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Conserved domains on  [gi|488923006|ref|WP_002834081|]
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excinuclease ABC subunit UvrA [Pediococcus pentosaceus]

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

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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: 1930.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006   1 MANDKIVIHGARAHNLKNIDVTIPRDKLVVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLGQMDKPDVDSIDG 80
Cdd:PRK00349   1 MMMDKIIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  81 LSPAISIDQKTTSKNPRSTVGTVTEINDYLRLLWARVGQPICPNDGTPITSQTVEQMVNRVLDLPERSKVQIISPIVRAK 160
Cdd:PRK00349  81 LSPAISIDQKTTSHNPRSTVGTVTEIYDYLRLLYARVGKPHCPNCGRPIEAQTVSQMVDRVLELPEGTRLQILAPVVRGR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 161 KGQHKKVFEKIKREGFVRVRVDDETMDVEEVPELDKNKVHTIDIVVDRVVVKDGIRSRLFDSFEAALRLSKGYATADVIG 240
Cdd:PRK00349 161 KGEHKKLLENLRKQGFVRVRVDGEVYDLDEPPKLDKNKKHTIEVVVDRLVVKEDIRQRLADSIETALKLSDGLVVVEVMD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 241 G---EPILFSEHYSCPVCGFTVGELEPRLFSFNAPFGACPECDGLGIKLEVDEDLVIPDPSKTLREGAIAPWNPISSQYY 317
Cdd:PRK00349 241 DpeaEELLFSEKFACPVCGFSIPELEPRLFSFNSPYGACPTCDGLGVKLEFDPDLVVPDPELSLAEGAIAPWSRSSSSYY 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 318 PTLLEQAAKSFGIDMDTPFEDLPKADRQLVLYGSKGKKFHFHYENDFGGVRDVDSVFEGVMVNIDRRYHETNSDFTRDQM 397
Cdd:PRK00349 321 FQMLKSLAEHYGFDLDTPWKDLPEEVQDIILYGSGDEEIEFRYKNDRGRTRERKHPFEGVIPNLERRYRETESEYVREEL 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 398 RLYMRELTCQTCHGYRLNRKALSVKIDGKHIAEISALPIDSAMEFFGNLNFSEQDTAVATPILKEIKDRLNFLRNVGLEY 477
Cdd:PRK00349 401 EKYMSERPCPSCKGKRLKPEALAVKVGGKNIGEVSELSIGEALEFFENLKLSEQEAKIAEPILKEIRERLKFLVDVGLDY 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 478 LTLSRSARTLSGGEAQRIRLATQIGSNLSGVLYILDEPSIGLHQRDNNRLISSLKKMRDLGNTLVVVEHDEDTMWAADYL 557
Cdd:PRK00349 481 LTLSRSAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDEDTIRAADYI 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 558 IDIGPGAGENGGEVMAAGTPKQVAKSRKSLTGKYLSGKKFIPVPETRRTGNGQSIKLKGVQENNLKNIDVDFPLGEFVAV 637
Cdd:PRK00349 561 VDIGPGAGVHGGEVVASGTPEEIMKNPNSLTGQYLSGKKKIEVPKERRKGNGKFLKLKGARENNLKNVDVEIPLGKFTCV 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 638 TGVSGSGKSTLVNMVLKRVLAQKLNHNSEKPGKYKSVSGIKNIEKVINIDQSPIGRTPRSNPATYTSVFDDIRGLFAQTN 717
Cdd:PRK00349 641 TGVSGSGKSTLINETLYKALARKLNGAKKVPGKHKEIEGLEHLDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAGTP 720
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 718 EAKLRGYTKGRFSFNVKGGRCEACKGDGILKIEMNFLPDVYVPCEVCHGTRYNSETLEVKYKGKTIADILDMTVEEATDF 797
Cdd:PRK00349 721 EAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEF 800
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 798 FAPIPKIARKLQTIIDVGLGYVHLGQSATTLSGGEAQRMKLASELHKKANGKNFYILDEPTTGLHTDDIKRLLDVLQRLV 877
Cdd:PRK00349 801 FEAIPKIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELSKRSTGKTLYILDEPTTGLHFEDIRKLLEVLHRLV 880
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488923006 878 DNGNTVLVIEHNLDVIKTADHLIDLGPEGGAGGGQVVAVGTPEAIAAVPESYTGKYLKEVLER 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: 1930.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006   1 MANDKIVIHGARAHNLKNIDVTIPRDKLVVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLGQMDKPDVDSIDG 80
Cdd:PRK00349   1 MMMDKIIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  81 LSPAISIDQKTTSKNPRSTVGTVTEINDYLRLLWARVGQPICPNDGTPITSQTVEQMVNRVLDLPERSKVQIISPIVRAK 160
Cdd:PRK00349  81 LSPAISIDQKTTSHNPRSTVGTVTEIYDYLRLLYARVGKPHCPNCGRPIEAQTVSQMVDRVLELPEGTRLQILAPVVRGR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 161 KGQHKKVFEKIKREGFVRVRVDDETMDVEEVPELDKNKVHTIDIVVDRVVVKDGIRSRLFDSFEAALRLSKGYATADVIG 240
Cdd:PRK00349 161 KGEHKKLLENLRKQGFVRVRVDGEVYDLDEPPKLDKNKKHTIEVVVDRLVVKEDIRQRLADSIETALKLSDGLVVVEVMD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 241 G---EPILFSEHYSCPVCGFTVGELEPRLFSFNAPFGACPECDGLGIKLEVDEDLVIPDPSKTLREGAIAPWNPISSQYY 317
Cdd:PRK00349 241 DpeaEELLFSEKFACPVCGFSIPELEPRLFSFNSPYGACPTCDGLGVKLEFDPDLVVPDPELSLAEGAIAPWSRSSSSYY 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 318 PTLLEQAAKSFGIDMDTPFEDLPKADRQLVLYGSKGKKFHFHYENDFGGVRDVDSVFEGVMVNIDRRYHETNSDFTRDQM 397
Cdd:PRK00349 321 FQMLKSLAEHYGFDLDTPWKDLPEEVQDIILYGSGDEEIEFRYKNDRGRTRERKHPFEGVIPNLERRYRETESEYVREEL 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 398 RLYMRELTCQTCHGYRLNRKALSVKIDGKHIAEISALPIDSAMEFFGNLNFSEQDTAVATPILKEIKDRLNFLRNVGLEY 477
Cdd:PRK00349 401 EKYMSERPCPSCKGKRLKPEALAVKVGGKNIGEVSELSIGEALEFFENLKLSEQEAKIAEPILKEIRERLKFLVDVGLDY 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 478 LTLSRSARTLSGGEAQRIRLATQIGSNLSGVLYILDEPSIGLHQRDNNRLISSLKKMRDLGNTLVVVEHDEDTMWAADYL 557
Cdd:PRK00349 481 LTLSRSAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDEDTIRAADYI 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 558 IDIGPGAGENGGEVMAAGTPKQVAKSRKSLTGKYLSGKKFIPVPETRRTGNGQSIKLKGVQENNLKNIDVDFPLGEFVAV 637
Cdd:PRK00349 561 VDIGPGAGVHGGEVVASGTPEEIMKNPNSLTGQYLSGKKKIEVPKERRKGNGKFLKLKGARENNLKNVDVEIPLGKFTCV 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 638 TGVSGSGKSTLVNMVLKRVLAQKLNHNSEKPGKYKSVSGIKNIEKVINIDQSPIGRTPRSNPATYTSVFDDIRGLFAQTN 717
Cdd:PRK00349 641 TGVSGSGKSTLINETLYKALARKLNGAKKVPGKHKEIEGLEHLDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAGTP 720
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 718 EAKLRGYTKGRFSFNVKGGRCEACKGDGILKIEMNFLPDVYVPCEVCHGTRYNSETLEVKYKGKTIADILDMTVEEATDF 797
Cdd:PRK00349 721 EAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEF 800
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 798 FAPIPKIARKLQTIIDVGLGYVHLGQSATTLSGGEAQRMKLASELHKKANGKNFYILDEPTTGLHTDDIKRLLDVLQRLV 877
Cdd:PRK00349 801 FEAIPKIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELSKRSTGKTLYILDEPTTGLHFEDIRKLLEVLHRLV 880
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488923006 878 DNGNTVLVIEHNLDVIKTADHLIDLGPEGGAGGGQVVAVGTPEAIAAVPESYTGKYLKEVLER 940
Cdd:PRK00349 881 DKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVATGTPEEVAKVEASYTGRYLKPVLER 943
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
1-941 0e+00

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


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 1861.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006   1 MANDKIVIHGARAHNLKNIDVTIPRDKLVVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLGQMDKPDVDSIDG 80
Cdd:COG0178    1 MMMDKIRIRGAREHNLKNIDVDIPRNKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  81 LSPAISIDQKTTSKNPRSTVGTVTEINDYLRLLWARVGQPICPNDGTPITSQTVEQMVNRVLDLPERSKVQIISPIVRAK 160
Cdd:COG0178   81 LSPAISIEQKTTSRNPRSTVGTVTEIYDYLRLLFARVGTPHCPICGRPVEKQTVDQIVDRILALPEGTRLQILAPVVRGR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 161 KGQHKKVFEKIKREGFVRVRVDDETMDVEEVPELDKNKVHTIDIVVDRVVVKDGIRSRLFDSFEAALRLSKGYATADVIG 240
Cdd:COG0178  161 KGEHKELLEELRKQGFVRVRVDGEVYDLDEEPELDKNKKHTIEVVVDRLVVKEDIRSRLADSVETALKLGDGLVIVEVVD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 241 -GEPILFSEHYSCPVCGFTVGELEPRLFSFNAPFGACPECDGLGIKLEVDEDLVIPDPSKTLREGAIAPWNPISSQYYPT 319
Cdd:COG0178  241 eGEELLFSEKFACPDCGISFEELEPRLFSFNSPYGACPTCDGLGRVLEFDPDLVIPDPSLSLAEGAIAPWSGPSSSYYFQ 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 320 LLEQAAKSFGIDMDTPFEDLPKADRQLVLYGSkGKKFHFHYENdFGGVRDVDSVFEGVMVNIDRRYHETNSDFTRDQMRL 399
Cdd:COG0178  321 LLEALAKHYGFDLDTPWKDLPEEQRDLILYGS-DEKIKFRYKN-RGRRRTYEKPFEGVIPFLERRYRETYSEHVREELSR 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 400 YMRELTCQTCHGYRLNRKALSVKIDGKHIAEISALPIDSAMEFFGNLNFSEQDTAVATPILKEIKDRLNFLRNVGLEYLT 479
Cdd:COG0178  399 YMSETPCPACKGARLKPEALAVKIGGKNIAELTALSIDEALEFFENLELTEREAEIAERILKEIRSRLGFLVDVGLDYLT 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 480 LSRSARTLSGGEAQRIRLATQIGSNLSGVLYILDEPSIGLHQRDNNRLISSLKKMRDLGNTLVVVEHDEDTMWAADYLID 559
Cdd:COG0178  479 LDRSAGTLSGGEAQRIRLATQIGSGLVGVLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDTIRAADYIID 558
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 560 IGPGAGENGGEVMAAGTPKQVAKSRKSLTGKYLSGKKFIPVPETRRTGNGQSIKLKGVQENNLKNIDVDFPLGEFVAVTG 639
Cdd:COG0178  559 IGPGAGEHGGEVVAQGTPEEILKNPDSLTGQYLSGRKRIPVPKKRRKGNGKFLTIKGARENNLKNVDVEIPLGVLTCVTG 638
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 640 VSGSGKSTLVNMVLKRVLAQKLNHNSEKPGKYKSVSGIKNIEKVINIDQSPIGRTPRSNPATYTSVFDDIRGLFAQTNEA 719
Cdd:COG0178  639 VSGSGKSTLVNDILYPALARKLNGAKEKPGPHDSIEGLEHIDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAQTPEA 718
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 720 KLRGYTKGRFSFNVKGGRCEACKGDGILKIEMNFLPDVYVPCEVCHGTRYNSETLEVKYKGKTIADILDMTVEEATDFFA 799
Cdd:COG0178  719 KARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEFFE 798
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 800 PIPKIARKLQTIIDVGLGYVHLGQSATTLSGGEAQRMKLASELHKKANGKNFYILDEPTTGLHTDDIKRLLDVLQRLVDN 879
Cdd:COG0178  799 NIPKIARKLQTLQDVGLGYIKLGQPATTLSGGEAQRVKLASELSKRSTGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDK 878
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488923006 880 GNTVLVIEHNLDVIKTADHLIDLgpeggagggqvvavgTPEAIAAVPESYTGKYLKEVLERA 941
Cdd:COG0178  879 GNTVVVIEHNLDVIKTADWIIDLgpeggdgggeivaegTPEEVAKVKASYTGRYLKEYLEAA 940
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
5-902 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: 1518.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006    5 KIVIHGARAHNLKNIDVTIPRDKLVVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLGQMDKPDVDSIDGLSPA 84
Cdd:TIGR00630   1 KIIVRGAREHNLKNIDVEIPRDKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGVMDKPDVDSIEGLSPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006   85 ISIDQKTTSKNPRSTVGTVTEINDYLRLLWARVGQPICPNDGTPITSQTVEQMVNRVLDLPERSKVQIISPIVRAKKGQH 164
Cdd:TIGR00630  81 ISIDQKTTSHNPRSTVGTITEIYDYLRLLFARVGTPYCPTCGRPISRQTPSQIVDQILALPEGTRVILLAPIVRGRKGEF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  165 KKVFEKIKREGFVRVRVDDETMDVEEVPELDKNKVHTIDIVVDRVVVKDGIRSRLFDSFEAALRLSKGYATA------DV 238
Cdd:TIGR00630 161 RKLLEKLRKQGFARVRVDGEVYPLEDPPKLEKNKKHTIDVVIDRLTVKNENRSRLAESVETALRLGDGLLEVefdddeEV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  239 IGGEPILFSEHYSCPVCGFTVGELEPRLFSFNAPFGACPECDGLGIKLEVDEDLVIPDPSKTLREGAIAPWNPISSQYYP 318
Cdd:TIGR00630 241 AESKEELFSEKFACPECGFSLPELEPRLFSFNSPYGACPECSGLGIKQEFDPELIIPDPLLSLNGGAIVPFKKSTTSYYR 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  319 TLLEQAAKSFGIDMDTPFEDLPKADRQLVLYGSKGKKFHFHYENDFGGVRDVDSVFEGVMVNIDRRYHETNSDFTRDQMR 398
Cdd:TIGR00630 321 QMFASLAEHLGFDLDTPWKDLPEEAQKAILYGSGEEVIVVKYRNGGGETFRYHKPFEGVIPELERRYLETESESMREYLE 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  399 LYMRELTCQTCHGYRLNRKALSVKIDGKHIAEISALPIDSAMEFFGNLNFSEQDTAVATPILKEIKDRLNFLRNVGLEYL 478
Cdd:TIGR00630 401 KFMSERPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFNQLTLTPEEKKIAEEVLKEIRERLGFLIDVGLDYL 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  479 TLSRSARTLSGGEAQRIRLATQIGSNLSGVLYILDEPSIGLHQRDNNRLISSLKKMRDLGNTLVVVEHDEDTMWAADYLI 558
Cdd:TIGR00630 481 SLSRAAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVI 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  559 DIGPGAGENGGEVMAAGTPKQVAKSRKSLTGKYLSGKKFIPVPETRRTGNGQSIKLKGVQENNLKNIDVDFPLGEFVAVT 638
Cdd:TIGR00630 561 DIGPGAGEHGGEVVASGTPEEILANPDSLTGQYLSGRKKIEVPAERRPGNGKFLTLKGARENNLKNITVSIPLGLFTCIT 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  639 GVSGSGKSTLVNMVLKRVLAQKLNHNSEKPGKYKSVSGIKNIEKVINIDQSPIGRTPRSNPATYTSVFDDIRGLFAQTNE 718
Cdd:TIGR00630 641 GVSGSGKSTLINDTLYPALANRLNGAKTVPGRYTSIEGLEHLDKVIHIDQSPIGRTPRSNPATYTGVFDEIRELFAETPE 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  719 AKLRGYTKGRFSFNVKGGRCEACKGDGILKIEMNFLPDVYVPCEVCHGTRYNSETLEVKYKGKTIADILDMTVEEATDFF 798
Cdd:TIGR00630 721 AKVRGYTPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEAYEFF 800
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  799 APIPKIARKLQTIIDVGLGYVHLGQSATTLSGGEAQRMKLASELHKKANGKNFYILDEPTTGLHTDDIKRLLDVLQRLVD 878
Cdd:TIGR00630 801 EAVPSISRKLQTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKRSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVD 880
                         890       900
                  ....*....|....*....|....
gi 488923006  879 NGNTVLVIEHNLDVIKTADHLIDL 902
Cdd:TIGR00630 881 KGNTVVVIEHNLDVIKTADYIIDL 904
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
612-902 9.62e-151

ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213238 [Multi-domain]  Cd Length: 261  Bit Score: 445.52  E-value: 9.62e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 612 IKLKGVQENNLKNIDVDFPLGEFVAVTGVSGSGKSTLVNMVLKRVLAQKLNHNSEKPGKYKSVSGIKNIEKVINIDQSPI 691
Cdd:cd03271    1 LTLKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPALARRLHLKKEQPGNHDRIEGLEHIDKVIVIDQSPI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 692 GRTPRSNPATYTSVFDDIRGLFaqtneaklrgytkgrfsfnvkggrceackgdgilkiemnflpdvyvpCEVCHGTRYNS 771
Cdd:cd03271   81 GRTPRSNPATYTGVFDEIRELF-----------------------------------------------CEVCKGKRYNR 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 772 ETLEVKYKGKTIADILDMTVEEATDFFAPIPKIARKLQTIIDVGLGYVHLGQSATTLSGGEAQRMKLASELHKKANGKNF 851
Cdd:cd03271  114 ETLEVRYKGKSIADVLDMTVEEALEFFENIPKIARKLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRSTGKTL 193
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488923006 852 YILDEPTTGLHTDDIKRLLDVLQRLVDNGNTVLVIEHNLDVIKTADHLIDL 902
Cdd:cd03271  194 YILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDL 244
UvrA_DNA-bind pfam17755
UvrA DNA-binding domain;
289-397 2.31e-51

UvrA DNA-binding domain;


Pssm-ID: 465484 [Multi-domain]  Cd Length: 110  Bit Score: 175.35  E-value: 2.31e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  289 DEDLVIPDPSKTLREGAIAPWNPISSQYYPTLLEQAAKSFGIDMDTPFEDLPKADRQLVLYGSKGKKFHFHYENdFGGVR 368
Cdd:pfam17755   1 DPDLVIPDPSLSLAEGAIAPWGKKRSSYYFQLLEALAKHYGFDLDTPFKDLPEEQQDIILYGSGEEIIVFYYSR-GGRTR 79
                          90       100
                  ....*....|....*....|....*....
gi 488923006  369 DVDSVFEGVMVNIDRRYHETNSDFTRDQM 397
Cdd:pfam17755  80 TYTKPFEGVIPNLERRYRETDSESVREEL 108
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
622-902 1.58e-09

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 58.40  E-value: 1.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTLVNMvlkrvlaqklnhnsekpgkyksvsgikniekvinidqspigrtprsnpat 701
Cdd:NF040873   8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKV-------------------------------------------------- 37
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 702 ytsvfddIRGLFAQTneaklrgytkgrfsfnvkGGRCEACKGDGIlkiemnflpdVYVPcevchgtrYNSEtlevkykgk 781
Cdd:NF040873  38 -------LAGVLRPT------------------SGTVRRAGGARV----------AYVP--------QRSE--------- 65
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 782 tIADILDMTVEEATD--FFA---PIPKIARKLQTIIDVGLGYVHL----GQSATTLSGGEAQRMKLASELHKKAngkNFY 852
Cdd:NF040873  66 -VPDSLPLTVRDLVAmgRWArrgLWRRLTRDDRAAVDDALERVGLadlaGRQLGELSGGQRQRALLAQGLAQEA---DLL 141
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 488923006 853 ILDEPTTGLHTDDIKRLLDVLQRLVDNGNTVLVIEHNLDVIKTADHLIDL 902
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
 
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: 1930.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006   1 MANDKIVIHGARAHNLKNIDVTIPRDKLVVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLGQMDKPDVDSIDG 80
Cdd:PRK00349   1 MMMDKIIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  81 LSPAISIDQKTTSKNPRSTVGTVTEINDYLRLLWARVGQPICPNDGTPITSQTVEQMVNRVLDLPERSKVQIISPIVRAK 160
Cdd:PRK00349  81 LSPAISIDQKTTSHNPRSTVGTVTEIYDYLRLLYARVGKPHCPNCGRPIEAQTVSQMVDRVLELPEGTRLQILAPVVRGR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 161 KGQHKKVFEKIKREGFVRVRVDDETMDVEEVPELDKNKVHTIDIVVDRVVVKDGIRSRLFDSFEAALRLSKGYATADVIG 240
Cdd:PRK00349 161 KGEHKKLLENLRKQGFVRVRVDGEVYDLDEPPKLDKNKKHTIEVVVDRLVVKEDIRQRLADSIETALKLSDGLVVVEVMD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 241 G---EPILFSEHYSCPVCGFTVGELEPRLFSFNAPFGACPECDGLGIKLEVDEDLVIPDPSKTLREGAIAPWNPISSQYY 317
Cdd:PRK00349 241 DpeaEELLFSEKFACPVCGFSIPELEPRLFSFNSPYGACPTCDGLGVKLEFDPDLVVPDPELSLAEGAIAPWSRSSSSYY 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 318 PTLLEQAAKSFGIDMDTPFEDLPKADRQLVLYGSKGKKFHFHYENDFGGVRDVDSVFEGVMVNIDRRYHETNSDFTRDQM 397
Cdd:PRK00349 321 FQMLKSLAEHYGFDLDTPWKDLPEEVQDIILYGSGDEEIEFRYKNDRGRTRERKHPFEGVIPNLERRYRETESEYVREEL 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 398 RLYMRELTCQTCHGYRLNRKALSVKIDGKHIAEISALPIDSAMEFFGNLNFSEQDTAVATPILKEIKDRLNFLRNVGLEY 477
Cdd:PRK00349 401 EKYMSERPCPSCKGKRLKPEALAVKVGGKNIGEVSELSIGEALEFFENLKLSEQEAKIAEPILKEIRERLKFLVDVGLDY 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 478 LTLSRSARTLSGGEAQRIRLATQIGSNLSGVLYILDEPSIGLHQRDNNRLISSLKKMRDLGNTLVVVEHDEDTMWAADYL 557
Cdd:PRK00349 481 LTLSRSAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDEDTIRAADYI 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 558 IDIGPGAGENGGEVMAAGTPKQVAKSRKSLTGKYLSGKKFIPVPETRRTGNGQSIKLKGVQENNLKNIDVDFPLGEFVAV 637
Cdd:PRK00349 561 VDIGPGAGVHGGEVVASGTPEEIMKNPNSLTGQYLSGKKKIEVPKERRKGNGKFLKLKGARENNLKNVDVEIPLGKFTCV 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 638 TGVSGSGKSTLVNMVLKRVLAQKLNHNSEKPGKYKSVSGIKNIEKVINIDQSPIGRTPRSNPATYTSVFDDIRGLFAQTN 717
Cdd:PRK00349 641 TGVSGSGKSTLINETLYKALARKLNGAKKVPGKHKEIEGLEHLDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAGTP 720
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 718 EAKLRGYTKGRFSFNVKGGRCEACKGDGILKIEMNFLPDVYVPCEVCHGTRYNSETLEVKYKGKTIADILDMTVEEATDF 797
Cdd:PRK00349 721 EAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEF 800
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 798 FAPIPKIARKLQTIIDVGLGYVHLGQSATTLSGGEAQRMKLASELHKKANGKNFYILDEPTTGLHTDDIKRLLDVLQRLV 877
Cdd:PRK00349 801 FEAIPKIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELSKRSTGKTLYILDEPTTGLHFEDIRKLLEVLHRLV 880
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488923006 878 DNGNTVLVIEHNLDVIKTADHLIDLGPEGGAGGGQVVAVGTPEAIAAVPESYTGKYLKEVLER 940
Cdd:PRK00349 881 DKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVATGTPEEVAKVEASYTGRYLKPVLER 943
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
1-941 0e+00

