLLKVLNRLVEnGDTVVIIEHNLDVIKTADY 898
Cdd:cd03245  134 IGERGRGLSGGQRQAVALARALLNDP---PILLLDEPTSAM--DMNSeeRLKERLRQLLG-DKTLIIITHRPSLLDLVDR 207

                 ..
gi 446585350 899 II 900
Cdd:cd03245  208 II 209
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
789-891 3.87e-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: 3.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 789 MTVEEATQFFENIPKIKR-----KLQTLVDVGLGYVTLGQQATTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHV 863
Cdd:cd03266   93 LTARENLEYFAGLYGLKGdeltaRLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP---PVLLLDEPTTGLDV 169
                         90       100
                 ....*....|....*....|....*...
gi 446585350 864 DDISRLLKVLNRLVENGDTVVIIEHNLD 891
Cdd:cd03266  170 MATRALREFIRQLRALGKCILFSTHIMQ 197
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
473-608 4.47e-04

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 43.55  E-value: 4.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 473 VGLEYLtLNRASGTLSGGEAQRIRLAtqigsR-LT---GVLyVLDEPSIGLhqrDN---DRLINTLKEM-RDLGNTLIVV 544
Cdd:COG3842  123 VGLEGL-ADRYPHQLSGGQQQRVALA-----RaLApepRVL-LLDEPLSAL---DAklrEEMREELRRLqRELGITFIYV 192
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446585350 545 EHD-DDTMRAADYLVDIgpgageHGGQIVSSGTPQKVmkdkksltgqylsgkkridvpeYRRPAS 608
Cdd:COG3842  193 THDqEEALALADRIAVM------NDGRIEQVGTPEEI----------------------YERPAT 229
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
828-894 4.48e-04

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 43.76  E-value: 4.48e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446585350 828 LSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHNLDVIK 894
Cdd:PRK13549 144 LGLGQQQLVEIAKALNKQA---RLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVK 207
cbiO PRK13645
energy-coupling factor transporter ATPase;
828-900 4.52e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 43.46  E-value: 4.52e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446585350 828 LSGGEAQRVKLASELhkRSTGKSIyILDEPTTGLHV---DDISRLLKVLNRlvENGDTVVIIEHNLD-VIKTADYII 900
Cdd:PRK13645 151 LSGGQKRRVALAGII--AMDGNTL-VLDEPTGGLDPkgeEDFINLFERLNK--EYKKRIIMVTHNMDqVLRIADEVI 222
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
470-559 4.68e-04

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: 42.78  E-value: 4.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 470 LNNVGLEYLtLNRASGTLSGGEAQRIRLATQIGSrlTGVLYVLDEPSIGL--HQRDN-DRLINTLKEMRDlgNTLIVVEH 546
Cdd:cd03237  100 AKPLQIEQI-LDREVPELSGGELQRVAIAACLSK--DADIYLLDEPSAYLdvEQRLMaSKVIRRFAENNE--KTAFVVEH 174
                         90
                 ....*....|...
gi 446585350 547 DddtMRAADYLVD 559
Cdd:cd03237  175 D---IIMIDYLAD 184
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
484-555 4.70e-04

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 42.94  E-value: 4.70e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446585350 484 SGTLSGGEAQRIRLATQIGSRLTgvLYVLDEPSIGLHQRDNDRLINTLKEMRDLGNTLIVVEHD-DDTMRAAD 555
Cdd:PRK11614 135 AGTMSGGEQQMLAIGRALMSQPR--LLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNaNQALKLAD 205
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
828-900 4.83e-04

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 42.69  E-value: 4.83e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446585350 828 LSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHNLDVI-KTADYII 900
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEP---QVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVArKTASRVV 212
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
827-924 4.90e-04

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 42.85  E-value: 4.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 827 TLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHVDDISRLLKVLNRLV-ENGDTVVIIEHNLDV-IKTADYIIDLGP 904
Cdd:PRK10575 147 SLSGGERQRAWIAMLVAQDS---RCLLLDEPTSALDIAHQVDVLALVHRLSqERGLTVIAVLHDINMaARYCDYLVALRG 223
                         90       100
                 ....*....|....*....|
gi 446585350 905 EGgsgggtIVATGTPEDIAQ 924
Cdd:PRK10575 224 GE------MIAQGTPAELMR 237
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
827-891 5.08e-04

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: 42.27  E-value: 5.08e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446585350 827 TLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHNLD 891
Cdd:cd03269  128 ELSKGNQQKVQFIAAVIHDP---ELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQME 189
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
817-900 5.14e-04

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 43.94  E-value: 5.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  817 GYVT-LGQQATTLSGGEAQRVKLASELHKRSTgksIYILDEPTTGLHVdDISRLLKVLNRLveNGDTVVIIEHNLDVIKT 895
Cdd:TIGR00958 606 GYDTeVGEKGSQLSGGQKQRIAIARALVRKPR---VLILDEATSALDA-ECEQLLQESRSR--ASRTVLLIAHRLSTVER 679

                  ....*
gi 446585350  896 ADYII 900
Cdd:TIGR00958 680 ADQIL 684
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
480-595 5.15e-04

