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Conserved domains on  [gi|494899544|ref|WP_007625589|]
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excinuclease ABC subunit UvrA [Gordonia soli]

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;
1-951 0e+00

excinuclease ABC subunit UvrA;


:

Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 1964.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544   1 MVDRLIVRGAREHNLRGIDVDLPRDSLIVFTGLSGSGKSSLAFDTIFAEGQRRYVESLSAYARQFLGQMDKPDVDFIEGL 80
Cdd:PRK00349   2 MMDKIIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  81 SPAVSIDQKSTNRNPRSTVGTITEVYDYLRLLYARAGRAHCPECGAAIAKQTPQQIVDQVLEMDEGTRFQVLAPVVRTRK 160
Cdd:PRK00349  82 SPAISIDQKTTSHNPRSTVGTVTEIYDYLRLLYARVGKPHCPNCGRPIEAQTVSQMVDRVLELPEGTRLQILAPVVRGRK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 161 GEFVDLFADLQTQGFSRARVDGVVHQLTDPPKLKKQEKHDIEVVIDRLVVKSSAKQRLTDSVETGLRLADGIIVLDFVDL 240
Cdd:PRK00349 162 GEHKKLLENLRKQGFVRVRVDGEVYDLDEPPKLDKNKKHTIEVVVDRLVVKEDIRQRLADSIETALKLSDGLVVVEVMDD 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 241 EENDpqrERRFSERMACPNgHPIAIDDLEPRSFSFNTPYGACPDCDGLGIRKEVDEELVVPDPDLSLSEGAIAPWSGGHN 320
Cdd:PRK00349 242 PEAE---ELLFSEKFACPV-CGFSIPELEPRLFSFNSPYGACPTCDGLGVKLEFDPDLVVPDPELSLAEGAIAPWSRSSS 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 321 aDYFLRLMTGLADQMDFDVDTPWKKLPVKARKALLNGS-DHQVHVKFRNRYGRTRSYYTEFEGVMSFLSRRMEQTESDAM 399
Cdd:PRK00349 318 -SYYFQMLKSLAEHYGFDLDTPWKDLPEEVQDIILYGSgDEEIEFRYKNDRGRTRERKHPFEGVIPNLERRYRETESEYV 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 400 KERYEGYMRDIPCPVCQGARLRPEILSVTLDHpvypsKSIADVCALSVADCAEYLSGLQLDSRQKAIAGPVLKEVQARIT 479
Cdd:PRK00349 397 REELEKYMSERPCPSCKGKRLKPEALAVKVGG-----KNIGEVSELSIGEALEFFENLKLSEQEAKIAEPILKEIRERLK 471
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 480 FLLDVGLDYLSLARAAGSLSGGEAQRIRLATQIGSGLAGVLYVLDEPSIGLHQRDNRRLIDTLTRLRDLGNTLIVVEHDE 559
Cdd:PRK00349 472 FLVDVGLDYLTLSRSAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDE 551
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 560 DTIRAADWIVDIGPRAGEHGGHVVHSGNYRDLLKNRKSLTGAYLSGRESLPVPAIRRPINrKRQLTVVGAREHNLRGIDV 639
Cdd:PRK00349 552 DTIRAADYIVDIGPGAGVHGGEVVASGTPEEIMKNPNSLTGQYLSGKKKIEVPKERRKGN-GKFLKLKGARENNLKNVDV 630
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 640 AFPLGVLTAVTGVSGSGKSTLVNDILATVLANKLNGARQVPGRHKRINGLDQLDKLVRVDQSPIGRTPRSNPATYTGVFD 719
Cdd:PRK00349 631 EIPLGKFTCVTGVSGSGKSTLINETLYKALARKLNGAKKVPGKHKEIEGLEHLDKVIDIDQSPIGRTPRSNPATYTGVFD 710
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 720 KIRTLFAATTEAKVRGYQPGRFSFNVKGGRCEACTGEGTIKIEMNFLPDVYVPCEVCQGARYNRETLEVHYKGKTISEVL 799
Cdd:PRK00349 711 PIRELFAGTPEAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEVKYKGKNIADVL 790
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 800 DMPIEEAADFFEPVTSIHRYLKTLVDVGLGYVRLGQPAPTLSGGEAQRVKLAAELQKRSAGRTIYILDEPTTGLHFEDIK 879
Cdd:PRK00349 791 DMTVEEALEFFEAIPKIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELSKRSTGKTLYILDEPTTGLHFEDIR 870
                        890       900       910       920       930       940       950
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494899544 880 KLLGVINGLVDKGNTVIVIEHNLDVIKTADWVIDMGPEGGTGGGTVIAEGTPEDIAEVPESHTGGFLADILD 951
Cdd:PRK00349 871 KLLEVLHRLVDKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVATGTPEEVAKVEASYTGRYLKPVLE 942
 