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


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 1861.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006   1 MANDKIVIHGARAHNLKNIDVTIPRDKLVVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLGQMDKPDVDSIDG 80
Cdd:COG0178    1 MMMDKIRIRGAREHNLKNIDVDIPRNKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  81 LSPAISIDQKTTSKNPRSTVGTVTEINDYLRLLWARVGQPICPNDGTPITSQTVEQMVNRVLDLPERSKVQIISPIVRAK 160
Cdd:COG0178   81 LSPAISIEQKTTSRNPRSTVGTVTEIYDYLRLLFARVGTPHCPICGRPVEKQTVDQIVDRILALPEGTRLQILAPVVRGR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 161 KGQHKKVFEKIKREGFVRVRVDDETMDVEEVPELDKNKVHTIDIVVDRVVVKDGIRSRLFDSFEAALRLSKGYATADVIG 240
Cdd:COG0178  161 KGEHKELLEELRKQGFVRVRVDGEVYDLDEEPELDKNKKHTIEVVVDRLVVKEDIRSRLADSVETALKLGDGLVIVEVVD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 241 -GEPILFSEHYSCPVCGFTVGELEPRLFSFNAPFGACPECDGLGIKLEVDEDLVIPDPSKTLREGAIAPWNPISSQYYPT 319
Cdd:COG0178  241 eGEELLFSEKFACPDCGISFEELEPRLFSFNSPYGACPTCDGLGRVLEFDPDLVIPDPSLSLAEGAIAPWSGPSSSYYFQ 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 320 LLEQAAKSFGIDMDTPFEDLPKADRQLVLYGSkGKKFHFHYENdFGGVRDVDSVFEGVMVNIDRRYHETNSDFTRDQMRL 399
Cdd:COG0178  321 LLEALAKHYGFDLDTPWKDLPEEQRDLILYGS-DEKIKFRYKN-RGRRRTYEKPFEGVIPFLERRYRETYSEHVREELSR 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 400 YMRELTCQTCHGYRLNRKALSVKIDGKHIAEISALPIDSAMEFFGNLNFSEQDTAVATPILKEIKDRLNFLRNVGLEYLT 479
Cdd:COG0178  399 YMSETPCPACKGARLKPEALAVKIGGKNIAELTALSIDEALEFFENLELTEREAEIAERILKEIRSRLGFLVDVGLDYLT 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 480 LSRSARTLSGGEAQRIRLATQIGSNLSGVLYILDEPSIGLHQRDNNRLISSLKKMRDLGNTLVVVEHDEDTMWAADYLID 559
Cdd:COG0178  479 LDRSAGTLSGGEAQRIRLATQIGSGLVGVLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDTIRAADYIID 558
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 560 IGPGAGENGGEVMAAGTPKQVAKSRKSLTGKYLSGKKFIPVPETRRTGNGQSIKLKGVQENNLKNIDVDFPLGEFVAVTG 639
Cdd:COG0178  559 IGPGAGEHGGEVVAQGTPEEILKNPDSLTGQYLSGRKRIPVPKKRRKGNGKFLTIKGARENNLKNVDVEIPLGVLTCVTG 638
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 640 VSGSGKSTLVNMVLKRVLAQKLNHNSEKPGKYKSVSGIKNIEKVINIDQSPIGRTPRSNPATYTSVFDDIRGLFAQTNEA 719
Cdd:COG0178  639 VSGSGKSTLVNDILYPALARKLNGAKEKPGPHDSIEGLEHIDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAQTPEA 718
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 720 KLRGYTKGRFSFNVKGGRCEACKGDGILKIEMNFLPDVYVPCEVCHGTRYNSETLEVKYKGKTIADILDMTVEEATDFFA 799
Cdd:COG0178  719 KARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEFFE 798
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 800 PIPKIARKLQTIIDVGLGYVHLGQSATTLSGGEAQRMKLASELHKKANGKNFYILDEPTTGLHTDDIKRLLDVLQRLVDN 879
Cdd:COG0178  799 NIPKIARKLQTLQDVGLGYIKLGQPATTLSGGEAQRVKLASELSKRSTGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDK 878
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488923006 880 GNTVLVIEHNLDVIKTADHLIDLgpeggagggqvvavgTPEAIAAVPESYTGKYLKEVLERA 941
Cdd:COG0178  879 GNTVVVIEHNLDVIKTADWIIDLgpeggdgggeivaegTPEEVAKVKASYTGRYLKEYLEAA 940
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
5-902 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: 1518.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006    5 KIVIHGARAHNLKNIDVTIPRDKLVVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLGQMDKPDVDSIDGLSPA 84
Cdd:TIGR00630   1 KIIVRGAREHNLKNIDVEIPRDKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGVMDKPDVDSIEGLSPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006   85 ISIDQKTTSKNPRSTVGTVTEINDYLRLLWARVGQPICPNDGTPITSQTVEQMVNRVLDLPERSKVQIISPIVRAKKGQH 164
Cdd:TIGR00630  81 ISIDQKTTSHNPRSTVGTITEIYDYLRLLFARVGTPYCPTCGRPISRQTPSQIVDQILALPEGTRVILLAPIVRGRKGEF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  165 KKVFEKIKREGFVRVRVDDETMDVEEVPELDKNKVHTIDIVVDRVVVKDGIRSRLFDSFEAALRLSKGYATA------DV 238
Cdd:TIGR00630 161 RKLLEKLRKQGFARVRVDGEVYPLEDPPKLEKNKKHTIDVVIDRLTVKNENRSRLAESVETALRLGDGLLEVefdddeEV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  239 IGGEPILFSEHYSCPVCGFTVGELEPRLFSFNAPFGACPECDGLGIKLEVDEDLVIPDPSKTLREGAIAPWNPISSQYYP 318
Cdd:TIGR00630 241 AESKEELFSEKFACPECGFSLPELEPRLFSFNSPYGACPECSGLGIKQEFDPELIIPDPLLSLNGGAIVPFKKSTTSYYR 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  319 TLLEQAAKSFGIDMDTPFEDLPKADRQLVLYGSKGKKFHFHYENDFGGVRDVDSVFEGVMVNIDRRYHETNSDFTRDQMR 398
Cdd:TIGR00630 321 QMFASLAEHLGFDLDTPWKDLPEEAQKAILYGSGEEVIVVKYRNGGGETFRYHKPFEGVIPELERRYLETESESMREYLE 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  399 LYMRELTCQTCHGYRLNRKALSVKIDGKHIAEISALPIDSAMEFFGNLNFSEQDTAVATPILKEIKDRLNFLRNVGLEYL 478
Cdd:TIGR00630 401 KFMSERPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFNQLTLTPEEKKIAEEVLKEIRERLGFLIDVGLDYL 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  479 TLSRSARTLSGGEAQRIRLATQIGSNLSGVLYILDEPSIGLHQRDNNRLISSLKKMRDLGNTLVVVEHDEDTMWAADYLI 558
Cdd:TIGR00630 481 SLSRAAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVI 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  559 DIGPGAGENGGEVMAAGTPKQVAKSRKSLTGKYLSGKKFIPVPETRRTGNGQSIKLKGVQENNLKNIDVDFPLGEFVAVT 638
Cdd:TIGR00630 561 DIGPGAGEHGGEVVASGTPEEILANPDSLTGQYLSGRKKIEVPAERRPGNGKFLTLKGARENNLKNITVSIPLGLFTCIT 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  639 GVSGSGKSTLVNMVLKRVLAQKLNHNSEKPGKYKSVSGIKNIEKVINIDQSPIGRTPRSNPATYTSVFDDIRGLFAQTNE 718
Cdd:TIGR00630 641 GVSGSGKSTLINDTLYPALANRLNGAKTVPGRYTSIEGLEHLDKVIHIDQSPIGRTPRSNPATYTGVFDEIRELFAETPE 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  719 AKLRGYTKGRFSFNVKGGRCEACKGDGILKIEMNFLPDVYVPCEVCHGTRYNSETLEVKYKGKTIADILDMTVEEATDFF 798
Cdd:TIGR00630 721 AKVRGYTPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEAYEFF 800
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  799 APIPKIARKLQTIIDVGLGYVHLGQSATTLSGGEAQRMKLASELHKKANGKNFYILDEPTTGLHTDDIKRLLDVLQRLVD 878
Cdd:TIGR00630 801 EAVPSISRKLQTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKRSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVD 880
                         890       900
                  ....*....|....*....|....
gi 488923006  879 NGNTVLVIEHNLDVIKTADHLIDL 902
Cdd:TIGR00630 881 KGNTVVVIEHNLDVIKTADYIIDL 904
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
1-944 0e+00

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 634.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006    1 MANDKIVIHGARAHNLKNIDVTIPRDKLVVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLGQMDKPDVDSIDG 80
Cdd:PRK00635    1 MPSLPVRLSGITVRNLKNISIEFCPREIVLLTGVSGSGKSSLAFDTIYAAGRKRYLSTLPSFFATTLDSLPDPSVEKIEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006   81 LSPAISIDQKTTSKNPRSTVGTVTEINDYLRLLWARVGQPICPNDGTPITSQTVEQMVNRVLDLPERSKVQIISPIVRak 160
Cdd:PRK00635   81 LSPTIAVKQNHFSQHSHATVGSTTELNSHLALLFSLEGQARDPVTLHPLTLYSKEKILSTIAAIPDGTQITLLAPLPA-- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  161 kGQHKKVFEKIkREGFVRVRVDDETMDV---------EEVP------ELDKNKVHTidivvdrvvvkdgirSRLFDSFEA 225
Cdd:PRK00635  159 -KDILAIRECL-RQGFTKVRIDGEISPIykfltsgipEDVPvdivvdTLIKNESNT---------------ARLKVSLFT 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  226 ALRLSKGYATADViGGEPILFSEHYSCPVCGFTVGELEPRLFSFNAPFGACPECDGLGIKLEVDEDLVIpDPSKTLREGA 305
Cdd:PRK00635  222 ALDIGHGECSLHF-DNQKRTFSTQATIPETQQTYTPLTPQLFSPHSLEDRCPQCQGSGIFISIDDPSLI-QQNLSIEENC 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  306 IAPWNPISSQYYPTLLEQAAKSFGIDMDTPFEDLPKADRQLVLYGSKGKKFHFH-YENDFGGVRDVDSVFEGVMVNIDR- 383
Cdd:PRK00635  300 CPFAGNCSTYLYHTIYQSLADSLGFSLSTPWKDLSPEIQNIFLYGKEGLVLPVRlFDGTLGKKTLTHKVWRGVLNEIGEk 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  384 -RYHETNSDFTRDQMRLYmrelTCQTCHGYRLNRKALSVKIDGKHIAEISALPIDSAMEFFGNLNFSEQDTavaTPILKE 462
Cdd:PRK00635  380 vRYSNKPSRYLPKGTSAT----SCPRCQGTGLGDYANAATWHGKTFAEFQQMSLQELFIFLSQLPSKSLSI---EEVLQG 452
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  463 IKDRLNFLRNVGLEYLTLSRSARTLSGGEAQRIRLATQIGSNLSGVLYILDEPSIGLHQRDNNRLISSLKKMRDLGNTLV 542
Cdd:PRK00635  453 LKSRLSILIDLGLPYLTPERALATLSGGEQERTALAKHLGAELIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVL 532
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  543 VVEHDEDTMWAADYLIDIGPGAGENGGEVMAAGTPKQVAKSRKSLTGKYLSGKKFIPVPETRRTGNGqSIKLKGVQENNL 622
Cdd:PRK00635  533 LVEHDEQMISLADRIIDIGPGAGIFGGEVLFNGSPREFLAKSDSLTAKYLRQELTIPIPEKRTNSLG-TLTLSKATKHNL 611
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  623 KNIDVDFPLGEFVAVTGVSGSGKSTLVNMVL----KRVLAQKlnhnsekPGKYKSVSGIKnIEKVINIDQSPIGRTPRSN 698
Cdd:PRK00635  612 KDLTISLPLGRLTVVTGVSGSGKSSLINDTLvpavEEFIEQG-------FCSNLSIQWGA-ISRLVHITRDLPGRSQRSI 683
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  699 PATYTSVFDDIRGLFAQTNEAKLRGYTKGRFSFNVKGGRCEACKGDGILKIEMNFLPdvyVPCEVCHGTRYNSETLEVKY 778
Cdd:PRK00635  684 PLTYIKAFDDLRELFAEQPRSKRLGLTKSHFSFNTPLGACAECQGLGSITTTDNRTS---IPCPSCLGKRFLPQVLEVRY 760
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  779 KGKTIADILDMTVEEATDFFAPIPKIARKLQTIIDVGLGYVHLGQSATTLSGGEAQRMKLASELHKKANGKNFYILDEPT 858
Cdd:PRK00635  761 KGKNIADILEMTAYEAEKFFLDEPSIHEKIHALCSLGLDYLPLGRPLSSLSGGEIQRLKLAYELLAPSKKPTLYVLDEPT 840
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  859 TGLHTDDIKRLLDVLQRLVDNGNTVLVIEHNLDVIKTADHLIDLGPEGGAGGGQVVAVGTPEAIAAVpESYTGKYLKEVL 938
Cdd:PRK00635  841 TGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLELGPEGGNLGGYLLASCSPEELIHL-HTPTAKALRPYL 919

                  ....*.
gi 488923006  939 ERAQEL 944
Cdd:PRK00635  920 SSPQEL 925
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
612-902 9.62e-151

ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213238 [Multi-domain]  Cd Length: 261  Bit Score: 445.52  E-value: 9.62e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 612 IKLKGVQENNLKNIDVDFPLGEFVAVTGVSGSGKSTLVNMVLKRVLAQKLNHNSEKPGKYKSVSGIKNIEKVINIDQSPI 691
Cdd:cd03271    1 LTLKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPALARRLHLKKEQPGNHDRIEGLEHIDKVIVIDQSPI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 692 GRTPRSNPATYTSVFDDIRGLFaqtneaklrgytkgrfsfnvkggrceackgdgilkiemnflpdvyvpCEVCHGTRYNS 771
Cdd:cd03271   81 GRTPRSNPATYTGVFDEIRELF-----------------------------------------------CEVCKGKRYNR 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 772 ETLEVKYKGKTIADILDMTVEEATDFFAPIPKIARKLQTIIDVGLGYVHLGQSATTLSGGEAQRMKLASELHKKANGKNF 851
Cdd:cd03271  114 ETLEVRYKGKSIADVLDMTVEEALEFFENIPKIARKLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRSTGKTL 193
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488923006 852 YILDEPTTGLHTDDIKRLLDVLQRLVDNGNTVLVIEHNLDVIKTADHLIDL 902
Cdd:cd03271  194 YILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDL 244
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
6-902 1.41e-107

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 366.85  E-value: 1.41e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006    6 IVIHGARAHNLKNIDVTIPRDKLVVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQ-FLGQMDKPDVDSIDGLSPA 84
Cdd:PRK00635  941 ITIKNAYQHNLKHIDLSLPRNALTAVTGPSASGKHSLVFDILYAAGNIAYAELFPPYIRQaLIKKTPLPSVDKVTGLSPV 1020
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006   85 ISIDQKTTSKNPRSTVGTVTEINDYLRLLWARVGQPICPNDGTPITSQTVEQMVNRVLDLPERSKVQIISPIvrAKKGQH 164
Cdd:PRK00635 1021 IAIEKTSASKNSNHSVASALEISNGLEKLFARLGHPYSPLSGDALRKITPQTIAEELLTHYTKGYVTITSPI--PKEEDL 1098
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  165 KKVFEKIKREGFVRVRVDDETMDVEE-VPELDKNKV----HTIDIVVDRvvvkdgirSRLFDSFEAALRLSkgyATADV- 238
Cdd:PRK00635 1099 FIYLQEKLKEGFLKLYANEQFYDLDEpLPTSLENPAiviqHTKISEKNL--------SSLLSSLTLAFSLS---SSICLh 1167
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  239 IGGEPILFSEHYSC---PVCGFTVGELEPRLFSFNAPFGACPECDGLGIKLEVDedlVIPDPSKTLREGAIAPWNPISSQ 315
Cdd:PRK00635 1168 IEYAGTSLSLTYRLgwqDSSGNLYPNITTPLLSRDHEEGLCPLCHGKGFILKCS---LLPHKEKIAHYTPLSLFTLFFPN 1244
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  316 YYPTLLEQAAKSFGIDMDTPFEDLPKADRQLVLYGSKgkkfhfhyenDFGGVRDVdsvfegVMVNIDRryhETNSDFTRD 395
Cdd:PRK00635 1245 QDPKPVYPLLKELGIPSIALFQELDTLSFESLCLGTQ----------QHPGLNAL------LMEAMLM---ESEEPLPPP 1305
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  396 qmrlYMRELTCQTCHGYRLNRKALSVKIDGKHIAEIsalpIDSAMEFFGNLNFSEQDTAvATPILKEIKDRLNFLRNVGL 475
Cdd:PRK00635 1306 ----LISKTPCNQCQGLGVYTYAHCVRIHNTSLSDI----YQEDVTFLKKFLLTIHDDE-EPSIIQDLLNRLTFIDKVGL 1376
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  476 EYLTLSRSARTLSGGEAQRIRLATQIGSNLSGVLYILDEPSIGLHQRDNNRLISSLKKMRDLGNTLVVVEHDEDTMWAAD 555
Cdd:PRK00635 1377 SYITLGQEQDTLSDGEHYRLHLAKKISSNLTDIIYLLEDPLSGLHPQDAPTLLQLIKELVTNNNTVIATDRSGSLAEHAD 1456
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  556 YLIDIGPGAGENGGEVMAAGTPKQvakSRKSLTGKYLsgKKFIPVPETRrtgngqsiklkgVQENNLKNIDVDFPLGEFV 635
Cdd:PRK00635 1457 HLIHLGPGSGPQGGYLLSTSALKQ---SQPDLHNTRS--SEETPTLSVS------------LSIHTIQNLNVSAPLHSLV 1519
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  636 AVTGVSGSGKSTLV-NMVLKRvlAQKLNHNsekpgkyksvsGIKNIEKVINIDQSPIGRTPRSNPATYTSVFDDIRGLFA 714
Cdd:PRK00635 1520 AISGVSGSGKTSLLlEGFYKQ--ACALIEK-----------GPSVFSEIIFLDSHPQISSQRSDISTYFDIAPSLRNFYA 1586
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  715 QTNEAKLRGYTKGRFSFNVKGGRCEACKGDGILKIEMNFLPDVYVPCEVCHGTRYNSETLEVKYKGKTIADILDMTVEEA 794
Cdd:PRK00635 1587 SLTQAKALNISASMFSTNTKQGQCSDCWGLGYQWIDRAFYALEKRPCPTCSGFRIQPLAQEVVYEGKHFGQLLQTPIEEV 1666
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  795 TDFFAPIPKIARKLQTIIDVGLGYVHLGQSATTLSGGEAQRMKLASELHKKANGKNFYILDEPTTGLHTDDIKRLLDVLQ 874
Cdd:PRK00635 1667 AETFPFLKKIQKPLQALIDNGLGYLPLGQNLSSLSLSEKIAIKIAKFLYLPPKHPTLFLLDEIATSLDNQQKSALLVQLR 1746
                         890       900
                  ....*....|....*....|....*...
gi 488923006  875 RLVDNGNTVLVIEHNLDVIKTADHLIDL 902
Cdd:PRK00635 1747 TLVSLGHSVIYIDHDPALLKQADYLIEM 1774
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
6-118 1.29e-75

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: 247.17  E-value: 1.29e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006   6 IVIHGARAHNLKNIDVTIPRDKLVVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLGQMDKPDVDSIDGLSPAI 85
Cdd:cd03270    1 IIVRGAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLSPAI 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 488923006  86 SIDQKTTSKNPRSTVGTVTEINDYLRLLWARVG 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 1.12e-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: 228.30  E-value: 1.12e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 463 IKDRLNFLRNVGLEYLTLSRSARTLSGGEAQRIRLATQIGSNLSGVLYILDEPSIGLHQRDNNRLISSLKKMRDLGNTLV 542
Cdd:cd03270  114 IRERLGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVL 193
                         90       100       110
                 ....*....|....*....|....*....|...
gi 488923006 543 VVEHDEDTMWAADYLIDIGPGAGENGGEVMAAG 575
Cdd:cd03270  194 VVEHDEDTIRAADHVIDIGPGAGVHGGEIVAQG 226
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
400-577 1.32e-52

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: 184.74  E-value: 1.32e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 400 YMRELTCQTCHGYRLNRKALSVKIDGKHIAEISALPIDSAMEFFGNLnfseqdtavatpilKEIKDRLNFLRNVGLEYLT 479
Cdd:cd03271   97 EIRELFCEVCKGKRYNRETLEVRYKGKSIADVLDMTVEEALEFFENI--------------PKIARKLQTLCDVGLGYIK 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 480 LSRSARTLSGGEAQRIRLATQIGSNLSG-VLYILDEPSIGLHQRDNNRLISSLKKMRDLGNTLVVVEHDEDTMWAADYLI 558
Cdd:cd03271  163 LGQPATTLSGGEAQRIKLAKELSKRSTGkTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWII 242
                        170
                 ....*....|....*....
gi 488923006 559 DIGPGAGENGGEVMAAGTP 577
Cdd:cd03271  243 DLGPEGGDGGGQVVASGTP 261
UvrA_DNA-bind pfam17755
UvrA DNA-binding domain;
289-397 2.31e-51

UvrA DNA-binding domain;


Pssm-ID: 465484 [Multi-domain]  Cd Length: 110  Bit Score: 175.35  E-value: 2.31e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  289 DEDLVIPDPSKTLREGAIAPWNPISSQYYPTLLEQAAKSFGIDMDTPFEDLPKADRQLVLYGSKGKKFHFHYENdFGGVR 368
Cdd:pfam17755   1 DPDLVIPDPSLSLAEGAIAPWGKKRSSYYFQLLEALAKHYGFDLDTPFKDLPEEQQDIILYGSGEEIIVFYYSR-GGRTR 79
                          90       100
                  ....*....|....*....|....*....
gi 488923006  369 DVDSVFEGVMVNIDRRYHETNSDFTRDQM 397
Cdd:pfam17755  80 TYTKPFEGVIPNLERRYRETDSESVREEL 108
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
612-902 1.24e-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: 169.36  E-value: 1.24e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 612 IKLKGVQENNLKNIDVDFPLGEFVAVTGVSGSGKSTLVNMVL-----KRVL------AQKLNHNSEKPgkykSVSGIKNI 680
Cdd:cd03270    1 IIVRGAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIyaegqRRYVeslsayARQFLGQMDKP----DVDSIEGL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 681 EKVINIDQSPIGRTPRSNPATYTSVFDDIRGLFAQtneaklrgytkgrfsfnvkggrceackgDGILkiemnflpdvyvp 760
Cdd:cd03270   77 SPAIAIDQKTTSRNPRSTVGTVTEIYDYLRLLFAR----------------------------VGIR------------- 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 761 cevchgtrynsetlevkykgktiadildmtveeatdffapipkiaRKLQTIIDVGLGYVHLGQSATTLSGGEAQRMKLAS 840
Cdd:cd03270  116 ---------------------------------------------ERLGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLAT 150
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488923006 841 ELHKKANGKnFYILDEPTTGLHTDDIKRLLDVLQRLVDNGNTVLVIEHNLDVIKTADHLIDL 902
Cdd:cd03270  151 QIGSGLTGV-LYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDI 211
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
612-934 1.04e-45

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 177.90  E-value: 1.04e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  612 IKLKGVQENNLKNIDVDFPLGEFVAVTGVSGSGKSTLVNMVL-----KRVLA-------QKLNhNSEKPgkykSVSGIKN 679
Cdd:TIGR00630   2 IIVRGAREHNLKNIDVEIPRDKLVVITGLSGSGKSSLAFDTIyaegqRRYVEslsayarQFLG-VMDKP----DVDSIEG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  680 IEKVINIDQSPIGRTPRSNPATYTSVFDDIRGLFAQTNEA---------------------------------------- 719
Cdd:TIGR00630  77 LSPAISIDQKTTSHNPRSTVGTITEIYDYLRLLFARVGTPycptcgrpisrqtpsqivdqilalpegtrvillapivrgr 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  720 ---------KLR--GYTKGR------------------------------------------------------------ 728
Cdd:TIGR00630 157 kgefrklleKLRkqGFARVRvdgevypledppkleknkkhtidvvidrltvknenrsrlaesvetalrlgdgllevefdd 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  729 --------------------------------FSFNVKGGRCEACKGDGI------------------------------ 746
Cdd:TIGR00630 237 deevaeskeelfsekfacpecgfslpeleprlFSFNSPYGACPECSGLGIkqefdpeliipdpllslnggaivpfkkstt 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  747 ---------LKIEMNFLPDV------------------------------------------------------------ 757
Cdd:TIGR00630 317 syyrqmfasLAEHLGFDLDTpwkdlpeeaqkailygsgeevivvkyrngggetfryhkpfegvipelerryletesesmr 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  758 --------YVPCEVCHGTRYNSETLEVKYKGKTIADILDMTVEEATDFF-------------APIPK-IARKLQTIIDVG 815
Cdd:TIGR00630 397 eylekfmsERPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFnqltltpeekkiaEEVLKeIRERLGFLIDVG 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  816 LGYVHLGQSATTLSGGEAQRMKLASELHKKANGKnFYILDEPTTGLHTDDIKRLLDVLQRLVDNGNTVLVIEHNLDVIKT 895
Cdd:TIGR00630 477 LDYLSLSRAAGTLSGGEAQRIRLATQIGSGLTGV-LYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRA 555
                         570       580       590
                  ....*....|....*....|....*....|....*....
gi 488923006  896 ADHLIDLGPEGGAGGGQVVAVGTPEAIAAVPESYTGKYL 934
Cdd:TIGR00630 556 ADYVIDIGPGAGEHGGEVVASGTPEEILANPDSLTGQYL 594
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
465-575 5.39e-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: 159.80  E-value: 5.39e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 465 DRLNFLRNVGLEYLTLSRSARTLSGGEAQRIRLATQIGSNLSGVLYILDEPSIGLHQRDNNRLISSLKKMRDLGNTLVVV 544
Cdd:cd03238   66 DQLQFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILI 145
                         90       100       110
                 ....*....|....*....|....*....|.
gi 488923006 545 EHDEDTMWAADYLIDIGPGAGENGGEVMAAG 575
Cdd:cd03238  146 EHNLDVLSSADWIIDFGPGSGKSGGKVVFSG 176
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
404-902 1.89e-41