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 42.98  E-value: 5.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 480 LNRASGTLSGGEAQRIRLATQIGSRLTGVLyvLDEPSIGLHQRDNDRLINTLKEMRDLGNTLIVVEHDDDTMRAADYLvd 559
Cdd:PRK14247 140 LDAPAGKLSGGQQQRLCIARALAFQPEVLL--ADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYV-- 215
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446585350 560 igpgAGEHGGQIVSSGTPQKVMKD-KKSLTGQYLSGK 595
Cdd:PRK14247 216 ----AFLYKGQIVEWGPTREVFTNpRHELTEKYVTGR 248
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
473-581 5.23e-04

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: 42.67  E-value: 5.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 473 VGLEYLTL-NRASGTLSGGEAQRIRLATQIGSRLTGVLyvLDEPSIGLHQRDNDRLINTLKEM-RDLGNTLIVVEHD-DD 549
Cdd:cd03295  121 VGLDPAEFaDRYPHELSGGQQQRVGVARALAADPPLLL--MDEPFGALDPITRDQLQEEFKRLqQELGKTIVFVTHDiDE 198
                         90       100       110
                 ....*....|....*....|....*....|..
gi 446585350 550 TMRAADYLVDIgpgageHGGQIVSSGTPQKVM 581
Cdd:cd03295  199 AFRLADRIAIM------KNGEIVQVGTPDEIL 224
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
487-922 6.03e-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: 43.64  E-value: 6.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  487 LSGGEAQRIRLATQIGSRltGVLYVLDEPSIGLHQRDNDRLINTLKE-MRDLGNTLIVVEHDDDTM-RAADYLVDIgpga 564
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKE--PFLFLADEPTGTLDPQTAKLVHNALEEaVKASGISMVLTSHWPEVIeDLSDKAIWL---- 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  565 geHGGQIVSSGTPQKV----MKDKKSLTG--QYLSGKKRIDVpeyrRPASDRKISIRGARSNNLKGIDVDIPLSIMTVVT 638
Cdd:TIGR03269 243 --ENGEIKEEGTPDEVvavfMEGVSEVEKecEVEVGEPIIKV----RNVSKRYISVDRGVVKAVDNVSLEVKEGEIFGIV 316
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  639 GVSGSGKSSLvnevlykslaqkinkskvkpglydkiegidqlDKIIdidqspIGRTPRSNPATYTGVFDDIRDVfaqtne 718
Cdd:TIGR03269 317 GTSGAGKTTL--------------------------------SKII------AGVLEPTSGEVNVRVGDEWVDM------ 352
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  719 AKIRGYQKGRfsfnvkggrceACKGDGIIKIEMHFLPdvyvpcevcdgkryNRETLEvtykgkNIADI--LEMTVEEAtq 796
Cdd:TIGR03269 353 TKPGPDGRGR-----------AKRYIGILHQEYDLYP--------------HRTVLD------NLTEAigLELPDELA-- 399
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  797 ffenipkIKRKLQTLVDVGL----GYVTLGQQATTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLhvDDISRLL-- 870
Cdd:TIGR03269 400 -------RMKAVITLKMVGFdeekAEEILDKYPDELSEGERHRVALAQVLIKEP---RIVILDEPTGTM--DPITKVDvt 467
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446585350  871 -KVLNRLVENGDTVVIIEHNLDVIKTadyIIDlgPEGGSGGGTIVATGTPEDI 922
Cdd:TIGR03269 468 hSILKAREEMEQTFIIVSHDMDFVLD---VCD--RAALMRDGKIVKIGDPEEI 515
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
803-922 6.34e-04

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 42.67  E-value: 6.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 803 KIKRKLQTLVDVGLGYVTlGQQATTLSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLH---VDDISRLLKVLNRlvEN 879
Cdd:PRK11300 130 ALDRAATWLERVGLLEHA-NRQAGNLAYGQQRRLEIARCM---VTQPEILMLDEPAAGLNpkeTKELDELIAELRN--EH 203
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 446585350 880 GDTVVIIEHNLD-VIKTADYIIdlgpegGSGGGTIVATGTPEDI 922
Cdd:PRK11300 204 NVTVLLIEHDMKlVMGISDRIY------VVNQGTPLANGTPEEI 241
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
789-922 6.68e-04

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: 42.63  E-value: 6.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 789 MTVEEATQF---FENIPKIKRK---LQTLVDVGL-GYVTlgQQATTLSGGEAQRVKLASELhkrSTGKSIYILDEPTTGL 861
Cdd:cd03294  117 RTVLENVAFgleVQGVPRAEREeraAEALELVGLeGWEH--KYPDELSGGMQQRVGLARAL---AVDPDILLMDEAFSAL 191
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446585350 862 hvDDISR--LLKVLNRLV-ENGDTVVIIEHNLD-VIKTADYIIDLGPEGgsgggtIVATGTPEDI 922
Cdd:cd03294  192 --DPLIRreMQDELLRLQaELQKTIVFITHDLDeALRLGDRIAIMKDGR------LVQVGTPEEI 248
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
486-564 6.84e-04

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: 42.04  E-value: 6.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 486 TLSGGEAQRIRLAtqigsRltGV-----LYVLDEPSIGLHQRDNDRLINTLKEMRDLGNTLIVVEHDDDTMRA-ADYLVD 559
Cdd:COG4778  152 TFSGGEQQRVNIA-----R--GFiadppLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAvADRVVD 224