Name Accession Description Interval E-value
uvrA PRK00349
excinuclease ABC subunit UvrA;
1-951 0e+00

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 1964.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544   1 MVDRLIVRGAREHNLRGIDVDLPRDSLIVFTGLSGSGKSSLAFDTIFAEGQRRYVESLSAYARQFLGQMDKPDVDFIEGL 80
Cdd:PRK00349   2 MMDKIIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  81 SPAVSIDQKSTNRNPRSTVGTITEVYDYLRLLYARAGRAHCPECGAAIAKQTPQQIVDQVLEMDEGTRFQVLAPVVRTRK 160
Cdd:PRK00349  82 SPAISIDQKTTSHNPRSTVGTVTEIYDYLRLLYARVGKPHCPNCGRPIEAQTVSQMVDRVLELPEGTRLQILAPVVRGRK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 161 GEFVDLFADLQTQGFSRARVDGVVHQLTDPPKLKKQEKHDIEVVIDRLVVKSSAKQRLTDSVETGLRLADGIIVLDFVDL 240
Cdd:PRK00349 162 GEHKKLLENLRKQGFVRVRVDGEVYDLDEPPKLDKNKKHTIEVVVDRLVVKEDIRQRLADSIETALKLSDGLVVVEVMDD 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 241 EENDpqrERRFSERMACPNgHPIAIDDLEPRSFSFNTPYGACPDCDGLGIRKEVDEELVVPDPDLSLSEGAIAPWSGGHN 320
Cdd:PRK00349 242 PEAE---ELLFSEKFACPV-CGFSIPELEPRLFSFNSPYGACPTCDGLGVKLEFDPDLVVPDPELSLAEGAIAPWSRSSS 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 321 aDYFLRLMTGLADQMDFDVDTPWKKLPVKARKALLNGS-DHQVHVKFRNRYGRTRSYYTEFEGVMSFLSRRMEQTESDAM 399
Cdd:PRK00349 318 -SYYFQMLKSLAEHYGFDLDTPWKDLPEEVQDIILYGSgDEEIEFRYKNDRGRTRERKHPFEGVIPNLERRYRETESEYV 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 400 KERYEGYMRDIPCPVCQGARLRPEILSVTLDHpvypsKSIADVCALSVADCAEYLSGLQLDSRQKAIAGPVLKEVQARIT 479
Cdd:PRK00349 397 REELEKYMSERPCPSCKGKRLKPEALAVKVGG-----KNIGEVSELSIGEALEFFENLKLSEQEAKIAEPILKEIRERLK 471
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 480 FLLDVGLDYLSLARAAGSLSGGEAQRIRLATQIGSGLAGVLYVLDEPSIGLHQRDNRRLIDTLTRLRDLGNTLIVVEHDE 559
Cdd:PRK00349 472 FLVDVGLDYLTLSRSAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDE 551
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 560 DTIRAADWIVDIGPRAGEHGGHVVHSGNYRDLLKNRKSLTGAYLSGRESLPVPAIRRPINrKRQLTVVGAREHNLRGIDV 639
Cdd:PRK00349 552 DTIRAADYIVDIGPGAGVHGGEVVASGTPEEIMKNPNSLTGQYLSGKKKIEVPKERRKGN-GKFLKLKGARENNLKNVDV 630
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 640 AFPLGVLTAVTGVSGSGKSTLVNDILATVLANKLNGARQVPGRHKRINGLDQLDKLVRVDQSPIGRTPRSNPATYTGVFD 719
Cdd:PRK00349 631 EIPLGKFTCVTGVSGSGKSTLINETLYKALARKLNGAKKVPGKHKEIEGLEHLDKVIDIDQSPIGRTPRSNPATYTGVFD 710
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 720 KIRTLFAATTEAKVRGYQPGRFSFNVKGGRCEACTGEGTIKIEMNFLPDVYVPCEVCQGARYNRETLEVHYKGKTISEVL 799
Cdd:PRK00349 711 PIRELFAGTPEAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEVKYKGKNIADVL 790
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 800 DMPIEEAADFFEPVTSIHRYLKTLVDVGLGYVRLGQPAPTLSGGEAQRVKLAAELQKRSAGRTIYILDEPTTGLHFEDIK 879
Cdd:PRK00349 791 DMTVEEALEFFEAIPKIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELSKRSTGKTLYILDEPTTGLHFEDIR 870
                        890       900       910       920       930       940       950
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494899544 880 KLLGVINGLVDKGNTVIVIEHNLDVIKTADWVIDMGPEGGTGGGTVIAEGTPEDIAEVPESHTGGFLADILD 951
Cdd:PRK00349 871 KLLEVLHRLVDKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVATGTPEEVAKVEASYTGRYLKPVLE 942
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
1-951 0e+00