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 165.77  E-value: 1.89e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  404 LTCQTCHGYRLNRKALSVKIDGKHIAEISALPIDSAMEFFgnlnfseqdtaVATPilkEIKDRLNFLRNVGLEYLTLSRS 483
Cdd:PRK00635  741 IPCPSCLGKRFLPQVLEVRYKGKNIADILEMTAYEAEKFF-----------LDEP---SIHEKIHALCSLGLDYLPLGRP 806
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  484 ARTLSGGEAQRIRLATQIgsnLSGV----LYILDEPSIGLHQRDNNRLISSLKKMRDLGNTLVVVEHDEDTMWAADYLID 559
Cdd:PRK00635  807 LSSLSGGEIQRLKLAYEL---LAPSkkptLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLE 883
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  560 IGPGAGENGGEVMAAGTPKQVAkSRKSLTGK----YLSGKKFIP-VPETR-RTGNGQSIKLKGVQENNLKNIDVDFPLGE 633
Cdd:PRK00635  884 LGPEGGNLGGYLLASCSPEELI-HLHTPTAKalrpYLSSPQELPyLPDPSpKPPVPADITIKNAYQHNLKHIDLSLPRNA 962
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  634 FVAVTGVSGSGKSTLV--------NMVLKRVLAQKLNHNSEKPGKYKSVSGIKNIEKVINIDQSPIGRTPRSNPATYTSV 705
Cdd:PRK00635  963 LTAVTGPSASGKHSLVfdilyaagNIAYAELFPPYIRQALIKKTPLPSVDKVTGLSPVIAIEKTSASKNSNHSVASALEI 1042
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  706 FDDIRGLFAQ-------------------------------------------------TNEAKLRGYTK---------- 726
Cdd:PRK00635 1043 SNGLEKLFARlghpysplsgdalrkitpqtiaeellthytkgyvtitspipkeedlfiyLQEKLKEGFLKlyaneqfydl 1122
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  727 -GRF-------------------------------------------------------------------------SFN 732
Cdd:PRK00635 1123 dEPLptslenpaiviqhtkiseknlssllssltlafslsssiclhieyagtslsltyrlgwqdssgnlypnittpllSRD 1202
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  733 VKGGRCEACKGDG-ILKIEM-----------------NFLPDVYV----------------------------------- 759
Cdd:PRK00635 1203 HEEGLCPLCHGKGfILKCSLlphkekiahytplslftLFFPNQDPkpvypllkelgipsialfqeldtlsfeslclgtqq 1282
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  760 ----------------------------PCEVCHGTRYNSETLEVKYKGKTIADILDMTVEEATDFFAPI-----PKIAR 806
Cdd:PRK00635 1283 hpglnallmeamlmeseeplppplisktPCNQCQGLGVYTYAHCVRIHNTSLSDIYQEDVTFLKKFLLTIhddeePSIIQ 1362
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  807 KLQ---TIID-VGLGYVHLGQSATTLSGGEAQRMKLAselhkKANGKNF----YILDEPTTGLHTDDIKRLLDVLQRLVD 878
Cdd:PRK00635 1363 DLLnrlTFIDkVGLSYITLGQEQDTLSDGEHYRLHLA-----KKISSNLtdiiYLLEDPLSGLHPQDAPTLLQLIKELVT 1437
                         730       740
                  ....*....|....*....|....
gi 488923006  879 NGNTVLVIEHNLDVIKTADHLIDL 902
Cdd:PRK00635 1438 NNNTVIATDRSGSLAEHADHLIHL 1461
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
612-902 7.57e-40

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: 145.16  E-value: 7.57e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 612 IKLKGVQENNLKNIDVDFPLGEFVAVTGVSGSGKSTLVNMVLKRVLAQKLNHNSEKPGKyksvsgikniEKVINIDQspi 691
Cdd:cd03238    1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKARLISFLPKFSR----------NKLIFIDQ--- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 692 grtprsnpatytsvfddirglfaqtneaklrgytkgrfsfnvkggrceackgdgilkiemnflpdvyvpcevchgtryns 771
Cdd:cd03238      --------------------------------------------------------------------------------
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 772 etlevkykgktiadildmtveeatdffapipkiarkLQTIIDVGLGYVHLGQSATTLSGGEAQRMKLASELHKKANGkNF 851
Cdd:cd03238   68 ------------------------------------LQFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPG-TL 110
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488923006 852 YILDEPTTGLHTDDIKRLLDVLQRLVDNGNTVLVIEHNLDVIKTADHLIDL 902
Cdd:cd03238  111 FILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDF 161
UvrA_inter pfam17760
UvrA interaction domain; This domain found in UvrA proteins interacts with the UvrB protein.
132-232 7.85e-35

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


Pssm-ID: 436020 [Multi-domain]  Cd Length: 109  Bit Score: 128.37  E-value: 7.85e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  132 QTVEQMVNRVLDLPERSKVQIISPIVRAKKGQHKKVFEKIKREGFVRVRVDDETMDVEEVPELDKNKVHTIDIVVDRVVV 211
Cdd:pfam17760   1 QTVDQIVDRILALPEGTKIQILAPVVRGRKGEHKELLDDLRKQGFVRVRVDGEIYDLDDEPKLDKNKKHTIEVVVDRLVV 80
                          90       100
                  ....*....|....*....|.
gi 488923006  212 KDGIRSRLFDSFEAALRLSKG 232
Cdd:pfam17760  81 KEDNRSRLADSVETALKLGKG 101
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
401-594 6.06e-22

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 102.60  E-value: 6.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  401 MRELTCQTCHGYRLNRKALSVKIDGKHIAEISALPIDSAMEFFgnlnfseqdtavatPILKEIKDRLNFLRNVGLEYLTL 480
Cdd:PRK00635 1628 LEKRPCPTCSGFRIQPLAQEVVYEGKHFGQLLQTPIEEVAETF--------------PFLKKIQKPLQALIDNGLGYLPL 1693
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  481 SRSARTLSGGEaqriRLATQIGSNL-----SGVLYILDEPSIGLHQRDNNRLISSLKKMRDLGNTLVVVEHDEDTMWAAD 555
Cdd:PRK00635 1694 GQNLSSLSLSE----KIAIKIAKFLylppkHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALLKQAD 1769
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 488923006  556 YLIDIGPGAGENGGEVMAAGTPKQVAKSRKSLTGKYLSG 594
Cdd:PRK00635 1770 YLIEMGPGSGKTGGKILFSGPPKDISASKDSLLKTYMCN 1808
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
6-113 9.62e-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: 89.98  E-value: 9.62e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006   6 IVIHGARAHNLKNIDVTIPRDKLVVVTGLSGSGKSSLAFDTLYAegqrryveslSAYARQFLGQMDKPDVDSIDGL---S 82
Cdd:cd03271    1 LTLKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYP----------ALARRLHLKKEQPGNHDRIEGLehiD 70
                         90       100       110
                 ....*....|....*....|....*....|.
gi 488923006  83 PAISIDQKTTSKNPRSTVGTVTEINDYLRLL 113
Cdd:cd03271   71 KVIVIDQSPIGRTPRSNPATYTGVFDEIREL 101
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
8-70 1.82e-19

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 86.61  E-value: 1.82e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488923006   8 IHGARAHNLKNIDVTIPRDKLVVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQ---FLGQM 70
Cdd:cd03238    3 VSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKARLISFLPKFSRNkliFIDQL 68
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
461-900 5.36e-18

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: 88.42  E-value: 5.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 461 KEIKDR-LNFLRNVGLEYLtLSRSARTLSGGEAQRIRLATQIGSNLSgvLYILDEPSIGL---HQRDNNRLISSLKkmRD 536
Cdd:COG1123  117 AEARARvLELLEAVGLERR-LDRYPHQLSGGQRQRVAIAMALALDPD--LLIADEPTTALdvtTQAEILDLLRELQ--RE 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 537 LGNTLVVVEHD-EDTMWAADYLIDIgpgageNGGEVMAAGTPKQVAKSRKSLTGKYLSGKKFIPVPETRRTGN------- 608
Cdd:COG1123  192 RGTTVLLITHDlGVVAEIADRVVVM------DDGRIVEDGPPEEILAAPQALAAVPRLGAARGRAAPAAAAAEpllevrn 265
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 609 -GQSIKLKGVQENN-LKNIDVDFPLGEFVAVTGVSGSGKSTLVNMVLkrvlaqklnhnsekpGKYKSVSGikniekVINI 686
Cdd:COG1123  266 lSKRYPVRGKGGVRaVDDVSLTLRRGETLGLVGESGSGKSTLARLLL---------------GLLRPTSG------SILF 324
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 687 DQSPIGRTPRSNPATYTS----VFDDirglfaqtneaklrGYTkgrfSFNvkggrceackgdgilkiemnflpdvyvpce 762
Cdd:COG1123  325 DGKDLTKLSRRSLRELRRrvqmVFQD--------------PYS----SLN------------------------------ 356
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 763 vchgtrynsetlevkyKGKTIADIldmtVEEATDFFAPIPK--IARKLQTIID-VGLGYVHLGQSATTLSGGEAQRMKLA 839
Cdd:COG1123  357 ----------------PRMTVGDI----IAEPLRLHGLLSRaeRRERVAELLErVGLPPDLADRYPHELSGGQRQRVAIA 416
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488923006 840 SELhkkANGKNFYILDEPTTGLhtdDIK---RLLDVLQRLVDNGN-TVLVIEHNLDVIKT-ADHLI 900
Cdd:COG1123  417 RAL---ALEPKLLILDEPTSAL---DVSvqaQILNLLRDLQRELGlTYLFISHDLAVVRYiADRVA 476
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
814-902 1.01e-16

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


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 78.56  E-value: 1.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 814 VGLGYVHLGQSATTLSGGEAQRMKLASELHK-KANGKNFYILDEPTTGLHTDDIKRLLDVLQRLVDNGNTVLVIEHNLDV 892
Cdd:cd03227   64 VAAVSAELIFTRLQLSGGEKELSALALILALaSLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPEL 143
                         90
                 ....*....|
gi 488923006 893 IKTADHLIDL 902
Cdd:cd03227  144 AELADKLIHI 153
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
472-562 3.64e-15

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


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 73.93  E-value: 3.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 472 NVGLEYLTLSRSARTLSGGEAQRIRLATQIG--SNLSGVLYILDEPSIGLHQRDNNRLISSLKKMRDLGNTLVVVEHDED 549
Cdd:cd03227   63 IVAAVSAELIFTRLQLSGGEKELSALALILAlaSLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPE 142
                         90
                 ....*....|...
gi 488923006 550 TMWAADYLIDIGP 562
Cdd:cd03227  143 LAELADKLIHIKK 155
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
828-902 6.05e-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: 73.05  E-value: 6.05e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488923006 828 LSGGEAQRMKLASELHKKANgknFYILDEPTTGLHTDDIKRLLDVLQRLVDNGNTVLVIEHNLDVIKTA-DHLIDL 902
Cdd:cd00267   81 LSGGQRQRVALARALLLNPD---LLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAaDRVIVL 153
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
599-902 5.68e-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: 75.95  E-value: 5.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 599 PVPETRR------TGNGQSIKLKGVQ------ENNLKNIDVDFPLGEFVAVTGVSGSGKSTLVNMVLKRVLAQklnhnse 666
Cdd:COG4988  318 PEPAAPAgtaplpAAGPPSIELEDVSfsypggRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPY------- 390
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 667 kpgkyksvSGikniekVINIDQSPIGRTPRsnpatytsvfDDIRGLFAqtneaklrgytkgrfsfnvkggrceackgdgi 746
Cdd:COG4988  391 --------SG------SILINGVDLSDLDP----------ASWRRQIA-------------------------------- 414
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 747 lkiemnflpdvYVPcevchgtryNSETLevkYKGkTIADILDMTVEEATD--------------FFAPIPkiaRKLQTII 812
Cdd:COG4988  415 -----------WVP---------QNPYL---FAG-TIRENLRLGRPDASDeeleaaleaagldeFVAALP---DGLDTPL 467
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 813 dvglgyvhlGQSATTLSGGEAQRMKLASELHKKAngkNFYILDEPTTGLhtdDI---KRLLDVLQRLVDnGNTVLVIEHN 889
Cdd:COG4988  468 ---------GEGGRGLSGGQAQRLALARALLRDA---PLLLLDEPTAHL---DAeteAEILQALRRLAK-GRTVILITHR 531
                        330
                 ....*....|...
gi 488923006 890 LDVIKTADHLIDL 902
Cdd:COG4988  532 LALLAQADRILVL 544
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
622-900 1.64e-13

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: 70.57  E-value: 1.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTLVnmvlkRVLAqklnhnsekpGKYKSVSGikniekVINIDQSPIGRTPRS---- 697
Cdd:cd03225   17 LDDISLTIKKGEFVLIVGPNGSGKSTLL-----RLLN----------GLLGPTSG------EVLVDGKDLTKLSLKelrr 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 698 -------NPAT---YTSVFDDIrglfaqtneaklrgytkgrfSFnvkggrceACKGDGILKIEMNflpdvyvpcevchgt 767
Cdd:cd03225   76 kvglvfqNPDDqffGPTVEEEV--------------------AF--------GLENLGLPEEEIE--------------- 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 768 rynsetlevkykgKTIADILDMtveeatdffapipkiarklqtiidVGLgYVHLGQSATTLSGGEAQRMKLASELhkkAN 847
Cdd:cd03225  113 -------------ERVEEALEL------------------------VGL-EGLRDRSPFTLSGGQKQRVAIAGVL---AM 151
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488923006 848 GKNFYILDEPTTGLHTDDIKRLLDVLQRLVDNGNTVLVIEHNLDVIKT-ADHLI 900
Cdd:cd03225  152 DPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLElADRVI 205
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
487-563 1.70e-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: 69.20  E-value: 1.70e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488923006 487 LSGGEAQRIRLATQIGSNLSgvLYILDEPSIGLHQRDNNRLISSLKKMRDLGNTLVVVEHD-EDTMWAADYLIDIGPG 563
Cdd:cd00267   81 LSGGQRQRVALARALLLNPD--LLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDpELAELAADRVIVLKDG 156
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
788-900 1.21e-12

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 68.55  E-value: 1.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 788 DMTVEEATDFFA-----PIPKIARKLQTIID-VGLGyVHLGQSATTLSGGEAQRMKLASELhkkANGKNFYILDEPTTGL 861
Cdd:COG1131   87 DLTVRENLRFFArlyglPRKEARERIDELLElFGLT-DAADRKVGTLSGGMKQRLGLALAL---LHDPELLILDEPTSGL 162
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 488923006 862 htdD---IKRLLDVLQRLVDNGNTVLVIEHNLDVI-KTADHLI 900
Cdd:COG1131  163 ---DpeaRRELWELLRELAAEGKTVLLSTHYLEEAeRLCDRVA 202
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
461-558 6.67e-12

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: 65.95  E-value: 6.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 461 KEIKDRLNF-LRNVGLEYLtLSRSARTLSGGEAQRIRLATQIGSNLSgvLYILDEPSIGLHQRDNNRLISSLKKMRDLGN 539
Cdd:cd03225  109 EEIEERVEEaLELVGLEGL-RDRSPFTLSGGQKQRVAIAGVLAMDPD--ILLLDEPTAGLDPAGRRELLELLKKLKAEGK 185
                         90       100
                 ....*....|....*....|
gi 488923006 540 TLVVVEHDEDTMWA-ADYLI 558
Cdd:cd03225  186 TIIIVTHDLDLLLElADRVI 205
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
622-900 9.02e-12

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: 65.63  E-value: 9.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTLvnmvLKRVLAQklnhnsekpgkyksvsgIKNIEKVINIDQSPIGRTPrsnpat 701
Cdd:cd03235   15 LEDVSFEVKPGEFLAIVGPNGAGKSTL----LKAILGL-----------------LKPTSGSIRVFGKPLEKER------ 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 702 ytsvfddirglfaqtneaKLRGYTKGRFSFNVkggrceackgdgilkiemNFLPDVYvpcEVCHGTRYNSETLEVKYKGK 781
Cdd:cd03235   68 ------------------KRIGYVPQRRSIDR------------------DFPISVR---DVVLMGLYGHKGLFRRLSKA 108
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 782 TIADildmtVEEATDFfapipkiarklqtiidVGL-GYVHlgQSATTLSGGEAQRMKLASELHKKANgknFYILDEPTTG 860
Cdd:cd03235  109 DKAK-----VDEALER----------------VGLsELAD--RQIGELSGGQQQRVLLARALVQDPD---LLLLDEPFAG 162
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 488923006 861 LHTDDIKRLLDVLQRLVDNGNTVLVIEHNLD-VIKTADHLI 900
Cdd:cd03235  163 VDPKTQEDIYELLRELRREGMTILVVTHDLGlVLEYFDRVL 203
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
443-580 9.68e-12

Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];


Pssm-ID: 440739 [Multi-domain]  Cd Length: 230  Bit Score: 65.82  E-value: 9.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 443 FG--NLNFSEqdtavatpilKEIKDRLN-FLRNVGLEYLtLSRSARTLSGGEAQRIRLAtqigsnlsGVL------YILD 513
Cdd:COG1122   99 FGpeNLGLPR----------EEIRERVEeALELVGLEHL-ADRPPHELSGGQKQRVAIA--------GVLamepevLVLD 159
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488923006 514 EPSIGLHQRDNNRLISSLKKMRDLGNTLVVVEHD-EDTMWAADYLIDIgpgageNGGEVMAAGTPKQV 580
Cdd:COG1122  160 EPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDlDLVAELADRVIVL------DDGRIVADGTPREV 221
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
622-902 3.10e-11

ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444011 [Multi-domain]  Cd Length: 569  Bit Score: 67.10  E-value: 3.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTLVNMVLkrvlaqklnhnsekpGKYKSVSGikniekVINIDQSPIgrtprsnpat 701
Cdd:COG4987  351 LDGLSLTLPPGERVAIVGPSGSGKSTLLALLL---------------RFLDPQSG------SITLGGVDL---------- 399
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 702 ytsvfddirglfAQTNEAKLRGYtkgrfsfnvkggrceackgdgilkieMNFLP-DVYVpcevchgtrYNSetlevkykg 780
Cdd:COG4987  400 ------------RDLDEDDLRRR--------------------------IAVVPqRPHL---------FDT--------- 423
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 781 kTIADILDMTVEEATDffapipkiARKLQTIIDVGLGYV----------HLGQSATTLSGGEAQRMKLASELHKKAngkN 850
Cdd:COG4987  424 -TLRENLRLARPDATD--------EELWAALERVGLGDWlaalpdgldtWLGEGGRRLSGGERRRLALARALLRDA---P 491
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488923006 851 FYILDEPTTGLHTDDIKRLLDVLQRLVDnGNTVLVIEHNLDVIKTADHLIDL 902
Cdd:COG4987  492 ILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLAGLERMDRILVL 542
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
622-900 3.34e-11

Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];


Pssm-ID: 440739 [Multi-domain]  Cd Length: 230  Bit Score: 64.28  E-value: 3.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTLVNMvlkrvlaqkLNhnsekpGKYKSVSGikniekVINIDQSPIGRTPRS---- 697
Cdd:COG1122   17 LDDVSLSIEKGEFVAIIGPNGSGKSTLLRL---------LN------GLLKPTSG------EVLVDGKDITKKNLRelrr 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 698 -------NPATY---TSVFDDIrgLFAQTNeaklRGYTKGrfsfnvkggrceackgdgilkiemnflpdvyvpcevchgt 767
Cdd:COG1122   76 kvglvfqNPDDQlfaPTVEEDV--AFGPEN----LGLPRE---------------------------------------- 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 768 rynsetlEVKykgKTIADILDMtveeatdffapipkiarklqtiidVGLgYVHLGQSATTLSGGEAQRMKLASELhkkAN 847
Cdd:COG1122  110 -------EIR---ERVEEALEL------------------------VGL-EHLADRPPHELSGGQKQRVAIAGVL---AM 151
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488923006 848 GKNFYILDEPTTGLHTDDIKRLLDVLQRLVDNGNTVLVIEHNLD-VIKTADHLI 900
Cdd:COG1122  152 EPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDlVAELADRVI 205
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
812-900 4.18e-11

First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.


Pssm-ID: 213183 [Multi-domain]  Cd Length: 163  Bit Score: 62.45  E-value: 4.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 812 IDVGLGYVHlgQsattLSGGEAQRMKLASELHKKANgknFYILDEPTTGLHTDDIKRLLDVLQRLVDNGNTVLVIEHNLD 891
Cdd:cd03216   73 RRAGIAMVY--Q----LSVGERQMVEIARALARNAR---LLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLD 143
                         90
                 ....*....|
gi 488923006 892 -VIKTADHLI 900
Cdd:cd03216  144 eVFEIADRVT 153
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
775-900 1.04e-10

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: 61.68  E-value: 1.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 775 EVKYKGKTIADIldmtveeatdffaPIPKIARKL----QTIIDVGLGyvHL-GQSATTLSGGEAQRMKLASELHKKAngk 849
Cdd:cd03214   55 EILLDGKDLASL-------------SPKELARKIayvpQALELLGLA--HLaDRPFNELSGGERQRVLLARALAQEP--- 116
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488923006 850 NFYILDEPTTGLhtdDIK---RLLDVLQRLVD-NGNTVLVIEHNLD-VIKTADHLI 900
Cdd:cd03214  117 PILLLDEPTSHL---DIAhqiELLELLRRLAReRGKTVVMVLHDLNlAARYADRVI 169
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
622-900 2.21e-10

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 62.03  E-value: 2.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTLVNMVLkrvlaqklnhnsekpGKYKSVSGikniekVINIDQSPIGRTPR----- 696
Cdd:COG1121   22 LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAIL---------------GLLPPTSG------TVRLFGKPPRRARRrigyv 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 697 -----SNPATYTSVFDDIR-GLFAQTneaklrgytkgrfsfnvkggrceackgdGILKiemnflpdvyvpcevchgtRYN 770
Cdd:COG1121   81 pqraeVDWDFPITVRDVVLmGRYGRR----------------------------GLFR-------------------RPS 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 771 SETLEVkykgktIADILDMTveEATDFfapipkiARKlqtiidvglgyvHLGQsattLSGGEAQRMKLASELhkkANGKN 850
Cdd:COG1121  114 RADREA------VDEALERV--GLEDL-------ADR------------PIGE----LSGGQQQRVLLARAL---AQDPD 159
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488923006 851 FYILDEPTTGLhtdDIK---RLLDVLQRLVDNGNTVLVIEHNLD-VIKTADHLI 900
Cdd:COG1121  160 LLLLDEPFAGV---DAAteeALYELLRELRREGKTILVVTHDLGaVREYFDRVL 210
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
789-900 2.86e-10

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: 61.08  E-value: 2.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 789 MTVEEATDFFAPIPKIARKlqtIIDVGLGYVHLGQSA----TTLSGGEAQRMKLASELhkkANGKNFYILDEPTTGLHTD 864
Cdd:cd03268   87 LTARENLRLLARLLGIRKK---RIDEVLDVVGLKDSAkkkvKGFSLGMKQRLGIALAL---LGNPDLLILDEPTNGLDPD 160
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 488923006 865 DIKRLLDVLQRLVDNGNTVLVIEHNL-DVIKTADHLI 900
Cdd:cd03268  161 GIKELRELILSLRDQGITVLISSHLLsEIQKVADRIG 197
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
593-902 2.89e-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: 2.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 593 SGKKFIPVPETRrtgngQSIKLKGV-------QENNLKNIDVDFPLGEFVAVTGVSGSGKSTLVNMVLkrvlaqklnhns 665
Cdd:COG2274  460 EGRSKLSLPRLK-----GDIELENVsfrypgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLL------------ 522
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 666 ekpGKYKSVSGikniekVINIDQSPIgrtpRS-NPATYTS----VFDDIRgLFAQTneakLRgytkgrfsFNVKGGRCEA 740
Cdd:COG2274  523 ---GLYEPTSG------RILIDGIDL----RQiDPASLRRqigvVLQDVF-LFSGT----IR--------ENITLGDPDA 576
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 741 ckgdgilkiemnflpdvyvpcevchgtrynseTLEvkykgkTIADILDMTveEATDFfapIPKIARKLQTIIdvglgyvh 820
Cdd:COG2274  577 --------------------------------TDE------EIIEAARLA--GLHDF---IEALPMGYDTVV-------- 605
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 821 lGQSATTLSGGEAQRMKLASELHKKAngkNFYILDEPTTGLhtDDI--KRLLDVLQRLvDNGNTVLVIEHNLDVIKTADH 898
Cdd:COG2274  606 -GEGGSNLSGGQRQRLAIARALLRNP---RILILDEATSAL--DAEteAIILENLRRL-LKGRTVIIIAHRLSTIRLADR 678

                 ....
gi 488923006 899 LIDL 902
Cdd:COG2274  679 IIVL 682
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
622-902 6.27e-10

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: 60.20  E-value: 6.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTLVNMVLKRvlaqklnhnsEKP--GKY----KSVSGIKNIEKvinidqspigrtp 695
Cdd:cd03255   20 LKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGL----------DRPtsGEVrvdgTDISKLSEKEL------------- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 696 rsnpatytsvfddirglfaqtneAKLRGYTKGrFSFNvkggrceackgdgilkiEMNFLPDvyvpcevchgtrynsetle 775
Cdd:cd03255   77 -----------------------AAFRRRHIG-FVFQ-----------------SFNLLPD------------------- 96
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 776 vkykgktiadildMTVEE---ATDFFAPIPKIARKLQtIIDVgLGYVHLGQSAT----TLSGGEAQRMKLASELhkkANG 848
Cdd:cd03255   97 -------------LTALEnveLPLLLAGVPKKERRER-AEEL-LERVGLGDRLNhypsELSGGQQQRVAIARAL---AND 158
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488923006 849 KNFYILDEPTTGLHTDDIKRLLDVLQRLVDN-GNTVLVIEHNLDVIKTADHLIDL 902
Cdd:cd03255  159 PKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEYADRIIEL 213
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
827-902 6.85e-10

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: 59.96  E-value: 6.85e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488923006 827 TLSGGEAQRMKLASELhkkANGKNFYILDEPTTGLHTDDIKRLLDVLQRLVDNGNTVLVIEHNLDVI-KTADHLIDL 902
Cdd:cd03226  126 SLSGGQKQRLAIAAAL---LSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLaKVCDRVLLL 199
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
814-900 9.57e-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: 59.76  E-value: 9.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 814 VGLGYvHLGQSATTLSGGEAQRMKLASELhkkANGKNFYILDEPTTGLHTDDIKRLLDVLQRLVDNGNTVLVIEHNLDVI 893
Cdd:cd03219  131 VGLAD-LADRPAGELSYGQQRRLEIARAL---ATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVV 206