                 ....*
gi 446585350 560 IGPGA 564
Cdd:COG4778  225 VTPFS 229
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
828-935 7.13e-04

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 42.31  E-value: 7.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 828 LSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHNLDVI-KTADYIIDLgpeg 906
Cdd:COG4161  142 LSGGQQQRVAIARALMMEP---QVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFArKVASQVVYM---- 214
                         90       100
                 ....*....|....*....|....*....
gi 446585350 907 gsGGGTIVATGTPEDIAQTKSSYTGKYLK 935
Cdd:COG4161  215 --EKGRIIEQGDASHFTQPQTEAFAHYLS 241
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
473-564 7.33e-04

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: 41.70  E-value: 7.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 473 VGLEYLtLNRASGTLSGGEAQRIRLATQIgsrLTGV-LYVLDEPSIGLHQRDNDRLINTLKEMRDLGNTLIVVEHDDDTM 551
Cdd:COG4133  119 VGLAGL-ADLPVRQLSAGQKRRVALARLL---LSPApLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLEL 194
                         90
                 ....*....|...
gi 446585350 552 RAADYLvDIGPGA 564
Cdd:COG4133  195 AAARVL-DLGDFK 206
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
469-594 7.67e-04

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 42.26  E-value: 7.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 469 FLNNVGLEYLTLNRASGTLSGGEAQRIRLATQIGSRLTGVLYvlDEPSIGLHQRDNDRLINTLKEMRDLGNTLIVVEHDD 548
Cdd:PRK10619 135 YLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLF--DEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEM 212
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446585350 549 DTMR-AADYLVDIgpgageHGGQIVSSGTPQKVMKDKKS-LTGQYLSG 594
Cdd:PRK10619 213 GFARhVSSHVIFL------HQGKIEEEGAPEQLFGNPQSpRLQQFLKG 254
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
428-588 9.42e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 42.05  E-value: 9.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 428 IGEVVEYSISQALnyyknidlseQDQAIANQILKEIISRLtfLNNVGLeyltLNRASG---TLSGGEAQRIRLATQIGsr 504
Cdd:PRK13648  97 VGSIVKYDVAFGL----------ENHAVPYDEMHRRVSEA--LKQVDM----LERADYepnALSGGQKQRVAIAGVLA-- 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 505 LTGVLYVLDEPSIGLHQRDNDRLINTLKEMRDLGN-TLIVVEHDDDTMRAADYLVDIgpgageHGGQIVSSGTPQKVMKD 583
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAMEADHVIVM------NKGTVYKEGTPTEIFDH 232

                 ....*
gi 446585350 584 KKSLT 588
Cdd:PRK13648 233 AEELT 237
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
805-889 9.74e-04

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 41.69  E-value: 9.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 805 KRKLQTLVDVGLGYvTLGQQATTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHV---DDISRLLKVLNRlvENGD 881
Cdd:PRK10584 125 NGAKALLEQLGLGK-RLDHLPAQLSGGEQQRVALARAFNGRP---DVLFADEPTGNLDRqtgDKIADLLFSLNR--EHGT 198

                 ....*...
gi 446585350 882 TVVIIEHN 889
Cdd:PRK10584 199 TLILVTHD 206
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
823-897 9.75e-04

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 42.73  E-value: 9.75e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446585350 823 QQATTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHV---DDISRLLKvlnRLVENGDTVVIIEHNLD-VIKTAD 897
Cdd:PRK15439 399 QAARTLSGGNQQKVLIAKCLEASP---QLLIVDEPTRGVDVsarNDIYQLIR---SIAAQNVAVLFISSDLEeIEQMAD 471
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
468-575 1.04e-03

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: 41.14  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 468 TFLNNVGLEyltlnrasgtLSGGEAQRIRLAtQIGSRLTGVLyVLDEPSIGLHQRDNDRLINTLKEMRDlGNTLIVVEHD 547
Cdd:cd03247   90 TLRNNLGRR----------FSGGERQRLALA-RILLQDAPIV-LLDEPTVGLDPITERQLLSLIFEVLK-DKTLIWITHH 156
                         90       100
                 ....*....|....*....|....*...
gi 446585350 548 DDTMRAADYLVDIgpgageHGGQIVSSG 575
Cdd:cd03247  157 LTGIEHMDKILFL------ENGKIIMQG 178
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
828-900 1.13e-03

ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444078 [Multi-domain]  Cd Length: 605  Bit Score: 42.88  E-value: 1.13e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446585350 828 LSGGEAQRVKLASELHKRStgkSIYILDEPTTGLhvDdiSR----LLKVLNRLVEnGDTVVIIEHNLDVIKTADYII 900
Cdd:COG5265  495 LSGGEKQRVAIARTLLKNP---PILIFDEATSAL--D--SRteraIQAALREVAR-GRTTLVIAHRLSTIVDADEIL 563
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
820-922 1.13e-03

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 42.46  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 820 TLGQQATTLSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHNL-DVIKTADY 898
Cdd:PRK09700 402 SVNQNITELSGGNQQKVLISKWL---CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELpEIITVCDR 478
                         90       100
                 ....*....|....*....|....
gi 446585350 899 IIDLGPEGGSGGGTIVATGTPEDI 922
Cdd:PRK09700 479 IAVFCEGRLTQILTNRDDMSEEEI 502
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
823-900 1.20e-03