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


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 1870.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544   1 MVDRLIVRGAREHNLRGIDVDLPRDSLIVFTGLSGSGKSSLAFDTIFAEGQRRYVESLSAYARQFLGQMDKPDVDFIEGL 80
Cdd:COG0178    2 MMDKIRIRGAREHNLKNIDVDIPRNKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  81 SPAVSIDQKSTNRNPRSTVGTITEVYDYLRLLYARAGRAHCPECGAAIAKQTPQQIVDQVLEMDEGTRFQVLAPVVRTRK 160
Cdd:COG0178   82 SPAISIEQKTTSRNPRSTVGTVTEIYDYLRLLFARVGTPHCPICGRPVEKQTVDQIVDRILALPEGTRLQILAPVVRGRK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 161 GEFVDLFADLQTQGFSRARVDGVVHQLTDPPKLKKQEKHDIEVVIDRLVVKSSAKQRLTDSVETGLRLADGIIVLDFVDL 240
Cdd:COG0178  162 GEHKELLEELRKQGFVRVRVDGEVYDLDEEPELDKNKKHTIEVVVDRLVVKEDIRSRLADSVETALKLGDGLVIVEVVDE 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 241 EEndpqrERRFSERMACPNgHPIAIDDLEPRSFSFNTPYGACPDCDGLGIRKEVDEELVVPDPDLSLSEGAIAPWSGGHN 320
Cdd:COG0178  242 GE-----ELLFSEKFACPD-CGISFEELEPRLFSFNSPYGACPTCDGLGRVLEFDPDLVIPDPSLSLAEGAIAPWSGPSS 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 321 AdYFLRLMTGLADQMDFDVDTPWKKLPVKARKALLNGSDHQVHVKFRNrYGRTRSYYTEFEGVMSFLSRRMEQTESDAMK 400
Cdd:COG0178  316 S-YYFQLLEALAKHYGFDLDTPWKDLPEEQRDLILYGSDEKIKFRYKN-RGRRRTYEKPFEGVIPFLERRYRETYSEHVR 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 401 ERYEGYMRDIPCPVCQGARLRPEILSVTLDhpvypSKSIADVCALSVADCAEYLSGLQLDSRQKAIAGPVLKEVQARITF 480
Cdd:COG0178  394 EELSRYMSETPCPACKGARLKPEALAVKIG-----GKNIAELTALSIDEALEFFENLELTEREAEIAERILKEIRSRLGF 468
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 481 LLDVGLDYLSLARAAGSLSGGEAQRIRLATQIGSGLAGVLYVLDEPSIGLHQRDNRRLIDTLTRLRDLGNTLIVVEHDED 560
Cdd:COG0178  469 LVDVGLDYLTLDRSAGTLSGGEAQRIRLATQIGSGLVGVLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDED 548
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 561 TIRAADWIVDIGPRAGEHGGHVVHSGNYRDLLKNRKSLTGAYLSGRESLPVPAIRRPINrKRQLTVVGAREHNLRGIDVA 640
Cdd:COG0178  549 TIRAADYIIDIGPGAGEHGGEVVAQGTPEEILKNPDSLTGQYLSGRKRIPVPKKRRKGN-GKFLTIKGARENNLKNVDVE 627
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 641 FPLGVLTAVTGVSGSGKSTLVNDILATVLANKLNGARQVPGRHKRINGLDQLDKLVRVDQSPIGRTPRSNPATYTGVFDK 720
Cdd:COG0178  628 IPLGVLTCVTGVSGSGKSTLVNDILYPALARKLNGAKEKPGPHDSIEGLEHIDKVIDIDQSPIGRTPRSNPATYTGVFDP 707
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 721 IRTLFAATTEAKVRGYQPGRFSFNVKGGRCEACTGEGTIKIEMNFLPDVYVPCEVCQGARYNRETLEVHYKGKTISEVLD 800