                 ....*...
gi 488923006 894 KT-ADHLI 900
Cdd:cd03219  207 MSlADRVT 214
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
622-902 1.02e-09

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 59.44  E-value: 1.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTLVnmvlkRVLAQkLNHNSEkpGKyksvsgikniekvINIDQSPIGRTPrsnPAT 701
Cdd:COG4619   16 LSPVSLTLEAGECVAITGPSGSGKSTLL-----RALAD-LDPPTS--GE-------------IYLDGKPLSAMP---PPE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 702 YtsvfddirglfaqtneaklrgytkgrfsfnvkggRCEACkgdgilkiemnflpdvYVPCEvchgtrynsetlevkykgk 781
Cdd:COG4619   72 W----------------------------------RRQVA----------------YVPQE------------------- 82
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 782 tiADILDMTVEEATDFFAPIPKIARKLQTIID----VGLGYVHLGQSATTLSGGEAQRMKLASELhkkANGKNFYILDEP 857
Cdd:COG4619   83 --PALWGGTVRDNLPFPFQLRERKFDRERALEllerLGLPPDILDKPVERLSGGERQRLALIRAL---LLQPDVLLLDEP 157
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 488923006 858 TTGLHTDDIKRLLDVLQRLVDNGN-TVLVIEHNLDVIKT-ADHLIDL 902
Cdd:COG4619  158 TSALDPENTRRVEELLREYLAEEGrAVLWVSHDPEQIERvADRVLTL 204
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
461-586 1.18e-09

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: 59.66  E-value: 1.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 461 KEIKDR-LNFLRNVGLEYLtLSRSARTLSGGEAQRIRLATQIGSNLSgvLYILDEPSIGLHQRDNNRLISSLKKMRDLGN 539
Cdd:cd03299  104 KEIERKvLEIAEMLGIDHL-LNRKPETLSGGEQQRVAIARALVVNPK--ILLLDEPFSALDVRTKEKLREELKKIRKEFG 180
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 488923006 540 TLVV-VEHD-EDTMWAADYLIDIgpgageNGGEVMAAGTPKQVAKSRKS 586
Cdd:cd03299  181 VTVLhVTHDfEEAWALADKVAIM------LNGKLIQVGKPEEVFKKPKN 223
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
622-902 1.58e-09

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 58.40  E-value: 1.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTLVNMvlkrvlaqklnhnsekpgkyksvsgikniekvinidqspigrtprsnpat 701
Cdd:NF040873   8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKV-------------------------------------------------- 37
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 702 ytsvfddIRGLFAQTneaklrgytkgrfsfnvkGGRCEACKGDGIlkiemnflpdVYVPcevchgtrYNSEtlevkykgk 781
Cdd:NF040873  38 -------LAGVLRPT------------------SGTVRRAGGARV----------AYVP--------QRSE--------- 65
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 782 tIADILDMTVEEATD--FFA---PIPKIARKLQTIIDVGLGYVHL----GQSATTLSGGEAQRMKLASELHKKAngkNFY 852
Cdd:NF040873  66 -VPDSLPLTVRDLVAmgRWArrgLWRRLTRDDRAAVDDALERVGLadlaGRQLGELSGGQRQRALLAQGLAQEA---DLL 141
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 488923006 853 ILDEPTTGLHTDDIKRLLDVLQRLVDNGNTVLVIEHNLDVIKTADHLIDL 902
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
821-890 2.71e-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: 60.95  E-value: 2.71e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488923006 821 LGQSATTLSGGEAQRMKLASELHKKAngkNFYILDEPTTGLhtdDIK---RLLDVLQRLVDNGNTVLVIEHNL 890
Cdd:COG1245  206 LDRDISELSGGELQRVAIAAALLRDA---DFYFFDEPSSYL---DIYqrlNVARLIRELAEEGKYVLVVEHDL 272
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
821-902 3.25e-09

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: 60.38  E-value: 3.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  821 LGQSATTLSGGEAQRMKLASELhkkANGKNFYILDEPTTGLHTDDIKRLLDVLQRLVdNGNTVLVIEHNLDVIKTADHLI 900
Cdd:TIGR02857 452 IGEGGAGLSGGQAQRLALARAF---LRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALAALADRIV 527

                  ..
gi 488923006  901 DL 902
Cdd:TIGR02857 528 VL 529
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
459-893 3.62e-09

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 60.59  E-value: 3.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 459 ILKEIKDRLNfLRNVgleyltLSRSARTLSGGEAQRIRLATQIGSNlsGVLYILDEPS----IGlhQRDN-NRLISSLKK 533
Cdd:PRK13409 192 KLDEVVERLG-LENI------LDRDISELSGGELQRVAIAAALLRD--ADFYFFDEPTsyldIR--QRLNvARLIRELAE 260
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 534 mrdlGNTLVVVEHDEDTMwaaDYLID-IGPGAGENGgevmAAGTpkqVAKSRKSLTG--KYLSGkkFIP----------- 599
Cdd:PRK13409 261 ----GKYVLVVEHDLAVL---DYLADnVHIAYGEPG----AYGV---VSKPKGVRVGinEYLKG--YLPeenmrirpepi 324
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 600 ---VPETRRTGNGQSIklkgVQENNL-KNIDvDFPL---------GEFVAVTGVSGSGKSTLVnmvlkRVLAqklnhNSE 666
Cdd:PRK13409 325 efeERPPRDESERETL----VEYPDLtKKLG-DFSLeveggeiyeGEVIGIVGPNGIGKTTFA-----KLLA-----GVL 389
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 667 KPgkyksvsgikniekvinidqspigrtprsnpatytsvfddirglfaqtneaklrgyTKGRFSFNVKggrceackgdgi 746
Cdd:PRK13409 390 KP--------------------------------------------------------DEGEVDPELK------------ 401
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 747 lkiemnflpdvyvpcevchgtrynsetleVKYKGKTIADILDMTVEE----ATDFFAP---IPKIARKLQtIIDVglgyv 819
Cdd:PRK13409 402 -----------------------------ISYKPQYIKPDYDGTVEDllrsITDDLGSsyyKSEIIKPLQ-LERL----- 446
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 820 hLGQSATTLSGGEAQRMKLASELHKKAngkNFYILDEPTTglHtddikrlLDVLQRLV----------DNGNTVLVIEHN 889
Cdd:PRK13409 447 -LDKNVKDLSGGELQRVAIAACLSRDA---DLYLLDEPSA--H-------LDVEQRLAvakairriaeEREATALVVDHD 513

                 ....
gi 488923006 890 LDVI 893
Cdd:PRK13409 514 IYMI 517
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
622-900 3.72e-09

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: 58.52  E-value: 3.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTLVnmvlkRVLAqklnhnsekpGKYKSVSGikniekVINIDQSPIGRTPRSNPAT 701
Cdd:COG1120   17 LDDVSLSLPPGEVTALLGPNGSGKSTLL-----RALA----------GLLKPSSG------EVLLDGRDLASLSRRELAR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 702 ytsvfddIRGLFAQTNEAklrgytkgRFSFNVKggrcEAckgdgilkIEMNFLPdvyvpcevcHGTRYNSETLEvkykgk 781
Cdd:COG1120   76 -------RIAYVPQEPPA--------PFGLTVR----EL--------VALGRYP---------HLGLFGRPSAE------ 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 782 tiadilDMT-VEEAtdffapipkiarklqtIIDVGLGyvHL-GQSATTLSGGEAQRMKLASELhkkANGKNFYILDEPTT 859
Cdd:COG1120  114 ------DREaVEEA----------------LERTGLE--HLaDRPVDELSGGERQRVLIARAL---AQEPPLLLLDEPTS 166
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 488923006 860 GLhtdDIK---RLLDVLQRLV-DNGNTVLVIEHNLD-VIKTADHLI 900
Cdd:COG1120  167 HL---DLAhqlEVLELLRRLArERGRTVVMVLHDLNlAARYADRLV 209
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
776-900 5.71e-09

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


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 57.80  E-value: 5.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 776 VKYKGKTIADILDMTVE----EATDFFAPIP----KIARKLQtIIDVglgyvhLGQSATTLSGGEAQRMKLASELHKKAn 847
Cdd:cd03237   63 VSYKPQYIKADYEGTVRdllsSITKDFYTHPyfktEIAKPLQ-IEQI------LDREVPELSGGELQRVAIAACLSKDA- 134
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488923006 848 gkNFYILDEPTTglHTDDIKRLL--DVLQRLVDNGN-TVLVIEHNLDVIK-TADHLI 900
Cdd:cd03237  135 --DIYLLDEPSA--YLDVEQRLMasKVIRRFAENNEkTAFVVEHDIIMIDyLADRLI 187
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
803-891 6.11e-09

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 58.56  E-value: 6.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 803 KIARKLQTIidVGLGYVHLGQSATTLSGGEAQRMKLASELhkkANGKNFYILDEPTTGLHTDDIKRLLDVLQRLVDNGNT 882
Cdd:PRK13651 143 KRAAKYIEL--VGLDESYLQRSPFELSGGQKRRVALAGIL---AMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKT 217

                 ....*....
gi 488923006 883 VLVIEHNLD 891
Cdd:PRK13651 218 IILVTHDLD 226
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
430-547 8.48e-09

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: 56.77  E-value: 8.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 430 EISALPIDSAMEFFGNLnfSEQDTAVATPILKEikdrlnflrnVGLEYLtLSRSARTLSGGEAQRIRLATQIGSNLSgvL 509
Cdd:cd03235   89 DVVLMGLYGHKGLFRRL--SKADKAKVDEALER----------VGLSEL-ADRQIGELSGGQQQRVLLARALVQDPD--L 153
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 488923006 510 YILDEPSIGL---HQRDnnrLISSLKKMRDLGNTLVVVEHD 547
Cdd:cd03235  154 LLLDEPFAGVdpkTQED---IYELLRELRREGMTILVVTHD 191
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
821-902 1.17e-08

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 58.67  E-value: 1.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 821 LGQSATTLSGGEAQRMKLASELHKKAngkNFYILDEPTTGLhtdDIK---RLLDVLQRLVDNgNTVLVIEHNLDVIktaD 897
Cdd:PRK13409 206 LDRDISELSGGELQRVAIAAALLRDA---DFYFFDEPTSYL---DIRqrlNVARLIRELAEG-KYVLVVEHDLAVL---D 275

                 ....*
gi 488923006 898 HLIDL 902
Cdd:PRK13409 276 YLADN 280
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
828-901 1.33e-08

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


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 56.99  E-value: 1.33e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488923006 828 LSGGEAQRMKLASELHKKANgknFYILDEPTTGLhtdDIKRLLD---VLQRLVDNGNTVLVIEHNLDVIktaDHLID 901
Cdd:cd03236  140 LSGGELQRVAIAAALARDAD---FYFFDEPSSYL---DIKQRLNaarLIRELAEDDNYVLVVEHDLAVL---DYLSD 207
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
828-900 1.34e-08

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: 55.10  E-value: 1.34e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488923006 828 LSGGEAQRMKLASELhkkANGKNFYILDEPTTGLHTDDIKRLLDVLQRLVDNGNTVLVIEHNLDVI-KTADHLI 900
Cdd:cd03230   96 LSGGMKQRLALAQAL---LHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAeRLCDRVA 166
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
443-603 2.11e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 56.57  E-value: 2.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 443 FGNLNF--SEQDT-AVATPILKEikdrlnflrnVGLEYLTLSRSARTLSGGEAQRIRLAtqigsnlsGVL------YILD 513
Cdd:PRK13634 109 FGPMNFgvSEEDAkQKAREMIEL----------VGLPEELLARSPFELSGGQMRRVAIA--------GVLamepevLVLD 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 514 EPSIGLHQRDNNRLI---SSLKKMRDLgnTLVVVEHD-EDTMWAADYLIDIgpgageNGGEVMAAGTPKQVAKSRKSLTG 589
Cdd:PRK13634 171 EPTAGLDPKGRKEMMemfYKLHKEKGL--TTVLVTHSmEDAARYADQIVVM------HKGTVFLQGTPREIFADPDELEA 242
                        170
                 ....*....|....
gi 488923006 590 KYLSgkkfipVPET 603
Cdd:PRK13634 243 IGLD------LPET 250
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
823-892 2.24e-08

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 57.54  E-value: 2.24e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 823 QSATTLSGGEAQRMKLASELhkkANGKNFYILDEPTTGLHTDDIKRLLDVLQRLVDNGNTVLVIEHNLDV 892
Cdd:PRK09536 135 RPVTSLSGGERQRVLLARAL---AQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDL 201
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
622-943 2.79e-08

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: 57.61  E-value: 2.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTLVnmvlkRVLAQKLNHNSEKPGKyksvsgikniekvINIDQSPIGRTPrsnpat 701
Cdd:COG1123   22 VDGVSLTIAPGETVALVGESGSGKSTLA-----LALMGLLPHGGRISGE-------------VLLDGRDLLELS------ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 702 ytsvfDDIRGlfaqtneaKLRGYtkgrfsfnvkggrceackgdgILKIEMNFLPDVYVPCEVChgtrynsETLEvkykgk 781
Cdd:COG1123   78 -----EALRG--------RRIGM---------------------VFQDPMTQLNPVTVGDQIA-------EALE------ 110
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 782 tiadILDMTVEEAtdffapipkIARKLQTIIDVGLGyVHLGQSATTLSGGEAQRMKLASELhkkANGKNFYILDEPTTGL 861
Cdd:COG1123  111 ----NLGLSRAEA---------RARVLELLEAVGLE-RRLDRYPHQLSGGQRQRVAIAMAL---ALDPDLLIADEPTTAL 173
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 862 HTDDIKRLLDVLQRLV-DNGNTVLVIEHNLDVI-KTADHLIDLGP-EGGAGGGQVVAVGTPEAIAAVPESYTGKYLKEVL 938
Cdd:COG1123  174 DVTTQAEILDLLRELQrERGTTVLLITHDLGVVaEIADRVVVMDDgRIVEDGPPEEILAAPQALAAVPRLGAARGRAAPA 253

                 ....*
gi 488923006 939 ERAQE 943
Cdd:COG1123  254 AAAAE 258
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
828-902 3.11e-08

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: 54.14  E-value: 3.11e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488923006 828 LSGGEAQRMKLASELHKKangKNFYILDEPTTGLHTDDIKRLLDVLQRLVDNGNTVLVIEHNLDVIKTADHLIDL 902
Cdd:cd03246   97 LSGGQRQRLGLARALYGN---PRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVL 168
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
622-902 3.15e-08

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 55.43  E-value: 3.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTLVNMV--LkrvlaqklnhnsEKP--GKYKsvsgikniekvinIDQSPIGRTPRs 697
Cdd:COG1136   24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLNILggL------------DRPtsGEVL-------------IDGQDISSLSE- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 698 npatytsvfddiRGLfaqtneAKLRGYTKGrF---SFNVkggrceackgdgilkiemnfLPD------VYVPCEvchgtr 768
Cdd:COG1136   78 ------------REL------ARLRRRHIG-FvfqFFNL--------------------LPEltalenVALPLL------ 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 769 ynsetlevkYKGKTIADildmtveeatdffapIPKIARKLqtIIDVGLGYvHLGQSATTLSGGEAQRMKLASELhkkANG 848
Cdd:COG1136  113 ---------LAGVSRKE---------------RRERAREL--LERVGLGD-RLDHRPSQLSGGQQQRVAIARAL---VNR 162
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488923006 849 KNFYILDEPTTGLHTDDIKRLLDVLQRLVDN-GNTVLVIEHNLDVIKTADHLIDL 902
Cdd:COG1136  163 PKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAARADRVIRL 217
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
480-580 3.24e-08

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 55.71  E-value: 3.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 480 LSRSARTLSGGEAQRIRLAT---QI--GSNLSGVLYILDEPSIGLHQRDNNRLISSLKKMRDLGNTLVVVEHD-EDTMWA 553
Cdd:PRK03695 120 LGRSVNQLSGGEWQRVRLAAvvlQVwpDINPAGQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDlNHTLRH 199
                         90       100
                 ....*....|....*....|....*....
gi 488923006 554 AD--YLIdigpgageNGGEVMAAGTPKQV 580
Cdd:PRK03695 200 ADrvWLL--------KQGKLLASGRRDEV 220
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
828-902 4.06e-08

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: 53.93  E-value: 4.06e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488923006 828 LSGGEAQRMKLASELHKKAngkNFYILDEPTTGLHTDDIKRLLDVLQRLvDNGNTVLVIEHNLDVIKTADHLIDL 902
Cdd:cd03228   97 LSGGQRQRIAIARALLRDP---PILILDEATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTIRDADRIIVL 167
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
622-890 7.57e-08

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: 56.21  E-value: 7.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  622 LKNIDVDFPLGEFVAVTGVSGSGKSTLVnMVLKRVLaqklnhnSEKPGKYkSVSGIknieKVINIDQSPIGRTprsnpat 701
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLL-ATLAGLL-------DPLQGEV-TLDGV----PVSSLDQDEVRRR------- 410
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  702 yTSVFDDIRGLFAQTneakLRGytkgrfsfNVKGGRceackgdgilkiemnflPDVyvpcevchgtrynsetlevkykgk 781
Cdd:TIGR02868 411 -VSVCAQDAHLFDTT----VRE--------NLRLAR-----------------PDA------------------------ 436
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  782 tiadildmTVEEATDFFAPIpKIARKLQTIIDvGLGYVhLGQSATTLSGGEAQRMKLASELHKKAngkNFYILDEPTTGL 861
Cdd:TIGR02868 437 --------TDEELWAALERV-GLADWLRALPD-GLDTV-LGEGGARLSGGERQRLALARALLADA---PILLLDEPTEHL 502
                         250       260
                  ....*....|....*....|....*....
gi 488923006  862 HTDDIKRLLDVLqRLVDNGNTVLVIEHNL 890
Cdd:TIGR02868 503 DAETADELLEDL-LAALSGRTVVLITHHL 530
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
487-580 1.64e-07

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 53.48  E-value: 1.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 487 LSGGEAQRIRLATQIGSNLSGVLyiLDEPSIGL---HQRDnnrLISSLKKMRDLGNTLVVVEHD--EDTMWaADYLIDIg 561
Cdd:PRK11231 139 LSGGQRQRAFLAMVLAQDTPVVL--LDEPTTYLdinHQVE---LMRLMRELNTQGKTVVTVLHDlnQASRY-CDHLVVL- 211
                         90
                 ....*....|....*....
gi 488923006 562 pgageNGGEVMAAGTPKQV 580
Cdd:PRK11231 212 -----ANGHVMAQGTPEEV 225
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
794-900 1.66e-07

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 55.02  E-value: 1.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 794 ATDFfapIPKIARKLQTIIdvglgyvhlGQSATTLSGGEAQRMKLASELHKKANgknFYILDEPTTGLHTDD---IKRLL 870
Cdd:PRK11176 459 AMDF---INKMDNGLDTVI---------GENGVLLSGGQRQRIAIARALLRDSP---ILILDEATSALDTESeraIQAAL 523
                         90       100       110
                 ....*....|....*....|....*....|
gi 488923006 871 DVLQRlvdnGNTVLVIEHNLDVIKTADHLI 900
Cdd:PRK11176 524 DELQK----NRTSLVIAHRLSTIEKADEIL 549
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
788-902 2.15e-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: 52.48  E-value: 2.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 788 DMTVEEATDFFAPIPKIARKLQTIID----VGLGYvHLGQSATTLSGGEAQRMKLASELHKKANgknFYILDEPTTGLHT 863
Cdd:COG4133   89 ELTVRENLRFWAALYGLRADREAIDEaleaVGLAG-LADLPVRQLSAGQKRRVALARLLLSPAP---LWLLDEPFTALDA 164
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 488923006 864 DDIKRLLDVLQRLVDNGNTVLVIEHNLDVIkTADHLIDL 902
Cdd:COG4133  165 AGVALLAELIAAHLARGGAVLLTTHQPLEL-AAARVLDL 202
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
470-575 2.44e-07

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: 51.67  E-value: 2.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 470 LRNVGLEYLtLSRSARTLSGGEAQRIRLA------TQIgsnlsgvlYILDEPSIGL---HQrdnNRLISSLKKM-RDLGN 539
Cdd:cd03214   82 LELLGLAHL-ADRPFNELSGGERQRVLLAralaqePPI--------LLLDEPTSHLdiaHQ---IELLELLRRLaRERGK 149
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 488923006 540 TLVVVEHDEDtmWA---ADYLIDIgpgageNGGEVMAAG 575
Cdd:cd03214  150 TVVMVLHDLN--LAaryADRVILL------KDGRIVAQG 180
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
803-902 2.46e-07

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 53.09  E-value: 2.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 803 KIARKLQTIIDVGLGYVHLGQSA----TTLSGGEAQRMKLASELhkkANGKNFYILDEPTTGLhtdDIKR---LLDVLQR 875
Cdd:PRK11231 110 RLSAEDNARVNQAMEQTRINHLAdrrlTDLSGGQRQRAFLAMVL---AQDTPVVLLDEPTTYL---DINHqveLMRLMRE 183
                         90       100
                 ....*....|....*....|....*...
gi 488923006 876 LVDNGNTVLVIEHNLD-VIKTADHLIDL 902
Cdd:PRK11231 184 LNTQGKTVVTVLHDLNqASRYCDHLVVL 211
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
470-585 2.79e-07

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: 52.44  E-value: 2.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 470 LRNVGLEYLtLSRSARTLSGGEAQRIRLATQIGSNLSgvLYILDEPSIGLHQRDNNRLISSLKKMRDLGNTLVVVEHDED 549
Cdd:cd03219  128 LERVGLADL-ADRPAGELSYGQQRRLEIARALATDPK--LLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMD 204
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 488923006 550 T-MWAADYLIDIgpgageNGGEVMAAGTPKQVAKSRK 585
Cdd:cd03219  205 VvMSLADRVTVL------DQGRVIAEGTPDEVRNNPR 235
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
828-900 2.86e-07

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: 52.51  E-value: 2.86e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488923006 828 LSGGEAQRMKLASELhkkANGKNFYILDEPTTGLhtdDIK---RLLDVLQRLVD-NGNTVLVIEHNLDVIK-TADHLI 900
Cdd:cd03257  146 LSGGQRQRVAIARAL---ALNPKLLIADEPTSAL---DVSvqaQILDLLKKLQEeLGLTLLFITHDLGVVAkIADRVA 217
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
459-893 3.26e-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: 54.02  E-value: 3.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 459 ILKEIKDRLNfLRNVgleyltLSRSARTLSGGEAQRIRLATQIGSNlsGVLYILDEPSIGL--HQRDN-NRLISSLKKMr 535
Cdd:COG1245  192 KLDELAEKLG-LENI------LDRDISELSGGELQRVAIAAALLRD--ADFYFFDEPSSYLdiYQRLNvARLIRELAEE- 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 536 dlGNTLVVVEHDedtMWAADYLID-IGPGAGENGgevmAAGTpkqVAKSRKSLTG--KYLSGkkFIP------------- 599
Cdd:COG1245  262 --GKYVLVVEHD---LAILDYLADyVHILYGEPG----VYGV---VSKPKSVRVGinQYLDG--YLPeenvrirdepief 327
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 600 -VPETRRTGNGQSIklkgVQENNL-KNIDvDFPL---------GEFVAVTGVSGSGKSTLVnmvlkRVLAqklnhnsekp 668
Cdd:COG1245  328 eVHAPRREKEEETL----VEYPDLtKSYG-GFSLeveggeireGEVLGIVGPNGIGKTTFA-----KILA---------- 387
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 669 GKYKSVSGikNIEKVINIDQSPigrtprsnpaTYtsvfddIRGLFAQTNEAKLRGYTKGRFSfnvkggrceackgdgilk 748
Cdd:COG1245  388 GVLKPDEG--EVDEDLKISYKP----------QY------ISPDYDGTVEEFLRSANTDDFG------------------ 431
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 749 iemnflpdvyvpcevchGTRYNSEtlevkykgktiadildmtveeatdffapipkIARKLqtiidvGLGYVhLGQSATTL 828
Cdd:COG1245  432 -----------------SSYYKTE-------------------------------IIKPL------GLEKL-LDKNVKDL 456
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488923006 829 SGGEAQRMKLASELHKKAngkNFYILDEPTTglHTDDIKRLL--DVLQRLVDN-GNTVLVIEHNLDVI 893
Cdd:COG1245  457 SGGELQRVAIAACLSRDA---DLYLLDEPSA--HLDVEQRLAvaKAIRRFAENrGKTAMVVDHDIYLI 519
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
480-560 3.41e-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: 53.83  E-value: 3.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  480 LSRSARTLSGGEAQRIRLAtQIGSNLSGVLyILDEPSIGLHQRDNNRLISSLKKMRDlGNTLVVVEHDEDTMWAADYLID 559
Cdd:TIGR02857 452 IGEGGAGLSGGQAQRLALA-RAFLRDAPLL-LLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAALADRIVV 528

                  .
gi 488923006  560 I 560
Cdd:TIGR02857 529 L 529
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
461-652 3.55e-07