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 42.59  E-value: 1.20e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446585350 823 QQATTLSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHNL-DVIKTADYII 900
Cdd:PRK11288 392 QLIMNLSGGNQQKAILGRWL---SEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLpEVLGVADRIV 467
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
468-583 1.25e-03

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 41.51  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 468 TFLNNVGLEYLTlNRASGTLSGGEAQRIRLATQIGSRLTgvLYVLDEPSIGLHQRDNDRLINTLKEMRD-LGNTLIVVEH 546
Cdd:PRK11300 136 TWLERVGLLEHA-NRQAGNLAYGQQRRLEIARCMVTQPE--ILMLDEPAAGLNPKETKELDELIAELRNeHNVTVLLIEH 212
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446585350 547 DDD-TMRAADYLVDIgpgagEHGGQIVsSGTPQKVMKD 583
Cdd:PRK11300 213 DMKlVMGISDRIYVV-----NQGTPLA-NGTPEEIRNN 244
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
828-894 1.29e-03

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 41.99  E-value: 1.29e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 828 LSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLH---VDDISRLLKVLNRlvENGDTVVIIEHNLDVIK 894
Cdd:COG1135  141 LSGGQKQRVGIARAL---ANNPKVLLCDEATSALDpetTRSILDLLKDINR--ELGLTIVLITHEMDVVR 205
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
809-891 1.43e-03

nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]


Pssm-ID: 130252 [Multi-domain]  Cd Length: 230  Bit Score: 41.30  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  809 QTLVDVGLGYVTLGQQA----TTLSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLhvDDISR------LLKVLNrlvE 878
Cdd:TIGR01184  92 RAIVEEHIALVGLTEAAdkrpGQLSGGMKQRVAIARAL---SIRPKVLLLDEPFGAL--DALTRgnlqeeLMQIWE---E 163
                          90
                  ....*....|...
gi 446585350  879 NGDTVVIIEHNLD 891
Cdd:TIGR01184 164 HRVTVLMVTHDVD 176
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
826-900 1.52e-03

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: 42.12  E-value: 1.52e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446585350  826 TTLSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHNL-DVIKTADYII 900
Cdd:TIGR02633 402 GRLSGGNQQKAVLAKML---LTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELaEVLGLSDRVL 474
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
782-894 1.53e-03

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 41.71  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 782 NIADILEMtveeatqffENIPK--IKRKLQTLVDVglgyVTLGQQATT----LSGGEAQRVKLASELhkrSTGKSIYILD 855
Cdd:PRK11153 102 NVALPLEL---------AGTPKaeIKARVTELLEL----VGLSDKADRypaqLSGGQKQRVAIARAL---ASNPKVLLCD 165
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446585350 856 EPTTGLH---VDDISRLLKVLNRlvENGDTVVIIEHNLDVIK 894
Cdd:PRK11153 166 EATSALDpatTRSILELLKDINR--ELGLTIVLITHEMDVVK 205
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
828-899 1.60e-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: 41.98  E-value: 1.60e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446585350 828 LSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLHV---DDISRLLKVLNRlvENGDTVVIIEHNLDVI-KTADYI 899
Cdd:COG4172  157 LSGGQRQRVMIAMAL---ANEPDLLIADEPTTALDVtvqAQILDLLKDLQR--ELGMALLLITHDLGVVrRFADRV 227
cbiO PRK13641
energy-coupling factor transporter ATPase;
808-902 1.78e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 41.35  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 808 LQTLVDVGLGYVTLGQQATTLSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIE 887
Cdd:PRK13641 126 LKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVM---AYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVT 202
                         90
                 ....*....|....*
gi 446585350 888 HNLDVIktADYIIDL 902
Cdd:PRK13641 203 HNMDDV--AEYADDV 215
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
809-902 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 446585350 809 QTLVDVGLGYVTLGQQATTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHVDDISRLLKVLNRlvENGdTVVIIEH 888
Cdd:COG0488  134 EILSGLGFPEEDLDRPVSELSGGWRRRVALARALLSEP---DLLLLDEPTNHLDLESIEWLEEFLKN--YPG-TVLVVSH 207
                         90
                 ....*....|....*..
gi 446585350 889 N---LDviKTADYIIDL 902
Cdd:COG0488  208 DryfLD--RVATRILEL 222
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
821-935 1.94e-03

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 42.32  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  821 LGQQATTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHVDDISRLLKVLNRLVENGD-TVVIIEHNLDVIKTADYI 899
Cdd:PTZ00265 1352 VGPYGKSLSGGQKQRIAIARALLREP---KILLLDEATSSLDSNSEKLIEKTIVDIKDKADkTIITIAHRIASIKRSDKI 1428
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 446585350  900 IdLGPEGGSGGGTIVATGTPEDIAQTKSSYTGKYLK 935
Cdd:PTZ00265 1429 V-VFNNPDRTGSFVQAHGTHEELLSVQDGVYKKYVK 1463
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
788-888 1.95e-03