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: 54.04  E-value: 3.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  461 KEIKDRLNFLRNVGLEYlTLSRSARTLSGGEAQRIRLATQIGSNlsGVLYILDEPSIGLHQRDNNRLISSLKK-MRDLGN 539
Cdd:TIGR03269 144 EAVGRAVDLIEMVQLSH-RITHIARDLSGGEKQRVVLARQLAKE--PFLFLADEPTGTLDPQTAKLVHNALEEaVKASGI 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  540 TLVVVEHDEDTMW-AADYLIDIgpgagENgGEVMAAGTPKQVAKsrksltgKYLSGkkfipVPETRRTGNGQS----IKL 614
Cdd:TIGR03269 221 SMVLTSHWPEVIEdLSDKAIWL-----EN-GEIKEEGTPDEVVA-------VFMEG-----VSEVEKECEVEVgepiIKV 282
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 488923006  615 KGVQE----------NNLKNIDVDFPLGEFVAVTGVSGSGKSTLVNMV 652
Cdd:TIGR03269 283 RNVSKryisvdrgvvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKII 330
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
420-583 3.58e-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: 52.12  E-value: 3.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 420 SVKIDGKHIAEIS-----ALPIDSAMEF-----FGNLNFSEQdtaVATPIL-------KEIKDR-LNFLRNVGLEYLTLS 481
Cdd:cd03261   56 EVLIDGEDISGLSeaelyRLRRRMGMLFqsgalFDSLTVFEN---VAFPLRehtrlseEEIREIvLEKLEAVGLRGAEDL 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 482 RSARtLSGGEAQRIRLATQIGSNLSGVLYilDEPSIGLH---QRDNNRLISSLKKMrdLGNTLVVVEHDEDTMWA-ADYL 557
Cdd:cd03261  133 YPAE-LSGGMKKRVALARALALDPELLLY--DEPTAGLDpiaSGVIDDLIRSLKKE--LGLTSIMVTHDLDTAFAiADRI 207
                        170       180
                 ....*....|....*....|....*.
gi 488923006 558 IDIGpgagenGGEVMAAGTPKQVAKS 583
Cdd:cd03261  208 AVLY------DGKIVAEGTPEELRAS 227
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
474-579 5.45e-07

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: 53.22  E-value: 5.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 474 GLEYLtLSRSARTLSGGEAQRIRLATQIGSNLSgvLYILDEPSIGLHQRDNNRLISSLKKMRDlGNTLVVVEHDEDTMWA 553
Cdd:COG4988  462 GLDTP-LGEGGRGLSGGQAQRLALARALLRDAP--LLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLAQ 537
                         90       100
                 ....*....|....*....|....*.
gi 488923006 554 ADYLIDIgpgageNGGEVMAAGTPKQ 579
Cdd:COG4988  538 ADRILVL------DDGRIVEQGTHEE 557
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
622-890 6.24e-07

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: 51.41  E-value: 6.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTLVnmvlkRVLAQKLNHNSEKPgkyksVSGikniekVINIDQspigrtprsnpat 701
Cdd:cd03260   16 LKDISLDIPKGEITALIGPSGCGKSTLL-----RLLNRLNDLIPGAP-----DEG------EVLLDG------------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 702 ytsvfDDIRGLfaQTNEAKLRgytkgrfsfnvkggrceackgdgiLKIEMNF-LPDVYvpcevcHGTRYNSETLEVKYKG 780
Cdd:cd03260   67 -----KDIYDL--DVDVLELR------------------------RRVGMVFqKPNPF------PGSIYDNVAYGLRLHG 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 781 KTIADILDMTVEEAtdffapipkiarkLQTiidVGL-GYVHLGQSATTLSGGEAQRMKLASELhkkANGKNFYILDEPTT 859
Cdd:cd03260  110 IKLKEELDERVEEA-------------LRK---AALwDEVKDRLHALGLSGGQQQRLCLARAL---ANEPEVLLLDEPTS 170
                        250       260       270
                 ....*....|....*....|....*....|....
gi 488923006 860 GL---HTDDIKRLLDVLQRLVdngnTVLVIEHNL 890
Cdd:cd03260  171 ALdpiSTAKIEELIAELKKEY----TIVIVTHNM 200
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
473-583 6.45e-07

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 51.71  E-value: 6.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 473 VGLEYLTlSRSARTLSGGEAQRIRLATQIGSNLSGVLyiLDEPSIGL---HQRDNNRLISSLKKMRDLgnTLVVVEHDED 549
Cdd:PRK10575 135 VGLKPLA-HRLVDSLSGGERQRAWIAMLVAQDSRCLL--LDEPTSALdiaHQVDVLALVHRLSQERGL--TVIAVLHDIN 209
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 488923006 550 tMWA--ADYLIDIgpgageNGGEVMAAGTPKQVAKS 583
Cdd:PRK10575 210 -MAAryCDYLVAL------RGGEMIAQGTPAELMRG 238
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
622-859 6.98e-07

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 49.57  E-value: 6.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  622 LKNIDVDFPLGEFVAVTGVSGSGKSTLVNMVLkrvlaqklnhnsekpGKYKSVSGIkniekvINIDQSPIGRTPRSnpat 701
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIA---------------GLLSPTEGT------ILLDGQDLTDDERK---- 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  702 ytsvfddirglfaqtneaklrgYTKGRFSfnvkggrceackgdgilkiemnflpdvYVPCEVCHGTRYnsetlevkykgk 781
Cdd:pfam00005  56 ----------------------SLRKEIG---------------------------YVFQDPQLFPRL------------ 74
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  782 TIADILDMTVEEATDFFApipKIARKLQTIID-VGLGYV---HLGQSATTLSGGEAQRMKLASELhkkANGKNFYILDEP 857
Cdd:pfam00005  75 TVRENLRLGLLLKGLSKR---EKDARAEEALEkLGLGDLadrPVGERPGTLSGGQRQRVAIARAL---LTKPKLLLLDEP 148

                  ..
gi 488923006  858 TT 859
Cdd:pfam00005 149 TA 150
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
612-898 8.42e-07

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 50.82  E-value: 8.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 612 IKLKGV---QENN---LKNIDVDFPLGEFVAVTGVSGSGKSTLVNMVLKrvlaqklnhnSEKP--GKYkSVSGiKNIEKv 683
Cdd:COG2884    2 IRFENVskrYPGGreaLSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYG----------EERPtsGQV-LVNG-QDLSR- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 684 INIDQSP-----IGRtprsnpatytsVFDDIRglfaqtneaklrgytkgrfsfnvkggrceackgdgilkiemnFLPDvy 758
Cdd:COG2884   69 LKRREIPylrrrIGV-----------VFQDFR------------------------------------------LLPD-- 93
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 759 vpcevchgtrynsetlevkykgKTIAD--ILDMTVEEatdffAPIPKIARKLQTIID-VGLG-----YVHlgqsatTLSG 830
Cdd:COG2884   94 ----------------------RTVYEnvALPLRVTG-----KSRKEIRRRVREVLDlVGLSdkakaLPH------ELSG 140
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 831 GEAQRMKLASELhkkANgkNFYIL--DEPTTGLHTDDIKRLLDVLQRLVDNGNTVLVIEHNLDVIKTADH 898
Cdd:COG2884  141 GEQQRVAIARAL---VN--RPELLlaDEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPK 205
cbiO PRK13637
energy-coupling factor transporter ATPase;
443-582 9.52e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 51.59  E-value: 9.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 443 FG--NLNFSEQDtavatpILKEIKDRLNFlrnVGLEYLTLS-RSARTLSGGEAQRIRLATQIGSNLSgVLyILDEPSIGL 519
Cdd:PRK13637 107 FGpiNLGLSEEE------IENRVKRAMNI---VGLDYEDYKdKSPFELSGGQKRRVAIAGVVAMEPK-IL-ILDEPTAGL 175
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488923006 520 HQRDNNRLISSLKKMRD-LGNTLVVVEHD-EDTMWAADYLIDIgpgageNGGEVMAAGTPKQVAK 582
Cdd:PRK13637 176 DPKGRDEILNKIKELHKeYNMTIILVSHSmEDVAKLADRIIVM------NKGKCELQGTPREVFK 234
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
622-898 1.06e-06

Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages


Pssm-ID: 213259 [Multi-domain]  Cd Length: 214  Bit Score: 50.48  E-value: 1.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTLVNMVLKRvlaqklnhnsEKPgkyksVSGikniekVINIDQSPIGRTPRSNPAT 701
Cdd:cd03292   17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKE----------ELP-----TSG------TIRVNGQDVSDLRGRAIPY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 702 YTS----VFDDIRglfaqtneaklrgytkgrfsfnvkggrceackgdgilkiemnFLPDVYVPCEVchgtrynSETLEVK 777
Cdd:cd03292   76 LRRkigvVFQDFR------------------------------------------LLPDRNVYENV-------AFALEVT 106
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 778 YKG-----KTIADILDMtveeatdffapipkiarklqtiidVGLGYVHlGQSATTLSGGEAQRMKLASELhkkANGKNFY 852
Cdd:cd03292  107 GVPpreirKRVPAALEL------------------------VGLSHKH-RALPAELSGGEQQRVAIARAI---VNSPTIL 158
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 488923006 853 ILDEPTTGLHTDDIKRLLDVLQRLVDNGNTVLVIEHNLDVIKTADH 898
Cdd:cd03292  159 IADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRH 204
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
485-549 1.13e-06

Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213193 [Multi-domain]  Cd Length: 205  Bit Score: 50.33  E-value: 1.13e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488923006 485 RTLSGGEAQRIRLATQIGSNLSgvLYILDEPSIGLhQRDNNRLISslKKMRDL---GNTLVVVEHDED 549
Cdd:cd03226  125 LSLSGGQKQRLAIAAALLSGKD--LLIFDEPTSGL-DYKNMERVG--ELIRELaaqGKAVIVITHDYE 187
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
470-587 1.61e-06

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 50.78  E-value: 1.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 470 LRNVGLEYLTLSRSARtLSGGEAQRIRLATQIGsnLSGVLYILDEPSIGLHQRDNNRLISSLKKMRDLGN-TLVVVEHDE 548
Cdd:PRK13635 125 LRQVGMEDFLNREPHR-LSGGQKQRVAIAGVLA--LQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDL 201
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 488923006 549 DTMWAADYLIDIgpgageNGGEVMAAGTPKQVAKSRKSL 587
Cdd:PRK13635 202 DEAAQADRVIVM------NKGEILEEGTPEEIFKSGHML 234
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
619-900 1.70e-06

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: 50.31  E-value: 1.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 619 ENNLKNIDVDFPLGEFVAVTGVSGSGKSTLVNMVlkrvlaqklnhnsekPGKYKSVSGikniekVINIDQspigrtprsn 698
Cdd:cd03251   15 PPVLRDISLDIPAGETVALVGPSGSGKSTLVNLI---------------PRFYDVDSG------RILIDG---------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 699 patytsvfDDIRGLFAQTNEAKLRGYTKGRFSFNvkggrceackgdgilkiemnflpdvyvpcevchGTRYNSetleVKY 778
Cdd:cd03251   64 --------HDVRDYTLASLRRQIGLVSQDVFLFN---------------------------------DTVAEN----IAY 98
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 779 kGKTIADilDMTVEEATdffapipKIARKLQTIIDVGLGY-VHLGQSATTLSGGEAQRMKLASELHKKAngkNFYILDEP 857
Cdd:cd03251   99 -GRPGAT--REEVEEAA-------RAANAHEFIMELPEGYdTVIGERGVKLSGGQRQRIAIARALLKDP---PILILDEA 165
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 488923006 858 TTGLHTDDIKRLLDVLQRLVDNgNTVLVIEHNLDVIKTADHLI 900
Cdd:cd03251  166 TSALDTESERLVQAALERLMKN-RTTFVIAHRLSTIENADRIV 207
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
807-902 2.10e-06

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.


Pssm-ID: 213188 [Multi-domain]  Cd Length: 144  Bit Score: 48.21  E-value: 2.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 807 KLQTIIDVGLGYVHlgQsattLSGGEAQRMKLASELHKKANgknFYILDEPTTGLHTDDIKRLLDVLQRLvdNGnTVLVI 886
Cdd:cd03221   56 IVTWGSTVKIGYFE--Q----LSGGEKMRLALAKLLLENPN---LLLLDEPTNHLDLESIEALEEALKEY--PG-TVILV 123
                         90
                 ....*....|....*..
gi 488923006 887 EHNLDVI-KTADHLIDL 902
Cdd:cd03221  124 SHDRYFLdQVATKIIEL 140
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
828-900 2.33e-06

ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213196 [Multi-domain]  Cd Length: 178  Bit Score: 48.72  E-value: 2.33e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488923006 828 LSGGEAQRMKLASELhkkANGKNFYILDEPTTGLHTDDIKRLLDVLQRLVDN-GNTVLVIEHNLDVIKT-ADHLI 900
Cdd:cd03229  101 LSGGQQQRVALARAL---AMDPDVLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARlADRVV 172
cbiO PRK13644
energy-coupling factor transporter ATPase;
775-900 2.36e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 50.37  E-value: 2.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 775 EVKYKGKTIADILDMTVEEATdfFAPIPKIARKLQTIIDVGLG-YVHlgQSATTLSGGEAQRMKLASELhkkANGKNFYI 853
Cdd:PRK13644  87 ETQFVGRTVEEDLAFGPENLC--LPPIEIRKRVDRALAEIGLEkYRH--RSPKTLSGGQGQCVALAGIL---TMEPECLI 159
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 488923006 854 LDEPTTGLHTDDIKRLLDVLQRLVDNGNTVLVIEHNLDVIKTADHLI 900
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRII 206
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
622-901 2.37e-06

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: 49.80  E-value: 2.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTLVnmvlkRVLAqklnhnsekpGKYKSVSGikniekVINIDQSPIGRT-PRSNPA 700
Cdd:COG1124   21 LKDVSLEVAPGESFGLVGESGSGKSTLL-----RALA----------GLERPWSG------EVTFDGRPVTRRrRKAFRR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 701 TYTSVFDDIRGlfaqtneaklrgytkgrfSFNvkggrceackgdgilkiemnflpdvyvPCevchgtrynsetlevkykg 780
Cdd:COG1124   80 RVQMVFQDPYA------------------SLH---------------------------PR------------------- 95
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 781 KTIADILD-----MTVEEATDffapipKIARKLQtiiDVGLGYVHLGQSATTLSGGEAQRMKLASEL-HKKAngknFYIL 854
Cdd:COG1124   96 HTVDRILAeplriHGLPDREE------RIAELLE---QVGLPPSFLDRYPHQLSGGQRQRVAIARALiLEPE----LLLL 162
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488923006 855 DEPTTGLhtdDI---KRLLDVLQRL-VDNGNTVLVIEHNLDVIktaDHLID 901
Cdd:COG1124  163 DEPTSAL---DVsvqAEILNLLKDLrEERGLTYLFVSHDLAVV---AHLCD 207
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
622-652 2.37e-06

ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 50.09  E-value: 2.37e-06
                         10        20        30
                 ....*....|....*....|....*....|.
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTLVNMV 652
Cdd:COG1116   27 LDDVSLTVAAGEFVALVGPSGCGKSTLLRLI 57
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
467-563 2.39e-06

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 49.43  E-value: 2.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 467 LNFLRNVGLEYLTLSRSARTLSGGEAQRIRLAtqigSNLS---GVLyILDEPSIGLHQrDNNRLISSL--KKMRDLGNTL 541
Cdd:COG4619  111 LELLERLGLPPDILDKPVERLSGGERQRLALI----RALLlqpDVL-LLDEPTSALDP-ENTRRVEELlrEYLAEEGRAV 184
                         90       100
                 ....*....|....*....|....*
gi 488923006 542 VVVEHDEDtmWA---ADYLIDIGPG 563
Cdd:COG4619  185 LWVSHDPE--QIervADRVLTLEAG 207
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
5-53 2.42e-06

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


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 48.51  E-value: 2.42e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 488923006   5 KIVIhGARAHNLKNIDVTIPRDKLVVVTGLSGSGKSSLAFDTLYAEGQR 53
Cdd:cd03227    1 KIVL-GRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGA 48
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
775-894 3.05e-06

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: 49.06  E-value: 3.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 775 EVKYKGKtiaDILDMTVEEATD------FFAP--IPKIarklqTIIDVgLGYVHLGqsattLSGGEAQRMKLASELHKKA 846
Cdd:cd03217   58 EILFKGE---DITDLPPEERARlgiflaFQYPpeIPGV-----KNADF-LRYVNEG-----FSGGEKKRNEILQLLLLEP 123
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488923006 847 NgknFYILDEPTTGLHTDDIKRLLDVLQRLVDNGNTVLVIEHN---LDVIK 894
Cdd:cd03217  124 D---LAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYqrlLDYIK 171
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
789-900 3.37e-06

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: 49.47  E-value: 3.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 789 MTVEEATDFFAPIPKIARK-LQTIID-----VGLGyVHLGQSATTLSGGeaQRMKLA---SELHKKANgknfYILDEPTT 859
Cdd:COG4555   89 LTVRENIRYFAELYGLFDEeLKKRIEelielLGLE-EFLDRRVGELSTG--MKKKVAlarALVHDPKV----LLLDEPTN 161
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 488923006 860 GLHTDDIKRLLDVLQRLVDNGNTVLVIEHNLDVI-KTADHLI 900
Cdd:COG4555  162 GLDVMARRLLREILRALKKEGKTVLFSSHIMQEVeALCDRVV 203
cbiO PRK13641
energy-coupling factor transporter ATPase;
443-593 3.76e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 49.83  E-value: 3.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 443 FGNLNFSEQDtavatpilKEIKDR-LNFLRNVGLEYLTLSRSARTLSGGEAQRIRLAtqigsnlsGVLYI------LDEP 515
Cdd:PRK13641 109 FGPKNFGFSE--------DEAKEKaLKWLKKVGLSEDLISKSPFELSGGQMRRVAIA--------GVMAYepeilcLDEP 172
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488923006 516 SIGLHQRDNNRLISSLKKMRDLGNTLVVVEHDEDTMwaADYLIDIgpgAGENGGEVMAAGTPKQVAKSRKSLTGKYLS 593
Cdd:PRK13641 173 AAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDV--AEYADDV---LVLEHGKLIKHASPKEIFSDKEWLKKHYLD 245
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
622-900 3.82e-06

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 50.55  E-value: 3.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTLVNMVLkRVlaqklnhnsekpgkYKSVSGikniekVINIDQSPIgrtprsnpAT 701
Cdd:COG1132  356 LKDISLTIPPGETVALVGPSGSGKSTLVNLLL-RF--------------YDPTSG------RILIDGVDI--------RD 406
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 702 YTsvFDDIRGLFAqtneaklrgytkgrfsfnvkggrceackgdgilkiemnflpdvYVPCEV--CHGT-RYNsetleVKY 778
Cdd:COG1132  407 LT--LESLRRQIG-------------------------------------------VVPQDTflFSGTiREN-----IRY 436
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 779 kGKtiADILDMTVEEA------TDFfapIPKIARKLQTIIdvglgyvhlGQSATTLSGGEAQRMKLASELHKKAngkNFY 852
Cdd:COG1132  437 -GR--PDATDEEVEEAakaaqaHEF---IEALPDGYDTVV---------GERGVNLSGGQRQRIAIARALLKDP---PIL 498
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 488923006 853 ILDEPTTGL--HTDdiKRLLDVLQRLVDnGNTVLVIEHNLDVIKTADHLI 900
Cdd:COG1132  499 ILDEATSALdtETE--ALIQEALERLMK-GRTTIVIAHRLSTIRNADRIL 545
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
480-559 3.96e-06

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


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 49.33  E-value: 3.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 480 LSRSARTLSGGEAQRIRLATQIGSNLSgvLYILDEPSIGL--HQRDN-----NRLISSLKKmrdlgnTLVVVEHDedtMW 552
Cdd:cd03237  109 LDREVPELSGGELQRVAIAACLSKDAD--IYLLDEPSAYLdvEQRLMaskviRRFAENNEK------TAFVVEHD---II 177

                 ....*..
gi 488923006 553 AADYLID 559
Cdd:cd03237  178 MIDYLAD 184
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
821-898 4.46e-06

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: 48.58  E-value: 4.46e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488923006 821 LGQSATTLSGGEAQRMKLASELHKKANgknFYILDEPTTGLHTDDIKRLLDVLQRLVDNGNTVLVIEHNLDVI-KTADH 898
Cdd:cd03224  126 RKQLAGTLSGGEQQMLAIARALMSRPK---LLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFAlEIADR 201
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
798-900 4.54e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 49.85  E-value: 4.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 798 FAPI----PKI-ARKLQT--IIDVGLGYVHLGQSATTLSGGEAQRMKLASELhkkANGKNFYILDEPTTGLHTDDIKRLL 870
Cdd:PRK13631 140 FGPValgvKKSeAKKLAKfyLNKMGLDDSYLERSPFGLSGGQKRRVAIAGIL---AIQPEILIFDEPTAGLDPKGEHEMM 216
                         90       100       110
                 ....*....|....*....|....*....|.
gi 488923006 871 DVLQRLVDNGNTVLVIEHNLD-VIKTADHLI 900
Cdd:PRK13631 217 QLILDAKANNKTVFVITHTMEhVLEVADEVI 247
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
622-653 4.59e-06

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 48.62  E-value: 4.59e-06
                         10        20        30
                 ....*....|....*....|....*....|..
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTLVNMVL 653
Cdd:cd03250   21 LKDINLEVPKGELVAIVGPVGSGKSSLLSALL 52
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
811-902 4.84e-06

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: 49.02  E-value: 4.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 811 IIDVGLGY-VHLGQSATTLSGGEAQRMKLASELHkkaNGKNFYILDEPTTGLHTDDIKRLLDVLQRLVDnGNTVLVIEHN 889
Cdd:cd03252  121 ISELPEGYdTIVGEQGAGLSGGQRQRIAIARALI---HNPRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHR 196
                         90
                 ....*....|...
gi 488923006 890 LDVIKTADHLIDL 902
Cdd:cd03252  197 LSTVKNADRIIVM 209
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
786-900 4.98e-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: 48.48  E-value: 4.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 786 ILDMTVEEATDFFAPIPKIARK-------LQTIIDVgLGY---VHLGQSATTLSGGEAQRMKLASELHKKAngkNFYILD 855
Cdd:cd03290   90 LLNATVEENITFGSPFNKQRYKavtdacsLQPDIDL-LPFgdqTEIGERGINLSGGQRQRICVARALYQNT---NIVFLD 165
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 488923006 856 EPTTGL--HTDDIKRLLDVLQRLVDNGNTVLVIEHNLDVIKTADHLI 900
Cdd:cd03290  166 DPFSALdiHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPHADWII 212
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
815-898 5.75e-06

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 50.23  E-value: 5.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 815 GLGYVhLGQSATTLSGGEAQRMKLASELHKKAngkNFYILDEPTTGLHTDDIKRLLDVLQRLVdNGNTVLVIEHNLDVIK 894
Cdd:PRK11174 474 GLDTP-IGDQAAGLSVGQAQRLALARALLQPC---QLLLLDEPTASLDAHSEQLVMQALNAAS-RRQTTLMVTHQLEDLA 548

                 ....
gi 488923006 895 TADH 898
Cdd:PRK11174 549 QWDQ 552
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
622-888 6.53e-06

Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.