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: 40.42  E-value: 1.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  788 EMTVEEATQFFENIPKIKRK--LQTLVDVGL-GYVTLgqQATTLSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLHVD 864
Cdd:TIGR01189  87 ELSALENLHFWAAIHGGAQRtiEDALAAVGLtGFEDL--PAAQLSAGQQRRLALARLW---LSRRPLWILDEPTTALDKA 161
                          90       100
                  ....*....|....*....|....
gi 446585350  865 DISRLLKVLNRLVENGDTVVIIEH 888
Cdd:TIGR01189 162 GVALLAGLLRAHLARGGIVLLTTH 185
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
449-593 2.00e-03

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: 40.84  E-value: 2.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 449 SEQDQAIANQILKEiisrltflnnVGLEYLtLNRASGTLSGGEAQRIRLAtqigsR--------LtgvlyVLDEPSIGL- 519
Cdd:COG1119  116 TDEQRERARELLEL----------LGLAHL-ADRPFGTLSQGEQRRVLIA-----RalvkdpelL-----ILDEPTAGLd 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 520 -HQRdnDRLINTLKEMRDLGN-TLIVVEHdddtmraadYLVDIGPGAGEH----GGQIVSSGTPQKVmkdkksLTGQYLS 593
Cdd:COG1119  175 lGAR--ELLLALLDKLAAEGApTLVLVTH---------HVEEIPPGITHVlllkDGRVVAAGPKEEV------LTSENLS 237
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
828-893 2.10e-03

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 41.76  E-value: 2.10e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446585350 828 LSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHVD---DISRLLKVLNRLVENGdtVVIIEHNLDVI 893
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRP---AVLIADEPTTALDVTiqaQILQLIKVLQKEMSMG--VIFITHDMGVV 232
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
828-922 2.10e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 41.23  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 828 LSGGEAQRVKLASELHKRStgKSIyILDEPTTGLhvDDISRL-----LKVLNRlvENGDTVVIIEHNLDVIKTADYIIDL 902
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRP--ECI-IFDEPTAML--DPSGRRevvntIKELNK--KYGITIILITHYMEEAVEADRIIVM 217
                         90       100
                 ....*....|....*....|
gi 446585350 903 GPEGgsgggtIVATGTPEDI 922
Cdd:PRK13633 218 DSGK------VVMEGTPKEI 231
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
828-900 2.17e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 40.87  E-value: 2.17e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446585350 828 LSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHNLD-VIKTADYII 900
Cdd:PRK13647 139 LSYGQKKRVAIAGVLAMDP---DVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDlAAEWADQVI 209
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
470-601 2.19e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 40.94  E-value: 2.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 470 LNNVGLEYLtLNRASGTLSGGEAQRIRLATQIGsrLTGVLYVLDEPSIGLHQRDNDRLINTLKEM-RDLGNTLIVVEHDD 548
Cdd:PRK13652 122 LHMLGLEEL-RDRVPHHLSGGEKKRVAIAGVIA--MEPQVLVLDEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQL 198
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446585350 549 DTM-RAADYLVDIgpgageHGGQIVSSGTPQKVMKDKKSLTgqylsgKKRIDVP 601
Cdd:PRK13652 199 DLVpEMADYIYVM------DKGRIVAYGTVEEIFLQPDLLA------RVHLDLP 240
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
440-580 2.20e-03

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: 40.68  E-value: 2.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 440 LNYYKNIDLSEQDQAIANQILKEIISRLtfLNNVGLEYLtLNRASGTLSGGEAQRIRLATQIGSRlTGVLyVLDEPSIGL 519
Cdd:cd03300   87 LTVFENIAFGLRLKKLPKAEIKERVAEA--LDLVQLEGY-ANRKPSQLSGGQQQRVAIARALVNE-PKVL-LLDEPLGAL 161
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446585350 520 HQRDNDRLINTLKEM-RDLGNTLIVVEHD-DDTMRAADYLVDIgpgageHGGQIVSSGTPQKV 580
Cdd:cd03300  162 DLKLRKDMQLELKRLqKELGITFVFVTHDqEEALTMSDRIAVM------NKGKIQQIGTPEEI 218
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
829-893 2.28e-03

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 41.25  E-value: 2.28e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446585350 829 SGGEAQRVKLASELHKRStgkSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVI-IEHNLDVI 893
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRP---KLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVV 225
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
809-917 2.32e-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: 40.55  E-value: 2.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 809 QTLVDVGLGYVTLG----QQATTLSGGEAQRVKLASELHKRstgKSIYILDEPTTGLhvDDISR--LLKVLNRL-VENGD 881
Cdd:cd03298  106 RQAIEVALARVGLAglekRLPGELSGGERQRVALARVLVRD---KPVLLLDEPFAAL--DPALRaeMLDLVLDLhAETKM 180
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446585350 882 TVVIIEHNL-DVIKTADYIIDLgpeggsGGGTIVATG 917
Cdd:cd03298  181 TVLMVTHQPeDAKRLAQRVVFL------DNGRIAAQG 211
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
788-889 2.49e-03