Pssm-ID: 213180 [Multi-domain]  Cd Length: 194  Bit Score: 47.93  E-value: 6.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTLVNmvlkrVLAQKLnhnsekpgKYKSVSGikniekvinidqspigrtprsnpat 701
Cdd:cd03213   25 LKNVSGKAKPGELTAIMGPSGAGKSTLLN-----ALAGRR--------TGLGVSG------------------------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 702 ytsvfddirglfaqtnEAKLRGYTKGRFSFnvkggRCEACkgdgilkiemnflpdvYVPCEvchgtrynsetlevkykgk 781
Cdd:cd03213   67 ----------------EVLINGRPLDKRSF-----RKIIG----------------YVPQD------------------- 90
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 782 tiaDIL--DMTVEEATDFFApipkiarKLQTIidvglgyvhlgqsattlSGGEAQRMKLASELhkkANGKNFYILDEPTT 859
Cdd:cd03213   91 ---DILhpTLTVRETLMFAA-------KLRGL-----------------SGGERKRVSIALEL---VSNPSLLFLDEPTS 140
                        250       260
                 ....*....|....*....|....*....
gi 488923006 860 GLHTDDIKRLLDVLQRLVDNGNTVLVIEH 888
Cdd:cd03213  141 GLDSSSALQVMSLLRRLADTGRTIICSIH 169
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
482-580 6.85e-06

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 49.45  E-value: 6.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 482 RSARTLSGGEAQRIRLATQIGSNlSGVLyILDEPSIGLhqrDNNRLISSLKKMRDL---GNTLVVVEHDEDTmwAADYLI 558
Cdd:PRK09536 135 RPVTSLSGGERQRVLLARALAQA-TPVL-LLDEPTASL---DINHQVRTLELVRRLvddGKTAVAAIHDLDL--AARYCD 207
                         90       100
                 ....*....|....*....|..
gi 488923006 559 DIGPGAgenGGEVMAAGTPKQV 580
Cdd:PRK09536 208 ELVLLA---DGRVRAAGPPADV 226
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
789-898 7.59e-06

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 49.64  E-value: 7.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 789 MTV--------EEATDFFAPIPKIARKLQTIID-VGLG-----YVHlgqsatTLSGGEAQR---MKLaseLHKKANgknF 851
Cdd:COG3845   95 LTVaenivlglEPTKGGRLDRKAARARIRELSErYGLDvdpdaKVE------DLSVGEQQRveiLKA---LYRGAR---I 162
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 488923006 852 YILDEPTTGLHTDDIKRLLDVLQRLVDNGNTVLVIEHNLDVIKT-ADH 898
Cdd:COG3845  163 LILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAiADR 210
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
461-587 7.83e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 48.45  E-value: 7.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 461 KEIKDRLNFL-RNVGLEYLtLSRSARTLSGGEAQRIRLATQIGSNLSgvLYILDEPSIGLHQRDNNRLISSLKKMRDLGN 539
Cdd:PRK13632 117 KKMKDIIDDLaKKVGMEDY-LDKEPQNLSGGQKQRVAIASVLALNPE--IIIFDESTSMLDPKGKREIKKIMVDLRKTRK 193
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 488923006 540 -TLVVVEHDEDTMWAADYLIDIgpgageNGGEVMAAGTPKQVAKSRKSL 587
Cdd:PRK13632 194 kTLISITHDMDEAILADKVIVF------SEGKLIAQGKPKEILNNKEIL 236
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
470-580 7.85e-06

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 48.61  E-value: 7.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 470 LRNVGLEYLTlSRSARTLSGGEAQRIRLA---TQI--GSNLSGVLyILDEPSIGL---HQRDNNRLISSLKKMRdlGNTL 541
Cdd:PRK13548 119 LAQVDLAHLA-GRDYPQLSGGEQQRVQLArvlAQLwePDGPPRWL-LLDEPTSALdlaHQHHVLRLARQLAHER--GLAV 194
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 488923006 542 VVVEHDED--TMWaADYLIDIgpgageNGGEVMAAGTPKQV 580
Cdd:PRK13548 195 IVVLHDLNlaARY-ADRIVLL------HQGRLVADGTPAEV 228
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
460-560 8.02e-06

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


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 48.52  E-value: 8.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 460 LKEIKDRLNfLRNVgleyltLSRSARTLSGGEAQRIRLATQIGSNlsGVLYILDEPS--IGLHQRDN-NRLISSLKKMrd 536
Cdd:cd03236  120 LDELVDQLE-LRHV------LDRNIDQLSGGELQRVAIAAALARD--ADFYFFDEPSsyLDIKQRLNaARLIRELAED-- 188
                         90       100
                 ....*....|....*....|....
gi 488923006 537 lGNTLVVVEHDEDTMwaaDYLIDI 560
Cdd:cd03236  189 -DNYVLVVEHDLAVL---DYLSDY 208
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
817-902 8.20e-06

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 48.44  E-value: 8.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 817 GYVHL-GQSATTLSGGEAQRMKLASELhkkANGKNFYILDEPTTGL---HTDDIKRLLDVLQRlvDNGNTVLVIEHNLD- 891
Cdd:PRK10253 132 GITHLaDQSVDTLSGGQRQRAWIAMVL---AQETAIMLLDEPTTWLdisHQIDLLELLSELNR--EKGYTLAAVLHDLNq 206
                         90
                 ....*....|.
gi 488923006 892 VIKTADHLIDL 902
Cdd:PRK10253 207 ACRYASHLIAL 217
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
821-898 8.49e-06

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 48.39  E-value: 8.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 821 LGQSATTLSGGEAQRMKLAS---ELHKKAN--GKnFYILDEPTTGLhtdDI--KRLLD-VLQRLVDNGNTVLVIEHNLDv 892
Cdd:PRK03695 120 LGRSVNQLSGGEWQRVRLAAvvlQVWPDINpaGQ-LLLLDEPMNSL---DVaqQAALDrLLSELCQQGIAVVMSSHDLN- 194

                 ....*.
gi 488923006 893 iKTADH 898
Cdd:PRK03695 195 -HTLRH 199
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
805-898 1.04e-05

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 48.16  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 805 ARKLQTIIDVGLGYVH--LGQSATTLSGGEAQRMKLASELHKKAngkNFYILDEPTTGLHTDDIKRLLDVLQRLV-DNGN 881
Cdd:PRK10418 116 ATLTAALEAVGLENAArvLKLYPFEMSGGMLQRMMIALALLCEA---PFIIADEPTTDLDVVAQARILDLLESIVqKRAL 192
                         90
                 ....*....|....*...
gi 488923006 882 TVLVIEHNLDVI-KTADH 898
Cdd:PRK10418 193 GMLLVTHDMGVVaRLADD 210
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
789-897 1.05e-05

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 47.95  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 789 MTVEE---ATDFFAPIPKIARKLQTIIDV-GLGYVHLGQSATTLSGGEAQRMKLASELHKKANgknFYILDEPTTGLHTD 864
Cdd:PRK11614  95 MTVEEnlaMGGFFAERDQFQERIKWVYELfPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPR---LLLLDEPSLGLAPI 171
                         90       100       110
                 ....*....|....*....|....*....|....
gi 488923006 865 DIKRLLDVLQRLVDNGNTVLVIEHNLD-VIKTAD 897
Cdd:PRK11614 172 IIQQIFDTIEQLREQGMTIFLVEQNANqALKLAD 205
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
461-580 1.19e-05

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 48.06  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 461 KEIKDRLN-FLRNVGLEYLTLsRSARTLSGGEAQRIRLATQIGSNLSgvLYILDEPSIGL---HQRDNNRLISSLKkmRD 536
Cdd:PRK10253 118 KEDEEAVTkAMQATGITHLAD-QSVDTLSGGQRQRAWIAMVLAQETA--IMLLDEPTTWLdisHQIDLLELLSELN--RE 192
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 488923006 537 LGNTLVVVEHD-EDTMWAADYLIDIgpgageNGGEVMAAGTPKQV 580
Cdd:PRK10253 193 KGYTLAAVLHDlNQACRYASHLIAL------REGKIVAQGAPKEI 231
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
797-891 1.21e-05

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 48.09  E-value: 1.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 797 FFAPIPKiARKLQTIIDVGLgyVHLG-QSATTLSGGEAQRMKLASELHKKAngkNFYILDEPTTGLHTDDIKRLLDVLQR 875
Cdd:PRK09984 124 WFTREQK-QRALQALTRVGM--VHFAhQRVSTLSGGQQQRVAIARALMQQA---KVILADEPIASLDPESARIVMDTLRD 197
                         90
                 ....*....|....*..
gi 488923006 876 LVDN-GNTVLVIEHNLD 891
Cdd:PRK09984 198 INQNdGITVVVTLHQVD 214
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
475-549 1.31e-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: 47.40  E-value: 1.31e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488923006 475 LEYLTLSRSART----LSGGEAQRIRLATQIGSNLSgvLYILDEPSIGLHQRDNNRLISSLKKMRDLGNTLVVVEHDED 549
Cdd:cd03292  121 LELVGLSHKHRAlpaeLSGGEQQRVAIARAIVNSPT--ILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKE 197
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
626-897 1.33e-05

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 48.80  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 626 DVDFPL--GEFVAVTGVSGSGKSTLVNMvLKRVlaqklnhnsekpgkYKSVSGIKNIEkviNIDQSPIGRTP-RSNPATy 702
Cdd:PRK13657 353 DVSFEAkpGQTVAIVGPTGAGKSTLINL-LQRV--------------FDPQSGRILID---GTDIRTVTRASlRRNIAV- 413
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 703 tsVFDDiRGLFAQTNEAKLRgytKGRfsfnvkggrceackgdgilkiemnflPDVyvpcevchgtrynseTLEVKYKGKT 782
Cdd:PRK13657 414 --VFQD-AGLFNRSIEDNIR---VGR--------------------------PDA---------------TDEEMRAAAE 446
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 783 IAdildmtveEATDFfapipkIARKLQtiidvglGY-VHLGQSATTLSGGEAQRMKLASELHKKAngkNFYILDEPTTGL 861
Cdd:PRK13657 447 RA--------QAHDF------IERKPD-------GYdTVVGERGRQLSGGERQRLAIARALLKDP---PILILDEATSAL 502
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 488923006 862 --HTDD-IKRLLDVLQRlvdnGNTVLVIEHNLDVIKTAD 897
Cdd:PRK13657 503 dvETEAkVKAALDELMK----GRTTFIIAHRLSTVRNAD 537
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
803-893 1.34e-05

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 48.08  E-value: 1.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 803 KIARKLQ---TIIDVGlGYVHlgQSATTLSGGEAQRMKLASELHKKANgknFYILDEPTTGLHTDDIKRLLDVLQRLVDN 879
Cdd:PRK13638 112 EITRRVDealTLVDAQ-HFRH--QPIQCLSHGQKKRVAIAGALVLQAR---YLLLDEPTAGLDPAGRTQMIAIIRRIVAQ 185
                         90
                 ....*....|....
gi 488923006 880 GNTVLVIEHNLDVI 893
Cdd:PRK13638 186 GNHVIISSHDIDLI 199
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
622-653 1.36e-05

Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443338 [Multi-domain]  Cd Length: 233  Bit Score: 47.43  E-value: 1.36e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTLVnMVL 653
Cdd:COG4181   28 LKGISLEVEAGESVAIVGASGSGKSTLL-GLL 58
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
799-890 1.44e-05

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 47.46  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 799 APIPKIARKLQTIID-----VGLgyVHLGQSA-TTLSGGEAQRMKLA---SELHKKANGKNFYILDEPTTGLhtdDIK-- 867
Cdd:PRK13548 102 APHGLSRAEDDALVAaalaqVDL--AHLAGRDyPQLSGGEQQRVQLArvlAQLWEPDGPPRWLLLDEPTSAL---DLAhq 176
                         90       100
                 ....*....|....*....|....*
gi 488923006 868 -RLLDVLQRLV-DNGNTVLVIEHNL 890
Cdd:PRK13548 177 hHVLRLARQLAhERGLAVIVVLHDL 201
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
455-547 1.48e-05

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 47.50  E-value: 1.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 455 VATPIL------KEIKDR-LNFLRNVGLEYLTLSRSARtLSGGEAQRIRLATQIGSNLSGVLyiLDEPSIGLHQRDNNRL 527
Cdd:PRK11629 108 VAMPLLigkkkpAEINSRaLEMLAAVGLEHRANHRPSE-LSGGERQRVAIARALVNNPRLVL--ADEPTGNLDARNADSI 184
                         90       100
                 ....*....|....*....|.
gi 488923006 528 ISSLKKM-RDLGNTLVVVEHD 547
Cdd:PRK11629 185 FQLLGELnRLQGTAFLVVTHD 205
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
820-900 1.71e-05

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: 47.15  E-value: 1.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 820 HLGQSATTLSGGEAQRMKLASELHKKAngkNFYILDEPTTGLHTDDIKRLLDVLQRLVdNGNTVLVIEHNLDVIKTADHL 899
Cdd:cd03249  132 LVGERGSQLSGGQKQRIAIARALLRNP---KILLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRLSTIRNADLI 207

                 .
gi 488923006 900 I 900
Cdd:cd03249  208 A 208
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
461-581 1.71e-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: 46.74  E-value: 1.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 461 KEIKDR-LNFLRNVGLEYLtLSRSARTLSGGEAQRIRLATQIGSNLSgvLYILDEPSIGLHQRDNNRLISSLKKM-RDLG 538
Cdd:cd03259  105 AEIRARvRELLELVGLEGL-LNRYPHELSGGQQQRVALARALAREPS--LLLLDEPLSALDAKLREELREELKELqRELG 181
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 488923006 539 NTLVVVEHD-EDTMWAADYLIdigpgagenggeVMAAGTPKQVA 581
Cdd:cd03259  182 ITTIYVTHDqEEALALADRIA------------VMNEGRIVQVG 213
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
458-581 1.74e-05

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: 47.04  E-value: 1.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 458 PILKEIKDRLnflrnvgleyltlsrsARTLSGGEAQriRLAtqIGSNLSG--VLYILDEPSIGL-----HQrdnnrLISS 530
Cdd:cd03224  120 PRLKERRKQL----------------AGTLSGGEQQ--MLA--IARALMSrpKLLLLDEPSEGLapkivEE-----IFEA 174
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488923006 531 LKKMRDLGNTLVVVEHDEDTMWA-AD--YLIDigpgagenGGEVMAAGTPKQVA 581
Cdd:cd03224  175 IRELRDEGVTILLVEQNARFALEiADraYVLE--------RGRVVLEGTAAELL 220
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
622-947 1.95e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 47.71  E-value: 1.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTLVnmvlkrvlaQKLNhnsekpGKYKSVSGIKNI-EKVInidqspigrTPRSNPA 700
Cdd:PRK13634  23 LYDVNVSIPSGSYVAIIGHTGSGKSTLL---------QHLN------GLLQPTSGTVTIgERVI---------TAGKKNK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 701 TytsvFDDIR---GLFAQTNEAKLrgytkgrFSFNVKGgrcEACKGdgilkiEMNFlpdvyvpcevchgtrynsetlevk 777
Cdd:PRK13634  79 K----LKPLRkkvGIVFQFPEHQL-------FEETVEK---DICFG------PMNF------------------------ 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 778 ykgktiadilDMTVEEATdffapipKIARKLqtIIDVGLGYVHLGQSATTLSGGEAQRMKLASELhkkANGKNFYILDEP 857
Cdd:PRK13634 115 ----------GVSEEDAK-------QKAREM--IELVGLPEELLARSPFELSGGQMRRVAIAGVL---AMEPEVLVLDEP 172
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 858 TTGLHTDDIKRLLDVLQRLVDNGN-TVLVIEHNL-DVIKTADHLIDLgpeggaGGGQVVAVGTPEAIAAVPESYTGKYLK 935
Cdd:PRK13634 173 TAGLDPKGRKEMMEMFYKLHKEKGlTTVLVTHSMeDAARYADQIVVM------HKGTVFLQGTPREIFADPDELEAIGLD 246
                        330
                 ....*....|....
gi 488923006 936 --EVLERAQELSQK 947
Cdd:PRK13634 247 lpETVKFKRALEEK 260
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
622-652 2.02e-05

ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213260 [Multi-domain]  Cd Length: 220  Bit Score: 46.70  E-value: 2.02e-05
                         10        20        30
                 ....*....|....*....|....*....|.
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTLVNMV 652
Cdd:cd03293   20 LEDISLSVEEGEFVALVGPSGCGKSTLLRII 50
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
828-902 2.18e-05

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 48.18  E-value: 2.18e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488923006 828 LSGGEAQRMKLASELhkkANGKNFYILDEPTTGLHTDDIKRLLDVLQRLVDNGNTVLVIEHNLDVIKTADHLIDL 902
Cdd:PRK10535 145 LSGGQQQRVSIARAL---MNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEI 216
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
16-42 2.21e-05

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: 46.31  E-value: 2.21e-05
                         10        20
                 ....*....|....*....|....*..
gi 488923006  16 LKNIDVTIPRDKLVVVTGLSGSGKSSL 42
Cdd:cd03250   21 LKDINLEVPKGELVAIVGPVGSGKSSL 47
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
612-652 2.99e-05

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 46.29  E-value: 2.99e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 488923006 612 IKLKGV---QENNLKNIDVDFPLGEFVAVTGVSGSGKSTLVNMV 652
Cdd:COG3840    2 LRLDDLtyrYGDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLI 45
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
828-900 3.03e-05

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 46.93  E-value: 3.03e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488923006 828 LSGGEAQRMKLASELhkkANGKNFYILDEPTTGLhtDDIKR--LLDVLQRLVDNGN-TVLVIEHNLDVIKTADHLI 900
Cdd:PRK13635 141 LSGGQKQRVAIAGVL---ALQPDIIILDEATSML--DPRGRreVLETVRQLKEQKGiTVLSITHDLDEAAQADRVI 211
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
486-588 3.08e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 46.67  E-value: 3.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 486 TLSGGEAQRIRLATQIGSNLSgvLYILDEPSIGLHQRDNNRLISSLKKMRDLGN-TLVVVEHDEDTMWAADYLIDIgpga 564
Cdd:PRK13648 142 ALSGGQKQRVAIAGVLALNPS--VIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAMEADHVIVM---- 215
                         90       100
                 ....*....|....*....|....
gi 488923006 565 geNGGEVMAAGTPKQVAKSRKSLT 588
Cdd:PRK13648 216 --NKGTVYKEGTPTEIFDHAEELT 237
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
827-900 3.22e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 46.67  E-value: 3.22e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488923006 827 TLSGGEAQRMKLASELhkkANGKNFYILDEPTTGLHTDDIKRLLDVLQRLVDNGN-TVLVIEHNLDVIKTADHLI 900
Cdd:PRK13648 142 ALSGGQKQRVAIAGVL---ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAMEADHVI 213
hmuV PRK13547
heme ABC transporter ATP-binding protein;
821-924 3.67e-05

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 46.74  E-value: 3.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 821 LGQSATTLSGGEAQRMKLASEL------HKKANGKNFYILDEPTTGLHTDDIKRLLDVLQRLVDNGNT-VLVIEHNLDV- 892
Cdd:PRK13547 139 VGRDVTTLSGGELARVQFARVLaqlwppHDAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLa 218
                         90       100       110
                 ....*....|....*....|....*....|..
gi 488923006 893 IKTADHLIDLGPEGGAGGGQVVAVGTPEAIAA 924
Cdd:PRK13547 219 ARHADRIAMLADGAIVAHGAPADVLTPAHIAR 250
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
788-900 3.73e-05

ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213231 [Multi-domain]  Cd Length: 211  Bit Score: 45.65  E-value: 3.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 788 DMTVEEATDFFAPIPKIA-RKLQTIIDVGLGYVHLGQSAT----TLSGGEAQRMKLASELhkkANGKNFYILDEPTTGLH 862
Cdd:cd03264   86 NFTVREFLDYIAWLKGIPsKEVKARVDEVLELVNLGDRAKkkigSLSGGMRRRVGIAQAL---VGDPSILIVDEPTAGLD 162
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 488923006 863 TDDIKRLLDVLQRLVDNgNTVLVIEHNL-DVIKTADHLI 900
Cdd:cd03264  163 PEERIRFRNLLSELGED-RIVILSTHIVeDVESLCNQVA 200
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
806-902 3.94e-05

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 46.50  E-value: 3.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 806 RKLQTIIDVGLGYVHLGQSATTLSGGEAQRMKLASELhkkANGKNFYILDEPTTGLHTDDIKRLLDVLQRLVDNGNTVLV 885
Cdd:PRK10619 131 RAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARAL---AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVV 207
                         90
                 ....*....|....*...
gi 488923006 886 IEHNLDVIK-TADHLIDL 902
Cdd:PRK10619 208 VTHEMGFARhVSSHVIFL 225
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
487-558 4.36e-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: 45.26  E-value: 4.36e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488923006 487 LSGGEAQRIRLATQIGSNLSgvLYILDEPSIGLHQRDNNRLISSLKKMRD-LGNTLVVVEHD-EDTMWAADYLI 558
Cdd:cd03229  101 LSGGQQQRVALARALAMDPD--VLLLDEPTSALDPITRREVRALLKSLQAqLGITVVLVTHDlDEAARLADRVV 172
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
803-894 4.83e-05

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 46.85  E-value: 4.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 803 KIARKLQTIIDVGLGYVHLGqsattlsGGEAQRMKLASELHKKANgknFYILDEPTTGLHTDDIKRLLDVLQRLVDNGNT 882
Cdd:PRK13549 126 KLLAQLKLDINPATPVGNLG-------LGQQQLVEIAKALNKQAR---LLILDEPTASLTESETAVLLDIIRDLKAHGIA 195
                         90
                 ....*....|..
gi 488923006 883 VLVIEHNLDVIK 894
Cdd:PRK13549 196 CIYISHKLNEVK 207
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
436-580 5.31e-05

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 46.15  E-value: 5.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 436 IDSAMEF-FGNLNFSEQDtavatpILKEIKDRLNFLRNVGLEYltlsRSARTLSGGEAQRIRLATQIgsNLSGVLYILDE 514
Cdd:PRK13638  95 IDSDIAFsLRNLGVPEAE------ITRRVDEALTLVDAQHFRH----QPIQCLSHGQKKRVAIAGAL--VLQARYLLLDE 162
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488923006 515 PSIGLHQRDNNRLISSLKKMRDLGNTLVVVEHDEDTMWA---ADYLIdigpgageNGGEVMAAGTPKQV 580
Cdd:PRK13638 163 PTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEisdAVYVL--------RQGQILTHGAPGEV 223
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
482-547 5.52e-05

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 46.03  E-value: 5.52e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488923006 482 RSARTLSGGEAQRIRLATQIGSNlsGVLYILDEPSIGLHQRDNNRLISSLKKMRDLGNTLVVVEHD 547
Cdd:PRK15056 138 RQIGELSGGQKKRVFLARAIAQQ--GQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHN 201
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
601-658 5.52e-05

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 45.82  E-value: 5.52e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488923006 601 PETRRTGNGQSIKLKGV-----QENNLKNIDVDFPLGEFVAVTGVSGSGKSTLVnmvlkRVLA 658
Cdd:PRK11247   2 MNTARLNQGTPLLLNAVskrygERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLL-----RLLA 59
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
486-562 5.57e-05

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 45.29  E-value: 5.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 486 TLSGGE------AQRIRLATQIGSNLSgvLYILDEPSIGL-HQRDNNRLISSLKKMRDLGN-TLVVVEHDEDTMWAADYL 557
Cdd:cd03240  115 RCSGGEkvlaslIIRLALAETFGSNCG--ILALDEPTTNLdEENIEESLAEIIEERKSQKNfQLIVITHDEELVDAADHI 192

                 ....*
gi 488923006 558 IDIGP 562
Cdd:cd03240  193 YRVEK 197
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
789-900 5.78e-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: 5.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 789 MTVEEATDFFAPIP-----KIARKLQTIIDVGLGYVHLGQSATT----LSGGEAQRMKLASELhkkANGKNFYILDEPTT 859
Cdd:cd03234   96 LTVRETLTYTAILRlprksSDAIRKKRVEDVLLRDLALTRIGGNlvkgISGGERRRVSIAVQL---LWDPKVLILDEPTS 172
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 488923006 860 GLHTDDIKRLLDVLQRLVDNGNTVLVIEHN--LDVIKTADHLI 900
Cdd:cd03234  173 GLDSFTALNLVSTLSQLARRNRIVILTIHQprSDLFRLFDRIL 215
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
822-902 5.83e-05

ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.


Pssm-ID: 213215 [Multi-domain]  Cd Length: 226  Bit Score: 45.54  E-value: 5.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 822 GQSATTLSGGEAQRMKLASELHKKAngkNFYILDEPTTGLhtdDIKRLLDVLQRLVD--NGNTVLVIEHNLDVIKTADHL 899
Cdd:cd03248  145 GEKGSQLSGGQKQRVAIARALIRNP---QVLILDEATSAL---DAESEQQVQQALYDwpERRTVLVIAHRLSTVERADQI 218

                 ...
gi 488923006 900 IDL 902
Cdd:cd03248  219 LVL 221
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
622-900 5.91e-05

ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213221 [Multi-domain]  Cd Length: 229  Bit Score: 45.29  E-value: 5.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTLVNMVLKRVLAQKlnhnsekpGKyksvsgikniekvINIDQSPIGRTP----RS 697
Cdd:cd03254   19 LKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQK--------GQ-------------ILIDGIDIRDISrkslRS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 698 NPATytsVFDDIrGLFAQTneaklrgytkgrFSFNVKGGRCEAckgdgilkiemnflpdvyvpcevchgtryNSEtlEVK 777
Cdd:cd03254   78 MIGV---VLQDT-FLFSGT------------IMENIRLGRPNA-----------------------------TDE--EVI 110
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 778 YKGKTIAdildmtveeATDFFAPIPKiarklqtiidvGLgYVHLGQSATTLSGGEAQRMKLASELHKKAngkNFYILDEP 857
Cdd:cd03254  111 EAAKEAG---------AHDFIMKLPN-----------GY-DTVLGENGGNLSQGERQLLAIARAMLRDP---KILILDEA 166
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 488923006 858 TTGLHTDDIKRLLDVLQRLVdNGNTVLVIEHNLDVIKTADHLI 900
Cdd:cd03254  167 TSNIDTETEKLIQEALEKLM-KGRTSIIIAHRLSTIKNADKIL 208
cbiO PRK13645
energy-coupling factor transporter ATPase;
798-900 6.07e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 46.15  E-value: 6.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 798 FAPI------PKIARKLQTIID-VGLGYVHLGQSATTLSGGEAQRMKLASELhkkANGKNFYILDEPTTGLHTDDIKRLL 870
Cdd:PRK13645 114 FGPVnlgenkQEAYKKVPELLKlVQLPEDYVKRSPFELSGGQKRRVALAGII---AMDGNTLVLDEPTGGLDPKGEEDFI 190
                         90       100       110
                 ....*....|....*....|....*....|..
gi 488923006 871 DVLQRLVDN-GNTVLVIEHNLD-VIKTADHLI 900
Cdd:PRK13645 191 NLFERLNKEyKKRIIMVTHNMDqVLRIADEVI 222
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
487-598 6.29e-05

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 46.64  E-value: 6.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 487 LSGGEAQRIRLATQIgsnLSGVLYIL-DEPSIGLHQRDNNRLISSLKKMRDLGNTLVVVEHDEDTMWAADYLIDIgpgag 565
Cdd:PRK10535 145 LSGGQQQRVSIARAL---MNGGQVILaDEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEI----- 216
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 488923006 566 eNGGEVMAAGTPK---QVAKSRKSLTGKYLSGKKFI 598
Cdd:PRK10535 217 -RDGEIVRNPPAQekvNVAGGTEPVVNTASGWRQFV 251
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
461-580 6.35e-05

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 46.24  E-value: 6.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 461 KEIKDRLN-FLRNVGLEYLtLSRSARTLSGGEAQRIRLA----TQigsnlSGVLyILDEPSIGLhqrDNN---RLISSLK 532
Cdd:COG3842  110 AEIRARVAeLLELVGLEGL-ADRYPHQLSGGQQQRVALAralaPE-----PRVL-LLDEPLSAL---DAKlreEMREELR 179
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 488923006 533 KM-RDLGNTLVVVEHD-EDTMWAADYLIDIgpgageNGGEVMAAGTPKQV 580
Cdd:COG3842  180 RLqRELGITFIYVTHDqEEALALADRIAVM------NDGRIEQVGTPEEI 223
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
599-689 6.77e-05

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 45.33  E-value: 6.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 599 PVPETRRTGNGQS---IKLKGVQENNLKNIDVDFPLGEFVAVTGVSGSGKSTLVNMVLKRVLAQKLNHNSEKPGK--YKS 673
Cdd:COG2401   20 VLDLSERVAIVLEafgVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNqfGRE 99
                         90
                 ....*....|....*.
gi 488923006 674 VSGIKNIEKVINIDQS 689
Cdd:COG2401  100 ASLIDAIGRKGDFKDA 115
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
828-888 7.39e-05