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 40.24  E-value: 2.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 788 EMTVEEATQFFENI--PKIKRKLQTLVDVGLGYVTlGQQATTLSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLHVDD 865
Cdd:PRK13539  87 ALTVAENLEFWAAFlgGEELDIAAALEAVGLAPLA-HLPFGYLSAGQKRRVALARLL---VSNRPIWILDEPTAALDAAA 162
                         90       100
                 ....*....|....*....|....
gi 446585350 866 ISRLLKVLNRLVENGDTVVIIEHN 889
Cdd:PRK13539 163 VALFAELIRAHLAQGGIVIAATHI 186
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
476-558 2.59e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 2.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 476 EY-LTLNRASGT------LSGGE----------AQRIRLATQI-GSRLTGVLyVLDEPSIGLHQRDNDRLINTLKEMRDL 537
Cdd:PRK02224 764 EYeLTVYQKDGEplepeqLSGGEralfnlslrcAIYRLLAEGIeGDAPLPPL-ILDEPTVFLDSGHVSQLVDLVESMRRL 842
                         90       100
                 ....*....|....*....|..
gi 446585350 538 G-NTLIVVEHDDDTMRAADYLV 558
Cdd:PRK02224 843 GvEQIVVVSHDDELVGAADDLV 864
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
821-900 2.73e-03

ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.


Pssm-ID: 213234 [Multi-domain]  Cd Length: 236  Bit Score: 40.39  E-value: 2.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 821 LGQQATTLSGGEAQRVKL-ASELHKrstgKSIYILDEPTTGLHV---DDISRLLKVLNRlvENGDTVVIIEHNL-DVIKT 895
Cdd:cd03267  147 LDTPVRQLSLGQRMRAEIaAALLHE----PEILFLDEPTIGLDVvaqENIRNFLKEYNR--ERGTTVLLTSHYMkDIEAL 220

                 ....*
gi 446585350 896 ADYII 900
Cdd:cd03267  221 ARRVL 225
cbiO PRK13650
energy-coupling factor transporter ATPase;
460-580 3.14e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 40.49  E-value: 3.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 460 LKEIISRLT-FLNNVGLEYLTlNRASGTLSGGEAQRIRLATQIGSRLTgvLYVLDEPSIGLHQRDNDRLINTLKEMRD-L 537
Cdd:PRK13650 114 HEEMKERVNeALELVGMQDFK-EREPARLSGGQKQRVAIAGAVAMRPK--IIILDEATSMLDPEGRLELIKTIKGIRDdY 190
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446585350 538 GNTLIVVEHDDDTMRAADYLVDIgpgageHGGQIVSSGTPQKV 580
Cdd:PRK13650 191 QMTVISITHDLDEVALSDRVLVM------KNGQVESTSTPREL 227
hmuV PRK13547
heme ABC transporter ATP-binding protein;
486-607 3.60e-03

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 40.20  E-value: 3.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 486 TLSGGEAQRIRLA-----------TQIGSRltgvLYVLDEPSIGLHQRDNDRLINTLKEM-RD--LGNTLIVveHDDD-T 550
Cdd:PRK13547 145 TLSGGELARVQFArvlaqlwpphdAAQPPR----YLLLDEPTAALDLAHQHRLLDTVRRLaRDwnLGVLAIV--HDPNlA 218
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446585350 551 MRAADYLVDIGPGAgehggqIVSSGTPQKVMKdKKSLTGQYLSGKKRIDVPEYRRPA 607
Cdd:PRK13547 219 ARHADRIAMLADGA------IVAHGAPADVLT-PAHIARCYGFAVRLVDAGDGVPPV 268
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
462-547 3.73e-03

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 40.95  E-value: 3.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 462 EIISRLtflnnvGLEYLtLNRASGTLSGGEAQRIRLATQIgSRlTGVLYVLDEPSIGL--HQRDN-DRLINTLKEMRDlg 538
Cdd:PRK13409 436 EIIKPL------QLERL-LDKNVKDLSGGELQRVAIAACL-SR-DADLYLLDEPSAHLdvEQRLAvAKAIRRIAEERE-- 504

                 ....*....
gi 446585350 539 NTLIVVEHD 547
Cdd:PRK13409 505 ATALVVDHD 513
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
467-566 3.74e-03

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 40.08  E-value: 3.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 467 LTFLNNVGLEYLTLNRASGTLSGGEAQRIRLATQIgSRLTGVLyVLDEPSIGLHQrDNDRLINTL--KEMRDLGNTLIVV 544
Cdd:PRK10247 118 LDDLERFALPDTILTKNIAELSGGEKQRISLIRNL-QFMPKVL-LLDEITSALDE-SNKHNVNEIihRYVREQNIAVLWV 194
                         90       100
                 ....*....|....*....|..
gi 446585350 545 EHDDDTMRAADYLVDIGPGAGE 566
Cdd:PRK10247 195 THDKDEINHADKVITLQPHAGE 216
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
486-547 3.81e-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: 40.81  E-value: 3.81e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446585350  486 TLSGGEAQRIRLATQIgsrLTGV-LYVLDEPSIGLHQRDNDRLINTLKEMRDlGNTLIVVEHD 547
Cdd:TIGR02868 471 RLSGGERQRLALARAL---LADApILLLDEPTEHLDAETADELLEDLLAALS-GRTVVLITHH 529
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
828-894 3.85e-03

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: 40.96  E-value: 3.85e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446585350  828 LSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVIIEHNLDVIK 894
Cdd:TIGR02633 142 YGGGQQQLVEIAKALNKQA---RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVK 205
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
805-894 4.14e-03