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 46.58  E-value: 7.39e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488923006  828 LSGGEAQRMKLASELhkkANGKNFYILDEPTTGLHTDDIKRLLDVLQRLVDNGNTVLVIEH 888
Cdd:TIGR00955 167 LSGGERKRLAFASEL---LTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
487-560 9.44e-05

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


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 44.10  E-value: 9.44e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488923006 487 LSGGEAQRIRLATQIGSNLSgvLYILDEPSIGLHQRDNNRLISSLKKMRDLGN-TLVVVEHDedtMWAADYLIDI 560
Cdd:cd03222   72 LSGGELQRVAIAAALLRNAT--FYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHD---LAVLDYLSDR 141
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
821-896 9.55e-05

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 44.88  E-value: 9.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 821 LGQSattLSGGEAQRMKLASELhkKANGKnFYILDEPTTGLHTDDIKRLLDVLQRLVDNGNTVLVIEHN----LDVIKTA 896
Cdd:PRK10895 134 MGQS---LSGGERRRVEIARAL--AANPK-FILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNvretLAVCERA 207
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
611-652 9.98e-05

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 45.45  E-value: 9.98e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 488923006 611 SIKLKGV-----QENNLKNIDVDFPLGEFVAVTGVSGSGKSTLVNMV 652
Cdd:COG3839    3 SLELENVsksygGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMI 49
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
612-648 1.06e-04

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: 45.11  E-value: 1.06e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 488923006  612 IKLKGV-------QENNLKNIDVDFPLGEFVAVTGVSGSGKSTL 648
Cdd:TIGR04520   1 IEVENVsfsypesEKPALKNVSLSIEKGEFVAIIGHNGSGKSTL 44
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
461-580 1.07e-04

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: 44.54  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 461 KEIKDRLN-FLRNVGLEYLtLSRSARTLSGGEAQRIRLATQIgSNLSGVLyILDEPSIGLHQRDNNRLISSLKKM-RDLG 538
Cdd:cd03300  105 AEIKERVAeALDLVQLEGY-ANRKPSQLSGGQQQRVAIARAL-VNEPKVL-LLDEPLGALDLKLRKDMQLELKRLqKELG 181
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 488923006 539 NTLVVVEHD-EDTMWAADYLidigpgAGENGGEVMAAGTPKQV 580
Cdd:cd03300  182 ITFVFVTHDqEEALTMSDRI------AVMNKGKIQQIGTPEEI 218
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
487-558 1.24e-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: 43.53  E-value: 1.24e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488923006 487 LSGGEAQRIRLATQIGSNLSgvLYILDEPSIGLhqrDN---NRLISSLKKMRDlGNTLVVVEHDEDTMWAADYLI 558
Cdd:cd03228   97 LSGGQRQRIAIARALLRDPP--ILILDEATSAL---DPeteALILEALRALAK-GKTVIVIAHRLSTIRDADRII 165
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
828-890 1.43e-04

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 44.87  E-value: 1.43e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488923006 828 LSGGEAQRMKLASELhkkANGKNFYILDEPTTGLHTDDIKRLLDVLQRLVDNGNTVLVIEHNL 890
Cdd:PRK15056 143 LSGGQKKRVFLARAI---AQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNL 202
cbiO PRK13646
energy-coupling factor transporter ATPase;
460-588 1.51e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 44.77  E-value: 1.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 460 LKEIKDR-------LNFLRNVgleyltLSRSARTLSGGEAQRIRLATQIGSNLSGVlyILDEPSIGLHQRDNNRLISSLK 532
Cdd:PRK13646 118 LDEVKNYahrllmdLGFSRDV------MSQSPFQMSGGQMRKIAIVSILAMNPDII--VLDEPTAGLDPQSKRQVMRLLK 189
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488923006 533 KMR-DLGNTLVVVEHD-EDTMWAADYLIDIgpgageNGGEVMAAGTPKQVAKSRKSLT 588
Cdd:PRK13646 190 SLQtDENKTIILVSHDmNEVARYADEVIVM------KEGSIVSQTSPKELFKDKKKLA 241
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
622-652 1.77e-04

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: 43.66  E-value: 1.77e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTLVNMV 652
Cdd:cd03259   16 LDDLSLTVEPGEFLALLGPSGCGKTTLLRLI 46
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
826-892 1.80e-04

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 44.15  E-value: 1.80e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488923006 826 TTLSGGEAQRMKLASELhkkANGKNFYILDEPTTGLHTDDIKRLLDVLQRLV-DNGNTVLVIEHNLDV 892
Cdd:PRK11701 150 TTFSGGMQQRLQIARNL---VTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVrELGLAVVIVTHDLAV 214
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
805-901 2.00e-04

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 44.82  E-value: 2.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 805 ARKLQTIIDVGLGYVHLGQSATT----LSGGEAQRMKLASELhkkANGKNFYILDEPTTGLHTDDIKRLLDVLQRLVDNG 880
Cdd:PRK13536 146 TREIEAVIPSLLEFARLESKADArvsdLSGGMKRRLTLARAL---INDPQLLILDEPTTGLDPHARHLIWERLRSLLARG 222
                         90       100
                 ....*....|....*....|.
gi 488923006 881 NTVLVIEHnldVIKTADHLID 901
Cdd:PRK13536 223 KTILLTTH---FMEEAERLCD 240
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
853-898 2.53e-04

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 44.62  E-value: 2.53e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 488923006 853 ILDEPTTGLHTDDIKRLLDVLQRLVDNGNTVLVIEHNLD-VIKTADH 898
Cdd:COG1129  163 ILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDeVFEIADR 209
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
462-580 2.76e-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: 43.48  E-value: 2.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 462 EIKDRLN-FLRNVGLEYLTlSRSARTLSGGEAQRIRLATQIGSNLSgVLyILDEPSIGLHQRDNNRLISSLKKMRD-LGN 539
Cdd:cd03296  112 EIRAKVHeLLKLVQLDWLA-DRYPAQLSGGQRQRVALARALAVEPK-VL-LLDEPFGALDAKVRKELRRWLRRLHDeLHV 188
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 488923006 540 TLVVVEHD-EDTMWAADYLIDIgpgageNGGEVMAAGTPKQV 580
Cdd:cd03296  189 TTVFVTHDqEEALEVADRVVVM------NKGRIEQVGTPDEV 224
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
487-564 2.92e-04

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: 42.59  E-value: 2.92e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488923006 487 LSGGEAQRIRLATQIGSNLSgvLYILDEPSIGLHQrDNNRLISS-LKKMRDLGNTLVVVEHDEDTMWAADYLIDIGPGA 564
Cdd:cd03246   97 LSGGQRQRLGLARALYGNPR--ILVLDEPNSHLDV-EGERALNQaIAALKAAGATRIVIAHRPETLASADRILVLEDGR 172
cbiO PRK13644
energy-coupling factor transporter ATPase;
462-580 2.94e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 43.82  E-value: 2.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 462 EIKDRLNF-LRNVGLEYLTlSRSARTLSGGEAQRIRLATQIgsNLSGVLYILDEPSIGLHQRDNNRLISSLKKMRDLGNT 540
Cdd:PRK13644 112 EIRKRVDRaLAEIGLEKYR-HRSPKTLSGGQGQCVALAGIL--TMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKT 188
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 488923006 541 LVVVEHDEDTMWAADYLIDIgpgageNGGEVMAAGTPKQV 580
Cdd:PRK13644 189 IVYITHNLEELHDADRIIVM------DRGKIVLEGEPENV 222
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
827-900 3.12e-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: 43.04  E-value: 3.12e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488923006 827 TLSGGEAQRMKLASELhkkANGKNFYILDEPTTGLHTDDIKRLLDVLQRLVDNGNTVLVIEHNLD-VIKTADHLI 900
Cdd:cd03269  128 ELSKGNQQKVQFIAAV---IHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMElVEELCDRVL 199
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
828-900 3.37e-04

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: 42.42  E-value: 3.37e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488923006 828 LSGGEAQRMKLASELHKKANgknFYILDEPTTGLhtdDI--KR-LLDVLQRLVDNGNTVLVIEHNLD-VIKTADHLI 900
Cdd:cd03215  105 LSGGNQQKVVLARWLARDPR---VLILDEPTRGV---DVgaKAeIYRLIRELADAGKAVLLISSELDeLLGLCDRIL 175
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
789-902 4.04e-04

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: 42.48  E-value: 4.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 789 MTVEEATDFFAPIPKIARKLQTIIDVGL-GYVHLgqSATTLSGGEAQRMKLASELhkkANGKNFYILDEPTTGLHTDDIK 867
Cdd:cd03231   88 LSVLENLRFWHADHSDEQVEEALARVGLnGFEDR--PVAQLSAGQQRRVALARLL---LSGRPLWILDEPTTALDKAGVA 162
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 488923006 868 RLLDVL-QRLVDNGNTVLVIEHNLDVIKTADHLIDL 902
Cdd:cd03231  163 RFAEAMaGHCARGGMVVLTTHQDLGLSEAGARELDL 198
cbiO PRK13641
energy-coupling factor transporter ATPase;
808-902 4.09e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 43.28  E-value: 4.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 808 LQTIIDVGLGYVHLGQSATTLSGGEAQRMKLASELhkkANGKNFYILDEPTTGLHTDDIKRLLDVLQRLVDNGNTVLVIE 887
Cdd:PRK13641 126 LKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVM---AYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVT 202
                         90
                 ....*....|....*.
gi 488923006 888 HNL-DVIKTADHLIDL 902
Cdd:PRK13641 203 HNMdDVAEYADDVLVL 218
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
511-648 4.16e-04

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 43.89  E-value: 4.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 511 ILDEPSIGLHQRDNNRLISSLKKMRDLGNTLVVVEHDEDTMWA-AD--------YLIDIGPGAGENGGEVMAAGTPKQVA 581
Cdd:PRK15439 163 ILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADrisvmrdgTIALSGKTADLSTDDIIQAITPAARE 242
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488923006 582 ksrKSLTGkylSGKKFIPVPETRRT-GNGQSI-KLKGVQENNLKNIDVDFPLGEFVAVTGVSGSGKSTL 648
Cdd:PRK15439 243 ---KSLSA---SQKLWLELPGNRRQqAAGAPVlTVEDLTGEGFRNISLEVRAGEILGLAGVVGAGRTEL 305
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
622-652 4.18e-04

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: 42.84  E-value: 4.18e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 488923006  622 LKNIDVDFPLGEFVAVTGVSGSGKSTLVNMV 652
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLI 31
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
461-580 4.51e-04

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: 43.74  E-value: 4.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 461 KEIKDRLN-FLRNVGLEYLTLSRSARTLSGGEAQRIRLATQIGSNLSgvLYILDEPSIGL---HQRdnnRLISSLKKMRD 536
Cdd:COG1123  378 AERRERVAeLLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPK--LLILDEPTSALdvsVQA---QILNLLRDLQR 452
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 488923006 537 -LGNTLVVVEHDedtMWAADYLidigpgAGE----NGGEVMAAGTPKQV 580
Cdd:COG1123  453 eLGLTYLFISHD---LAVVRYI------ADRvavmYDGRIVEDGPTEEV 492
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
420-515 4.60e-04

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: 41.48  E-value: 4.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  420 SVKIDGKHI---------AEISALP----IDSAMEFFGNLNFSEQDTAVATPILK-EIKDRLNFLRNVGLEYLTLSRSAR 485
Cdd:pfam00005  41 TILLDGQDLtdderkslrKEIGYVFqdpqLFPRLTVRENLRLGLLLKGLSKREKDaRAEEALEKLGLGDLADRPVGERPG 120
                          90       100       110
                  ....*....|....*....|....*....|
gi 488923006  486 TLSGGEAQRIRLAtqIGSNLSGVLYILDEP 515
Cdd:pfam00005 121 TLSGGQRQRVAIA--RALLTKPKLLLLDEP 148
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
827-900 4.73e-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: 42.52  E-value: 4.73e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488923006 827 TLSGGEAQRMKLASEL--HKKAngknfYILDEPTTGLHTDDIKRLLDVLQRLVDNGNTVLVIEHNLDVI-KTADHLI 900
Cdd:cd03262  135 QLSGGQQQRVAIARALamNPKV-----MLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFArEVADRVI 206
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
622-649 5.28e-04

ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213223 [Multi-domain]  Cd Length: 241  Bit Score: 42.56  E-value: 5.28e-04
                         10        20
                 ....*....|....*....|....*...
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTLV 649
Cdd:cd03256   17 LKDVSLSINPGEFVALIGPSGAGKSTLL 44
cbiO PRK13640
energy-coupling factor transporter ATPase;
828-902 5.33e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 42.86  E-value: 5.33e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488923006 828 LSGGEAQRMKLASELhkkANGKNFYILDEPTTGLHTDDIKRLLDVLQRL-VDNGNTVLVIEHNLDVIKTADHLIDL 902
Cdd:PRK13640 144 LSGGQKQRVAIAGIL---AVEPKIIILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEANMADQVLVL 216
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
16-43 5.87e-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: 41.60  E-value: 5.87e-04
                         10        20
                 ....*....|....*....|....*...
gi 488923006  16 LKNIDVTIPRDKLVVVTGLSGSGKSSLA 43
Cdd:cd03228   18 LKDVSLTIKPGEKVAIVGPSGSGKSTLL 45
cbiO PRK13643
energy-coupling factor transporter ATPase;
470-580 5.88e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 42.80  E-value: 5.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 470 LRNVGLEYLTLSRSARTLSGGEAQRIRLATQIGsnLSGVLYILDEPSIGLHQRDNNRLISSLKKMRDLGNTLVVVEH-DE 548
Cdd:PRK13643 128 LEMVGLADEFWEKSPFELSGGQMRRVAIAGILA--MEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHlMD 205
                         90       100       110
                 ....*....|....*....|....*....|..
gi 488923006 549 DTMWAADYLIDIgpgageNGGEVMAAGTPKQV 580
Cdd:PRK13643 206 DVADYADYVYLL------EKGHIISCGTPSDV 231
cbiO PRK13649
energy-coupling factor transporter ATPase;
470-580 5.89e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 42.81  E-value: 5.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 470 LRNVGLEYLTLSRSARTLSGGEAQRIRLATQIGSNLSgvLYILDEPSIGLHQRDNNRLISSLKKMRDLGNTLVVVEH-DE 548
Cdd:PRK13649 129 LALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPK--ILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHlMD 206
                         90       100       110
                 ....*....|....*....|....*....|..
gi 488923006 549 DTMWAADYLIDIgpgageNGGEVMAAGTPKQV 580
Cdd:PRK13649 207 DVANYADFVYVL------EKGKLVLSGKPKDI 232
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
828-898 5.92e-04

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: 43.52  E-value: 5.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 828 LSGGEAQR----MKLASE---LhkkangknfyILDEPTTGLhtD-----DIKRLLDVLQRlvDNGNTVLVIEHNLDVI-K 894
Cdd:COG4172  157 LSGGQRQRvmiaMALANEpdlL----------IADEPTTAL--DvtvqaQILDLLKDLQR--ELGMALLLITHDLGVVrR 222

                 ....
gi 488923006 895 TADH 898
Cdd:COG4172  223 FADR 226
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
828-891 5.95e-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: 42.35  E-value: 5.95e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488923006 828 LSGGEAQRMKLASEL-HKKANgknfYILDEPTTGLHTDDIKRLLDVLQRLVDNGNTVLVIEHNLD 891
Cdd:cd03266  137 FSTGMRQKVAIARALvHDPPV----LLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQ 197
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
14-42 6.06e-04

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 41.46  E-value: 6.06e-04
                         10        20
                 ....*....|....*....|....*....
gi 488923006  14 HNLKNIDVTIPRDKLVVVTGLSGSGKSSL 42
Cdd:cd00267   13 TALDNVSLTLKAGEIVALVGPNGSGKSTL 41
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
461-549 6.22e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 42.77  E-value: 6.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 461 KEIKDR-LNFLRNVGLEYLTLSRSARTLSGGEAQRIRLAtqigsnlsGVL------YILDEPSIGLHQRDNNRLISSLKK 533
Cdd:PRK13651 139 EEAKKRaAKYIELVGLDESYLQRSPFELSGGQKRRVALA--------GILamepdfLVFDEPTAGLDPQGVKEILEIFDN 210
                         90
                 ....*....|....*.
gi 488923006 534 MRDLGNTLVVVEHDED 549
Cdd:PRK13651 211 LNKQGKTIILVTHDLD 226
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
622-652 7.02e-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: 7.02e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTLVNMV 652
Cdd:COG4778   27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCI 57
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
611-652 7.11e-04

sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 42.91  E-value: 7.11e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 488923006 611 SIKLKGVQ---ENN---LKNIDVDFPLGEFVAVTGVSGSGKSTLVNMV 652
Cdd:PRK11650   3 GLKLQAVRksyDGKtqvIKGIDLDVADGEFIVLVGPSGCGKSTLLRMV 50
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
474-546 7.20e-04

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 43.29  E-value: 7.20e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488923006 474 GLEYLTLSRSARtLSGGEAQRIRLATQIGSNlsGVLYILDEPSIGLHQRDNNRLISSLKKMRdLGNTLVVVEH 546
Cdd:PRK11174 474 GLDTPIGDQAAG-LSVGQAQRLALARALLQP--CQLLLLDEPTASLDAHSEQLVMQALNAAS-RRQTTLMVTH 542
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
821-902 7.70e-04

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 42.01  E-value: 7.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 821 LGQSATTLSGGEAQRMKLASELHkkangknFY----ILDEPTTGLHTDDIKRLLDVLQRLV-DNGNTVLVIEHNLDVIKT 895
Cdd:PRK10247 131 LTKNIAELSGGEKQRISLIRNLQ-------FMpkvlLLDEITSALDESNKHNVNEIIHRYVrEQNIAVLWVTHDKDEINH 203

                 ....*..
gi 488923006 896 ADHLIDL 902
Cdd:PRK10247 204 ADKVITL 210
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
16-43 7.81e-04

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: 41.68  E-value: 7.81e-04
                         10        20
                 ....*....|....*....|....*...
gi 488923006  16 LKNIDVTIPRDKLVVVTGLSGSGKSSLA 43
Cdd:cd03225   17 LDDISLTIKKGEFVLIVGPNGSGKSTLL 44
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
626-652 7.87e-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: 41.71  E-value: 7.87e-04
                         10        20
                 ....*....|....*....|....*..
gi 488923006 626 DVDFPLGEFVAVTGVSGSGKSTLVNMV 652
Cdd:cd03298   18 DLTFAQGEITAIVGPSGSGKSTLLNLI 44
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
622-652 8.08e-04

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 42.38  E-value: 8.08e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTLVNMV 652
Cdd:COG1101   22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAI 52
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
827-902 8.71e-04

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 43.13  E-value: 8.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 827 TLSGGEAQRMKLASELHKKAngkNFYILDEPTTGLhtdDIKrLLDVLQRLVDN--GnTVLVIEHN---LDviKTADHLID 901
Cdd:COG0488  432 VLSGGEKARLALAKLLLSPP---NVLLLDEPTNHL---DIE-TLEALEEALDDfpG-TVLLVSHDryfLD--RVATRILE 501

                 .
gi 488923006 902 L 902
Cdd:COG0488  502 F 502
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
622-648 9.04e-04

ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440744 [Multi-domain]  Cd Length: 241  Bit Score: 41.89  E-value: 9.04e-04
                         10        20
                 ....*....|....*....|....*..
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTL 648
Cdd:COG1127   21 LDGVSLDVPRGEILAIIGGSGSGKSVL 47
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
443-580 9.39e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 42.37  E-value: 9.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 443 FG--NLNFSEQDtavatpILKEIKDRLnflRNVGLEYLTlSRSARTLSGGEAQRIRLATQIGSNLSgvLYILDEPSIGLH 520
Cdd:PRK13639 102 FGplNLGLSKEE------VEKRVKEAL---KAVGMEGFE-NKPPHHLSGGQKKRVAIAGILAMKPE--IIVLDEPTSGLD 169
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488923006 521 QRDNNRLISSLKKMRDLGNTLVVVEHDED--TMWAAD-YLIdigpgageNGGEVMAAGTPKQV 580
Cdd:PRK13639 170 PMGASQIMKLLYDLNKEGITIIISTHDVDlvPVYADKvYVM--------SDGKIIKEGTPKEV 224
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
485-580 9.50e-04

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: 42.90  E-value: 9.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 485 RTLSGGEAQRIRLATQIGSNlSGVLyILDEPSIGLHQRDNNRLISSLKKMRDlGNTLVVVEHDEDTMWAADYLIDIgpga 564
Cdd:COG2274  610 SNLSGGQRQRLAIARALLRN-PRIL-ILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIRLADRIIVL---- 682
                         90
                 ....*....|....*.
gi 488923006 565 geNGGEVMAAGTPKQV 580
Cdd:COG2274  683 --DKGRIVEDGTHEEL 696
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
487-548 1.09e-03

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 41.69  E-value: 1.09e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488923006 487 LSGGEAQRIRLATQIgSNLSGVLYIlDEPSIGLHQRDNNRLISSLKKM-RDLGNTLVVVEHDE 548
Cdd:PRK10584 147 LSGGEQQRVALARAF-NGRPDVLFA-DEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDL 207
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
461-549 1.13e-03

ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.


Pssm-ID: 213222 [Multi-domain]  Cd Length: 218  Bit Score: 41.32  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 461 KEIKDR-LNFLRNVGLEYLtLSRSARTLSGGEAQRIRLATQIGSNLSGVLyiLDEPSIGLHQRDNNRLISSLKKM-RDLG 538
Cdd:cd03255  115 KERRERaEELLERVGLGDR-LNHYPSELSGGQQQRVAIARALANDPKIIL--ADEPTGNLDSETGKEVMELLRELnKEAG 191
                         90
                 ....*....|.
gi 488923006 539 NTLVVVEHDED 549
Cdd:cd03255  192 TTIVVVTHDPE 202
ABC_sbcCD cd03279
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ...
480-549 1.19e-03

ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.


Pssm-ID: 213246 [Multi-domain]  Cd Length: 213  Bit Score: 41.49  E-value: 1.19e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488923006 480 LSRSARTLSGGE------AQRIRLATQIGSNLSGVL--YILDEPSIGLHQRDNNRLISSLKKMRDLGNTLVVVEHDED 549
Cdd:cd03279  117 LARPVSTLSGGEtflaslSLALALSEVLQNRGGARLeaLFIDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEE 194
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
828-900 1.25e-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: 40.76  E-value: 1.25e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488923006 828 LSGGEAQRMKLASELHKKANgknFYILDEPTTGLHTDDIKRLLDVLQRLVDNgNTVLVIEHNLDVIKTADHLI 900
Cdd:cd03247   99 FSGGERQRLALARILLQDAP---IVLLDEPTVGLDPITERQLLSLIFEVLKD-KTLIWITHHLTGIEHMDKIL 167
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
511-558 1.26e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 1.26e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 488923006 511 ILDEPSIGLHQRDNNRLISSLKKMRDLG-NTLVVVEHDEDTMWAADYLI 558
Cdd:PRK02224 816 ILDEPTVFLDSGHVSQLVDLVESMRRLGvEQIVVVSHDDELVGAADDLV 864
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
622-654 1.30e-03

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: 40.63  E-value: 1.30e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTLVNMVLK 654
Cdd:cd03229   16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAG 48
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
467-566 1.31e-03

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 41.24  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 467 LNFLRNVGLEYLTLSRSARTLSGGEAQRIRLATQIgSNLSGVLyILDEPSIGL--HQRDN-NRLISSLkkMRDLGNTLVV 543
Cdd:PRK10247 118 LDDLERFALPDTILTKNIAELSGGEKQRISLIRNL-QFMPKVL-LLDEITSALdeSNKHNvNEIIHRY--VREQNIAVLW 193
                         90       100
                 ....*....|....*....|...
gi 488923006 544 VEHDEDTMWAADYLIDIGPGAGE 566
Cdd:PRK10247 194 VTHDKDEINHADKVITLQPHAGE 216
CP_lyasePhnL TIGR02324
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ...
486-562 1.31e-03

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


Pssm-ID: 131377 [Multi-domain]  Cd Length: 224  Bit Score: 41.22  E-value: 1.31e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488923006  486 TLSGGEAQRIRLATQIGSNLSGVLyiLDEPSIGLHQRDNNRLISSLKKMRDLGNTLVVVEHDEDTMWA-ADYLIDIGP 562
Cdd:TIGR02324 149 TFSGGEQQRVNIARGFIADYPILL--LDEPTASLDAANRQVVVELIAEAKARGAALIGIFHDEEVRELvADRVMDVTP 224
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
474-549 1.39e-03

The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.