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 39.80  E-value: 4.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 805 KRKLQTLVDVGLGYVTlGQQATTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGL---HVDDISRLLKVLNRlvENGD 881
Cdd:PRK11629 124 SRALEMLAAVGLEHRA-NHRPSELSGGERQRVAIARALVNNP---RLVLADEPTGNLdarNADSIFQLLGELNR--LQGT 197
                         90
                 ....*....|...
gi 446585350 882 TVVIIEHNLDVIK 894
Cdd:PRK11629 198 AFLVVTHDLQLAK 210
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
487-608 4.49e-03

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 40.52  E-value: 4.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 487 LSGGEAQRI---R-LATQigsrlTGVLyVLDEPSIGL--HQRDNDR--LINTLKEmrdLGNTLIVVEHD-DDTMRAADYL 557
Cdd:COG1118  134 LSGGQRQRValaRaLAVE-----PEVL-LLDEPFGALdaKVRKELRrwLRRLHDE---LGGTTVFVTHDqEEALELADRV 204
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446585350 558 VDIgpgageHGGQIVSSGTPQKVmkdkksltgqylsgkkridvpeYRRPAS 608
Cdd:COG1118  205 VVM------NQGRIEQVGTPDEV----------------------YDRPAT 227
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
16-43 5.12e-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: 38.90  E-value: 5.12e-03
                         10        20
                 ....*....|....*....|....*...
gi 446585350  16 LKDIDIELPKNKLIVMTGLSGSGKSSLA 43
Cdd:cd03228   18 LKDVSLTIKPGEKVAIVGPSGSGKSTLL 45
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
14-42 5.13e-03

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: 38.77  E-value: 5.13e-03
                         10        20
                 ....*....|....*....|....*....
gi 446585350  14 HNLKDIDIELPKNKLIVMTGLSGSGKSSL 42
Cdd:cd00267   13 TALDNVSLTLKAGEIVALVGPNGSGKSTL 41
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
803-899 5.52e-03

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 39.65  E-value: 5.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 803 KIKRKLQTLVD-----VGLG---YVTLGQQATTLSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLHVDDISRLLKVLN 874
Cdd:PRK14246 121 KEKREIKKIVEeclrkVGLWkevYDRLNSPASQLSGGQQQRLTIARAL---ALKPKVLLMDEPTSMIDIVNSQAIEKLIT 197
                         90       100
                 ....*....|....*....|....*.
gi 446585350 875 RLvENGDTVVIIEHN-LDVIKTADYI 899
Cdd:PRK14246 198 EL-KNEIAIVIVSHNpQQVARVADYV 222
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
785-891 5.53e-03

ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.


Pssm-ID: 213230 [Multi-domain]  Cd Length: 220  Bit Score: 39.41  E-value: 5.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 785 DIL--EMTVEEATQFF---ENIPKIKRKLQtlVDVGLGYVTLGQ----QATTLSGGeaQRVKLaselhkrST------GK 849
Cdd:cd03263   84 DALfdELTVREHLRFYarlKGLPKSEIKEE--VELLLRVLGLTDkankRARTLSGG--MKRKL-------SLaialigGP 152
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 446585350 850 SIYILDEPTTGLhvDDISR--LLKVLNRLVENgDTVVIIEHNLD 891
Cdd:cd03263  153 SVLLLDEPTSGL--DPASRraIWDLILEVRKG-RSIILTTHSMD 193
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
16-43 5.80e-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: 39.37  E-value: 5.80e-03
                         10        20
                 ....*....|....*....|....*...
gi 446585350  16 LKDIDIELPKNKLIVMTGLSGSGKSSLA 43
Cdd:cd03225   17 LDDISLTIKKGEFVLIVGPNGSGKSTLL 44
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
828-893 6.13e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 39.83  E-value: 6.13e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446585350 828 LSGGEAQRVKLASELhkrSTGKSIYILDEPTTGLHVDDISRLLKVLNRLVEN-GDTVVIIEHNLDVI 893
Cdd:PRK13636 142 LSFGQKKRVAIAGVL---VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIV 205
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
828-924 6.28e-03

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 39.33  E-value: 6.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 828 LSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHVDDISRLLKVLNRL-VENGDTVVIIEHNLD-VIKTADYIIDLGPE 905
Cdd:PRK09544 121 LSGGETQRVLLARALLNRP---QLLVLDEPTQGVDVNGQVALYDLIDQLrRELDCAVLMVSHDLHlVMAKTDEVLCLNHH 197
                         90
                 ....*....|....*....
gi 446585350 906 ggsgggtIVATGTPEDIAQ 924
Cdd:PRK09544 198 -------ICCSGTPEVVSL 209
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
804-922 6.38e-03

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: 40.17  E-value: 6.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350  804 IKRKLQTLVDVGLGYvTLGQQATTLSGGEAQRVKLASELHKRSTgksIYILDEPTTGLHVDDISRLLKVLNRLV-ENGDT 882
Cdd:TIGR03269 146 VGRAVDLIEMVQLSH-RITHIARDLSGGEKQRVVLARQLAKEPF---LFLADEPTGTLDPQTAKLVHNALEEAVkASGIS 221
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 446585350  883 VVIIEHNLDVI-KTADYIIDLGPEGgsgggtIVATGTPEDI 922
Cdd:TIGR03269 222 MVLTSHWPEVIeDLSDKAIWLENGE------IKEEGTPDEV 256
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
440-595 6.42e-03