Pssm-ID: 213268 [Multi-domain]  Cd Length: 213  Bit Score: 41.09  E-value: 1.39e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488923006 474 GLEYLtLSRSARTLSGGEAQRIRLATQIGSNLSgvLYILDEPSIGLHQRDNNRLISSLKKM-RDLGNTLVVVEHDED 549
Cdd:cd03301  119 QIEHL-LDRKPKQLSGGQRQRVALGRAIVREPK--VFLMDEPLSNLDAKLRVQMRAELKRLqQRLGTTTIYVTHDQV 192
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
622-652 1.43e-03

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 41.22  E-value: 1.43e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTLVNMV 652
Cdd:COG1134   42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLI 72
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
461-584 1.45e-03

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: 41.38  E-value: 1.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 461 KEIKDRL-NFLRNVGLEyLTLSRSARTLSGGEAQRIRLATQIGSNLSgvLYILDEPSIGLHQRDNNRLISSLKKMRDLGN 539
Cdd:COG4555  107 EELKKRIeELIELLGLE-EFLDRRVGELSTGMKKKVALARALVHDPK--VLLLDEPTNGLDVMARRLLREILRALKKEGK 183
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 488923006 540 TLVVVEHDEDTMWA-ADYLIDIgpgageNGGEVMAAGTPKQVAKSR 584
Cdd:COG4555  184 TVLFSSHIMQEVEAlCDRVVIL------HKGKVVAQGSLDELREEI 223
cbiO PRK13637
energy-coupling factor transporter ATPase;
814-900 1.56e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 41.57  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 814 VGLGY-VHLGQSATTLSGGEAQRMKLASELhkkANGKNFYILDEPTTGLH---TDDIKRLLDVLQRlvDNGNTVLVIEHN 889
Cdd:PRK13637 130 VGLDYeDYKDKSPFELSGGQKRRVAIAGVV---AMEPKILILDEPTAGLDpkgRDEILNKIKELHK--EYNMTIILVSHS 204
                         90
                 ....*....|..
gi 488923006 890 L-DVIKTADHLI 900
Cdd:PRK13637 205 MeDVAKLADRII 216
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
487-601 1.62e-03

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 41.29  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 487 LSGGEAQRIRLATQIGsnLSGVLYILDEPSIGlhqRDN------NRLISSLKKMrdLGNTLVVVEHD-EDTMWAADYLID 559
Cdd:PRK11831 144 LSGGMARRAALARAIA--LEPDLIMFDEPFVG---QDPitmgvlVKLISELNSA--LGVTCVVVSHDvPEVLSIADHAYI 216
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 488923006 560 IGpgagenGGEVMAAGTPKQVAKSRKSLTGKYLSGKKFIPVP 601
Cdd:PRK11831 217 VA------DKKIVAHGSAQALQANPDPRVRQFLDGIADGPVP 252
cbiO PRK13646
energy-coupling factor transporter ATPase;
789-900 1.65e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 41.69  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 789 MTVEEATDffapipkiaRKLQTIIDVGLGYVHLGQSATTLSGGEAQRMKLASELhkkANGKNFYILDEPTTGL---HTDD 865
Cdd:PRK13646 116 MNLDEVKN---------YAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSIL---AMNPDIIVLDEPTAGLdpqSKRQ 183
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 488923006 866 IKRLLDVLQrlVDNGNTVLVIEHNL-DVIKTADHLI 900
Cdd:PRK13646 184 VMRLLKSLQ--TDENKTIILVSHDMnEVARYADEVI 217
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
461-582 1.71e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 41.23  E-value: 1.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 461 KEIKDRL-NFLRNVGL-EYltlSRSA-RTLSGGEAQRIRLAtqigsnlsGVL------YILDEPSIGLHQRDNNRLISSL 531
Cdd:PRK13633 119 EEIRERVdESLKKVGMyEY---RRHApHLLSGGQKQRVAIA--------GILamrpecIIFDEPTAMLDPSGRREVVNTI 187
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488923006 532 KKM-RDLGNTLVVVEHDEDTMWAADYLIDIgpgageNGGEVMAAGTPKQVAK 582
Cdd:PRK13633 188 KELnKKYGITIILITHYMEEAVEADRIIVM------DSGKVVMEGTPKEIFK 233
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
16-43 1.72e-03

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 39.94  E-value: 1.72e-03
                          10        20
                  ....*....|....*....|....*...
gi 488923006   16 LKNIDVTIPRDKLVVVTGLSGSGKSSLA 43
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLL 28
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
484-548 1.73e-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: 41.96  E-value: 1.73e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488923006  484 ARTLSGGEAQRIRLATQIgsnLSGV-LYILDEPSIGLHQRDNNRLISSLKKMRDlGNTLVVVEHDE 548
Cdd:TIGR02868 469 GARLSGGERQRLALARAL---LADApILLLDEPTEHLDAETADELLEDLLAALS-GRTVVLITHHL 530
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
828-893 1.95e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 41.33  E-value: 1.95e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488923006 828 LSGGEAQRMKLASELhkkANGKNFYILDEPTTGLHTDDIKRLLDVLQRLVDN-GNTVLVIEHNLDVI 893
Cdd:PRK13652 138 LSGGEKKRVAIAGVI---AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLV 201
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
485-546 2.04e-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: 39.99  E-value: 2.04e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488923006 485 RTLSGGEAQRIRLATQIGSNLSgvLYILDEPSIGLHQRDNNRLISSLKKMRDlGNTLVVVEH 546
Cdd:cd03247   97 RRFSGGERQRLALARILLQDAP--IVLLDEPTVGLDPITERQLLSLIFEVLK-DKTLIWITH 155
PLN03211 PLN03211
ABC transporter G-25; Provisional
485-546 2.07e-03

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 41.79  E-value: 2.07e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488923006 485 RTLSGGEAQRIRLATQIGSNLSgvLYILDEPSIGLHQRDNNRLISSLKKMRDLGNTLVVVEH 546
Cdd:PLN03211 205 RGISGGERKRVSIAHEMLINPS--LLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
789-895 2.32e-03

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: 40.78  E-value: 2.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 789 MTVEEATDF-----FAPIPKIARKLQTIIDVgLGYVH-LGQSATTLSGGEAQRMKLASELHKKAngkNFYILDEPTTGLH 862
Cdd:cd03299   86 MTVYKNIAYglkkrKVDKKEIERKVLEIAEM-LGIDHlLNRKPETLSGGEQQRVAIARALVVNP---KILLLDEPFSALD 161
                         90       100       110
                 ....*....|....*....|....*....|....
gi 488923006 863 TDDIKRLLDVLQRLVDN-GNTVLVIEHNLDVIKT 895
Cdd:cd03299  162 VRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWA 195
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
828-888 2.35e-03

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 41.86  E-value: 2.35e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488923006 828 LSGGEAQRMKLASELHKKANgknFYILDEPTTGLhtdDIKRlLDVLQRLVDN-GNTVLVIEH 888
Cdd:PRK11147 441 LSGGERNRLLLARLFLKPSN---LLILDEPTNDL---DVET-LELLEELLDSyQGTVLLVSH 495
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
622-651 2.37e-03

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 41.63  E-value: 2.37e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTLVNM 651
Cdd:PRK10535  24 LKGISLDIYAGEMVAIVGASGSGKSTLMNI 53
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
782-890 2.56e-03

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 41.35  E-value: 2.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 782 TIADILDMTVEEATDffapipkiARKLQTIIDVGLGYV---------HLGQSATTLSGGEAQRMKLASELHKKANgknFY 852
Cdd:PRK11160 429 TLRDNLLLAAPNASD--------EALIEVLQQVGLEKLleddkglnaWLGEGGRQLSGGEQRRLGIARALLHDAP---LL 497
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 488923006 853 ILDEPTTGLHTDDIKRLLDVLQRLVDNgNTVLVIEHNL 890
Cdd:PRK11160 498 LLDEPTEGLDAETERQILELLAEHAQN-KTVLMITHRL 534
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
828-894 2.62e-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: 41.35  E-value: 2.62e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488923006  828 LSGGEAQRMKLASELHKKANgknFYILDEPTTGLHTDDIKRLLDVLQRLVDNGNTVLVIEHNLDVIK 894
Cdd:TIGR02633 142 YGGGQQQLVEIAKALNKQAR---LLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVK 205
cbiO PRK13649
energy-coupling factor transporter ATPase;
814-891 2.94e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 40.50  E-value: 2.94e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488923006 814 VGLGYVHLGQSATTLSGGEAQRMKLASELhkkANGKNFYILDEPTTGLHTDDIKRLLDVLQRLVDNGNTVLVIEHNLD 891
Cdd:PRK13649 132 VGISESLFEKNPFELSGGQMRRVAIAGIL---AMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMD 206
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
470-595 2.95e-03

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 40.42  E-value: 2.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 470 LRNVGL---EYLTLSRSARTLSGGEAQRIRLATQIGsnLSGVLYILDEPSIGL---HQRDNNRLISSLKKMRdlgnTLVV 543
Cdd:PRK14246 134 LRKVGLwkeVYDRLNSPASQLSGGQQQRLTIARALA--LKPKVLLMDEPTSMIdivNSQAIEKLITELKNEI----AIVI 207
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488923006 544 VEHD-EDTMWAADYLidigpgAGENGGEVMAAGTPKQVAKSRKS-LTGKYLSGK 595
Cdd:PRK14246 208 VSHNpQQVARVADYV------AFLYNGELVEWGSSNEIFTSPKNeLTEKYVIGR 255
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
622-652 2.98e-03

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 40.90  E-value: 2.98e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTLVNMV 652
Cdd:COG1118   18 LDDVSLEIASGELVALLGPSGSGKTTLLRII 48
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
622-665 3.02e-03

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 40.84  E-value: 3.02e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTLVnmvlkRVLAQKLNHNS 665
Cdd:PRK10851  18 LNDISLDIPSGQMVALLGPSGSGKTTLL-----RIIAGLEHQTS 56
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
803-888 3.05e-03

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 40.46  E-value: 3.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 803 KIARKLqtiidvgLGYVHLGQSA----TTLSGGEAQRMKLASELHKKANgknFYILDEPTTGLHTDDIKRLLDVLQRLVD 878
Cdd:PRK09493 115 KQAREL-------LAKVGLAERAhhypSELSGGQQQRVAIARALAVKPK---LMLFDEPTSALDPELRHEVLKVMQDLAE 184
                         90
                 ....*....|
gi 488923006 879 NGNTVLVIEH 888
Cdd:PRK09493 185 EGMTMVIVTH 194
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
807-900 3.08e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 40.74  E-value: 3.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 807 KLQTIID-----VGLGYvHLGQSATTLSGGEAQRMKLASELhkkANGKNFYILDEPTTGLH---TDDIKRLLDVLQRlvD 878
Cdd:PRK13632 118 KMKDIIDdlakkVGMED-YLDKEPQNLSGGQKQRVAIASVL---ALNPEIIIFDESTSMLDpkgKREIKKIMVDLRK--T 191
                         90       100
                 ....*....|....*....|..
gi 488923006 879 NGNTVLVIEHNLDVIKTADHLI 900
Cdd:PRK13632 192 RKKTLISITHDMDEAILADKVI 213
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
827-902 3.13e-03

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).


Pssm-ID: 213190 [Multi-domain]  Cd Length: 166  Bit Score: 39.44  E-value: 3.13e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488923006 827 TLSGGEAQRMKLASE-LHKKAngknFYILDEPTTGLHTDDIKRLLDVLQRLvdnGNTVLVIEHNLDVIKTADHLIDL 902
Cdd:cd03223   91 VLSGGEQQRLAFARLlLHKPK----FVFLDEATSALDEESEDRLYQLLKEL---GITVISVGHRPSLWKFHDRVLDL 160
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
821-900 3.18e-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: 3.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 821 LGQSATTLSGGeaQRMK---LASELHKKangkNFYILDEPTTGLHT---DDIKRLLDVLQRlvDNGNTVLVIEHNL-DVI 893
Cdd:cd03267  147 LDTPVRQLSLG--QRMRaeiAAALLHEP----EILFLDEPTIGLDVvaqENIRNFLKEYNR--ERGTTVLLTSHYMkDIE 218

                 ....*..
gi 488923006 894 KTADHLI 900
Cdd:cd03267  219 ALARRVL 225
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
611-658 3.28e-03

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: 40.40  E-value: 3.28e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488923006 611 SIKLKGVQEN-----NLKNIDVDFPLGEFVAVTGVSGSGKSTLVnmvlkRVLA 658
Cdd:cd03296    2 SIEVRNVSKRfgdfvALDDVSLDIPSGELVALLGPSGSGKTTLL-----RLIA 49
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
486-564 3.37e-03

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];


Pssm-ID: 443809 [Multi-domain]  Cd Length: 229  Bit Score: 40.11  E-value: 3.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 486 TLSGGEAQRIRLAtqigsnlSGV-----LYILDEPSIGLHQRDNNRLISSLKKMRDLGNTLVVVEHDEDTMWA-ADYLID 559
Cdd:COG4778  152 TFSGGEQQRVNIA-------RGFiadppLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAvADRVVD 224

                 ....*
gi 488923006 560 IGPGA 564
Cdd:COG4778  225 VTPFS 229
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
788-900 3.38e-03

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: 40.18  E-value: 3.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 788 DMTVEEATDFF---------APIPKIAR-KLQTiidVGL-GYVHL--GQsattLSGGEAQRMKLASELhkkANGKNFYIL 854
Cdd:cd03261   91 SLTVFENVAFPlrehtrlseEEIREIVLeKLEA---VGLrGAEDLypAE----LSGGMKKRVALARAL---ALDPELLLY 160
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 488923006 855 DEPTTGLH---TDDIKRLLDVLQRLvdNGNTVLVIEHNLD-VIKTADHLI 900
Cdd:cd03261  161 DEPTAGLDpiaSGVIDDLIRSLKKE--LGLTSIMVTHDLDtAFAIADRIA 208
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
623-652 3.38e-03

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 40.78  E-value: 3.38e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 488923006 623 KNIDVDFPLGEFVAVTGVSGSGKSTLVNMV 652
Cdd:PRK11000  20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMI 49
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
622-652 3.59e-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: 39.91  E-value: 3.59e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTLVNMV 652
Cdd:cd03300   16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLI 46
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
461-592 3.74e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 40.22  E-value: 3.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 461 KEIKDRL-NFLRNVGLEYLTlSRSARTLSGGEAQRIRLAtqigsnlsGVL------YILDEPSIGLHQRDNNRLISSLKK 533
Cdd:PRK13636 116 DEVRKRVdNALKRTGIEHLK-DKPTHCLSFGQKKRVAIA--------GVLvmepkvLVLDEPTAGLDPMGVSEIMKLLVE 186
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488923006 534 M-RDLGNTLVVVEHDedtmwaadylIDIGPGAGENG-----GEVMAAGTPKQVAKSRKSLTGKYL 592
Cdd:PRK13636 187 MqKELGLTIIIATHD----------IDIVPLYCDNVfvmkeGRVILQGNPKEVFAEKEMLRKVNL 241
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
626-659 4.07e-03

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 39.91  E-value: 4.07e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 488923006 626 DVDFPL--GEFVAVTGVSGSGKSTLVNMVLKRVLAQ 659
Cdd:PRK11701  24 DVSFDLypGEVLGIVGESGSGKTTLLNALSARLAPD 59
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
622-648 4.27e-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: 40.96  E-value: 4.27e-03
                         10        20
                 ....*....|....*....|....*..
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTL 648
Cdd:COG5265  374 LKGVSFEVPAGKTVAIVGPSGAGKSTL 400
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
789-889 4.43e-03

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 39.47  E-value: 4.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 789 MTVEEATDFFAPI-----PKIARklqTIIDVGLGYV-HLgqSATTLSGGEAQRMKLASELhkkANGKNFYILDEPTTGLH 862
Cdd:PRK13539  88 LTVAENLEFWAAFlggeeLDIAA---ALEAVGLAPLaHL--PFGYLSAGQKRRVALARLL---VSNRPIWILDEPTAALD 159
                         90       100
                 ....*....|....*....|....*..
gi 488923006 863 TDDIKRLLDVLQRLVDNGNTVLVIEHN 889
Cdd:PRK13539 160 AAAVALFAELIRAHLAQGGIVIAATHI 186
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
16-43 4.80e-03

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: 40.59  E-value: 4.80e-03
                         10        20
                 ....*....|....*....|....*...
gi 488923006  16 LKNIDVTIPRDKLVVVTGLSGSGKSSLA 43
Cdd:COG2274  491 LDNISLTIKPGERVAIVGRSGSGKSTLL 518
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
16-42 4.88e-03

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 39.65  E-value: 4.88e-03
                         10        20
                 ....*....|....*....|....*..
gi 488923006  16 LKNIDVTIPRDKLVVVTGLSGSGKSSL 42
Cdd:COG2884   18 LSDVSLEIEKGEFVFLTGPSGAGKSTL 44
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
814-897 4.97e-03

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 40.42  E-value: 4.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 814 VGLGYVHLGQSATTLSGGEAQRMKLASELhkKANGKnFYILDEPTTGLHT---DDIKRLldvLQRLVDNGNTVLVIEHNL 890
Cdd:PRK15439 390 LNIKFNHAEQAARTLSGGNQQKVLIAKCL--EASPQ-LLIVDEPTRGVDVsarNDIYQL---IRSIAAQNVAVLFISSDL 463

                 ....*...
gi 488923006 891 D-VIKTAD 897
Cdd:PRK15439 464 EeIEQMAD 471
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
612-648 5.02e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 39.97  E-value: 5.02e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 488923006 612 IKLKGV------QENN-LKNIDVDFPLGEFVAVTGVSGSGKSTL 648
Cdd:PRK13632   8 IKVENVsfsypnSENNaLKNVSFEINEGEYVAILGHNGSGKSTI 51
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
470-546 5.04e-03

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 40.58  E-value: 5.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 470 LRNVGLEYLT---------LSRSARTLSGGEAQRIRLATQIGSNlsGVLYILDEPSIGLhQRDNNRLISSL--KKMRDlg 538
Cdd:PRK11160 450 LQQVGLEKLLeddkglnawLGEGGRQLSGGEQRRLGIARALLHD--APLLLLDEPTEGL-DAETERQILELlaEHAQN-- 524

                 ....*...
gi 488923006 539 NTLVVVEH 546
Cdd:PRK11160 525 KTVLMITH 532
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
622-658 5.46e-03

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 40.56  E-value: 5.46e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTLVnmvlkRVLA 658
Cdd:COG4178  379 LEDLSLSLKPGERLLITGPSGSGKSTLL-----RAIA 410
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
822-900 6.02e-03

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 40.48  E-value: 6.02e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488923006  822 GQSATTLSGGEAQRMKLASELHKKANgknFYILDEPTTGLHTDdIKRLLDVLQRLvdNGNTVLVIEHNLDVIKTADHLI 900
Cdd:TIGR00958 612 GEKGSQLSGGQKQRIAIARALVRKPR---VLILDEATSALDAE-CEQLLQESRSR--ASRTVLLIAHRLSTVERADQIL 684
cbiO PRK13643
energy-coupling factor transporter ATPase;
805-899 6.68e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 39.72  E-value: 6.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 805 ARKLQTiidVGLGYVHLGQSATTLSGGEAQRMKLASELhkkANGKNFYILDEPTTGLHTDDIKRLLDVLQRLVDNGNTVL 884
Cdd:PRK13643 125 AEKLEM---VGLADEFWEKSPFELSGGQMRRVAIAGIL---AMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVV 198
                         90
                 ....*....|....*.
gi 488923006 885 VIEHNL-DVIKTADHL 899
Cdd:PRK13643 199 LVTHLMdDVADYADYV 214
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
16-42 6.75e-03

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 39.26  E-value: 6.75e-03
                         10        20
                 ....*....|....*....|....*..
gi 488923006  16 LKNIDVTIPRDKLVVVTGLSGSGKSSL 42
Cdd:COG1136   24 LRGVSLSIEAGEFVAIVGPSGSGKSTL 50
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
462-560 6.83e-03

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: 40.15  E-value: 6.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 462 EIKDRLnflrnvGLEYLtLSRSARTLSGGEAQRirLAtqIGSNLS--GVLYILDEPSIGL--HQRDN-NRLISSLkkMRD 536
Cdd:COG1245  438 EIIKPL------GLEKL-LDKNVKDLSGGELQR--VA--IAACLSrdADLYLLDEPSAHLdvEQRLAvAKAIRRF--AEN 504
                         90       100
                 ....*....|....*....|....
gi 488923006 537 LGNTLVVVEHDEdtmwaadYLIDI 560
Cdd:COG1245  505 RGKTAMVVDHDI-------YLIDY 521
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
828-894 7.04e-03

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 40.07  E-value: 7.04e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 828 LSGGEAQRMKLASELHKKAngkNFYILDEPTTGLHTD---DIKRLLDVLQRLVDNGntVLVIEHNLDVIK 894
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRP---ELLIADEPTTALDVSvqaQILQLLRELQQELNMG--LLFITHNLSIVR 221
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
622-648 7.14e-03

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: 39.02  E-value: 7.14e-03
                         10        20
                 ....*....|....*....|....*..
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTL 648
Cdd:cd03261   16 LKGVDLDVRRGEILAIIGPSGSGKSTL 42
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
16-42 7.28e-03

ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.


Pssm-ID: 213222 [Multi-domain]  Cd Length: 218  Bit Score: 39.01  E-value: 7.28e-03
                         10        20
                 ....*....|....*....|....*..
gi 488923006  16 LKNIDVTIPRDKLVVVTGLSGSGKSSL 42
Cdd:cd03255   20 LKGVSLSIEKGEFVAIVGPSGSGKSTL 46
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
622-652 7.29e-03

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: 39.21  E-value: 7.29e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTLVNMV 652
Cdd:cd03295   17 VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMI 47
cbiO PRK13650
energy-coupling factor transporter ATPase;
460-580 7.54e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 39.33  E-value: 7.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 460 LKEIKDRLN-FLRNVGLEYLTLSRSARtLSGGEAQRIRLATQIGsnLSGVLYILDEPSIGLHQRDNNRLISSLKKMRD-L 537
Cdd:PRK13650 114 HEEMKERVNeALELVGMQDFKEREPAR-LSGGQKQRVAIAGAVA--MRPKIIILDEATSMLDPEGRLELIKTIKGIRDdY 190
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 488923006 538 GNTLVVVEHDEDTMWAADYLIDIgpgageNGGEVMAAGTPKQV 580
Cdd:PRK13650 191 QMTVISITHDLDEVALSDRVLVM------KNGQVESTSTPREL 227
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
827-902 7.81e-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: 39.30  E-value: 7.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 827 TLSGGEAQRMKLA------SELhkkangknfYILDEPTTGLhtDDIKR--LLDVLQRLVDNGNTVLV-IEHNL-DVIKTA 896
Cdd:COG1119  142 TLSQGEQRRVLIAralvkdPEL---------LILDEPTAGL--DLGARelLLALLDKLAAEGAPTLVlVTHHVeEIPPGI 210

                 ....*.
gi 488923006 897 DHLIDL 902
Cdd:COG1119  211 THVLLL 216
PLN03211 PLN03211
ABC transporter G-25; Provisional
828-888 8.17e-03

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 39.86  E-value: 8.17e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488923006 828 LSGGEAQRMKLASELhkkANGKNFYILDEPTTGLHTDDIKRLLDVLQRLVDNGNTVLVIEH 888
Cdd:PLN03211 207 ISGGERKRVSIAHEM---LINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
462-580 8.18e-03

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 39.55  E-value: 8.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 462 EIKDR-LNFLRNVGLEYLTlSRSARTLSGGEAQRIRLATQIgSNLSGVLyILDEPSIGLHQRDNNRLISSLKKM-RDLGN 539
Cdd:PRK09452 120 EITPRvMEALRMVQLEEFA-QRKPHQLSGGQQQRVAIARAV-VNKPKVL-LLDESLSALDYKLRKQMQNELKALqRKLGI 196
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 488923006 540 TLVVVEHDED---TMwaADYLIDIgpgageNGGEVMAAGTPKQV 580
Cdd:PRK09452 197 TFVFVTHDQEealTM--SDRIVVM------RDGRIEQDGTPREI 232
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
596-652 8.33e-03

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 39.87  E-value: 8.33e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488923006 596 KFIPVPETRRTGNGQSIKLK--------GVQENNLKNIDVDFPLGEFVAVTGVSGSGKSTLVNMV 652
Cdd:PRK13545   6 KFEHVTKKYKMYNKPFDKLKdlffrskdGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLI 70
PTZ00243 PTZ00243
ABC transporter; Provisional
16-42 8.40e-03

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 40.15  E-value: 8.40e-03
                          10        20
                  ....*....|....*....|....*..
gi 488923006   16 LKNIDVTIPRDKLVVVTGLSGSGKSSL 42
Cdd:PTZ00243  676 LRDVSVSVPRGKLTVVLGATGSGKSTL 702
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
625-652 8.62e-03

ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 443319 [Multi-domain]  Cd Length: 358  Bit Score: 39.31  E-value: 8.62e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 488923006 625 IDVDF--PLGEFVAVTGVSGSGKSTLVNMV 652
Cdd:COG4148   16 LDVDFtlPGRGVTALFGPSGSGKTTLLRAI 45
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
450-546 9.18e-03

ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]


Pssm-ID: 130261 [Multi-domain]  Cd Length: 708  Bit Score: 39.72  E-value: 9.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006  450 EQDTAVATPILKEIKDRLnflRNVGLEYLT-LSRSARTLSGGEAQRIRLATQIGSNlSGVLyILDEPSIGLHQRDNNRLI 528
Cdd:TIGR01193 577 SQDEIWAACEIAEIKDDI---ENMPLGYQTeLSEEGSSISGGQKQRIALARALLTD-SKVL-ILDESTSNLDTITEKKIV 651
                          90
                  ....*....|....*...
gi 488923006  529 SSLKKMRDlgNTLVVVEH 546
Cdd:TIGR01193 652 NNLLNLQD--KTIIFVAH 667
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
622-653 9.63e-03

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 39.70  E-value: 9.63e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 488923006 622 LKNIDVDFPLGEFVAVTGVSGSGKSTLVNMVL 653
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLM 388
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
785-901 9.95e-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: 38.64  E-value: 9.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488923006 785 DILD--MTVEEATDFFAPI------PKIARKLQTIIDVGLgYVHLGQSATTLSGGEAQRMKLASELhkkANGKNFYILDE 856
Cdd:cd03263   84 DALFdeLTVREHLRFYARLkglpksEIKEEVELLLRVLGL-TDKANKRARTLSGGMKRKLSLAIAL---IGGPSVLLLDE 159
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 488923006 857 PTTGLhtdD--IKRLL-DVLQRLVDNgNTVLVIEHNLDViktADHLID 901
Cdd:cd03263  160 PTSGL---DpaSRRAIwDLILEVRKG-RSIILTTHSMDE---AEALCD 200
 
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.
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