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 39.65  E-value: 6.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 440 LNYYKNIDLSEQDQAIANQ-----ILKEIISRLTFLNNVgleYLTLNRASGTLSGGEAQRIRLATQIGsrLTGVLYVLDE 514
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKreikkIVEECLRKVGLWKEV---YDRLNSPASQLSGGQQQRLTIARALA--LKPKVLLMDE 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 515 PSIGL---HQRDNDRLINTLK-EMrdlgnTLIVVEHD-DDTMRAADYLvdigpgAGEHGGQIVSSGTPQKVMKD-KKSLT 588
Cdd:PRK14246 180 PTSMIdivNSQAIEKLITELKnEI-----AIVIVSHNpQQVARVADYV------AFLYNGELVEWGSSNEIFTSpKNELT 248

                 ....*..
gi 446585350 589 GQYLSGK 595
Cdd:PRK14246 249 EKYVIGR 255
GguA NF040905
sugar ABC transporter ATP-binding protein;
820-886 6.45e-03

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 40.16  E-value: 6.45e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446585350 820 TLGQQATTLSGGEAQRVKLASELHkrsTGKSIYILDEPTTGLHVDDISRLLKVLNRLVENGDTVVII 886
Cdd:NF040905 397 SVFQKVGNLSGGNQQKVVLSKWLF---TDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVI 460
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
790-902 6.45e-03

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 40.66  E-value: 6.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350   790 TVEEATQFFENIPKIKRKLQTLvdvglgyvtLGQQATTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHVDDISRL 869
Cdd:TIGR01271  520 SVIKACQLEEDIALFPEKDKTV---------LGEGGITLSGGQRARISLARAVYKDA---DLYLLDSPFTHLDVVTEKEI 587
                           90       100       110
                   ....*....|....*....|....*....|....
gi 446585350   870 L-KVLNRLVENgDTVVIIEHNLDVIKTADYIIDL 902
Cdd:TIGR01271  588 FeSCLCKLMSN-KTRILVTSKLEHLKKADKILLL 620
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
804-890 6.67e-03

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 39.35  E-value: 6.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 804 IKRKLQTLVDVGLGyvtlGQQAT---TLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHVDDISRLLKVLNRLVENG 880
Cdd:PRK11264 122 TARARELLAKVGLA----GKETSyprRLSGGQQQRVAIARALAMRP---EVILFDEPTSALDPELVGEVLNTIRQLAQEK 194
                         90
                 ....*....|
gi 446585350 881 DTVVIIEHNL 890
Cdd:PRK11264 195 RTMVIVTHEM 204
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
487-558 7.16e-03

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: 38.18  E-value: 7.16e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446585350 487 LSGGEAQRIRLATQI--GSRLTgvlyVLDEPSIGLHQRDNDRLINTLKEMRDLGNTLIVVEHD-DDTMRAADYLV 558
Cdd:cd03216   83 LSVGERQMVEIARALarNARLL----ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRlDEVFEIADRVT 153
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
470-592 7.32e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 39.45  E-value: 7.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 470 LNNVGLEYLTlNRASGTLSGGEAQRIRLAtqigsrltGVL------YVLDEPSIGLHQRDNDRLINTLKEM-RDLGNTLI 542
Cdd:PRK13636 126 LKRTGIEHLK-DKPTHCLSFGQKKRVAIA--------GVLvmepkvLVLDEPTAGLDPMGVSEIMKLLVEMqKELGLTII 196
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 446585350 543 VVEHDDDTMraADYlVDIGPGAGEhgGQIVSSGTPQKVMKDKKSLTGQYL 592
Cdd:PRK13636 197 IATHDIDIV--PLY-CDNVFVMKE--GRVILQGNPKEVFAEKEMLRKVNL 241
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
799-899 7.39e-03

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 40.03  E-value: 7.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 799 ENI-------PKIKRKLQTLVDVGLGYVTLGQQATTLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHVDDISRLLK 871
Cdd:PRK15439 105 ENIlfglpkrQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDS---RILILDEPTASLTPAETERLFS 181
                         90       100
                 ....*....|....*....|....*....
gi 446585350 872 VLNRLVENGDTVVIIEHNL-DVIKTADYI 899
Cdd:PRK15439 182 RIRELLAQGVGIVFISHKLpEIRQLADRI 210
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
789-889 8.90e-03

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 39.43  E-value: 8.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446585350 789 MTVEEATQFFENIPKI-KRKLQTLVDVGLGYVTLGQQAT----TLSGGEAQRVKLASELHKRStgkSIYILDEPTTGLHV 863
Cdd:PRK11607 106 MTVEQNIAFGLKQDKLpKAEIASRVNEMLGLVHMQEFAKrkphQLSGGQRQRVALARSLAKRP---KLLLLDEPMGALDK 182
                         90       100
                 ....*....|....*....|....*..
gi 446585350 864 DDISRL-LKVLNRLVENGDTVVIIEHN 889
Cdd:PRK11607 183 KLRDRMqLEVVDILERVGVTCVMVTHD 209
 
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