Cdd:COG0178  708 IRELFAQTPEAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLD 787
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 801 MPIEEAADFFEPVTSIHRYLKTLVDVGLGYVRLGQPAPTLSGGEAQRVKLAAELQKRSAGRTIYILDEPTTGLHFEDIKK 880
Cdd:COG0178  788 MTVEEALEFFENIPKIARKLQTLQDVGLGYIKLGQPATTLSGGEAQRVKLASELSKRSTGKTLYILDEPTTGLHFHDIRK 867
                        890       900       910       920       930       940       950
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494899544 881 LLGVINGLVDKGNTVIVIEHNLDVIKTADWVIDMGPEGGTGGGTVIAEGTPEDIAEVPESHTGGFLADILD 951
Cdd:COG0178  868 LLEVLHRLVDKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVAEGTPEEVAKVKASYTGRYLKEYLE 938
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
4-935 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: 1640.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544    4 RLIVRGAREHNLRGIDVDLPRDSLIVFTGLSGSGKSSLAFDTIFAEGQRRYVESLSAYARQFLGQMDKPDVDFIEGLSPA 83
Cdd:TIGR00630   1 KIIVRGAREHNLKNIDVEIPRDKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGVMDKPDVDSIEGLSPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544   84 VSIDQKSTNRNPRSTVGTITEVYDYLRLLYARAGRAHCPECGAAIAKQTPQQIVDQVLEMDEGTRFQVLAPVVRTRKGEF 163
Cdd:TIGR00630  81 ISIDQKTTSHNPRSTVGTITEIYDYLRLLFARVGTPYCPTCGRPISRQTPSQIVDQILALPEGTRVILLAPIVRGRKGEF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  164 VDLFADLQTQGFSRARVDGVVHQLTDPPKLKKQEKHDIEVVIDRLVVKSSAKQRLTDSVETGLRLADGIIVLDFVDLEEN 243
Cdd:TIGR00630 161 RKLLEKLRKQGFARVRVDGEVYPLEDPPKLEKNKKHTIDVVIDRLTVKNENRSRLAESVETALRLGDGLLEVEFDDDEEV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  244 DPQRERRFSERMACPnGHPIAIDDLEPRSFSFNTPYGACPDCDGLGIRKEVDEELVVPDPDLSLSEGAIAPWSGGHNaDY 323
Cdd:TIGR00630 241 AESKEELFSEKFACP-ECGFSLPELEPRLFSFNSPYGACPECSGLGIKQEFDPELIIPDPLLSLNGGAIVPFKKSTT-SY 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  324 FLRLMTGLADQMDFDVDTPWKKLPVKARKALLNGSDHQVHVKF-RNRYGRTRSYYTEFEGVMSFLSRRMEQTESDAMKER 402
Cdd:TIGR00630 319 YRQMFASLAEHLGFDLDTPWKDLPEEAQKAILYGSGEEVIVVKyRNGGGETFRYHKPFEGVIPELERRYLETESESMREY 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  403 YEGYMRDIPCPVCQGARLRPEILSVTLDhpvypSKSIADVCALSVADCAEYLSGLQLDSRQKAIAGPVLKEVQARITFLL 482
Cdd:TIGR00630 399 LEKFMSERPCPSCGGTRLKPEALAVTVG-----GKSIADVSELSIREAHEFFNQLTLTPEEKKIAEEVLKEIRERLGFLI 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  483 DVGLDYLSLARAAGSLSGGEAQRIRLATQIGSGLAGVLYVLDEPSIGLHQRDNRRLIDTLTRLRDLGNTLIVVEHDEDTI 562
Cdd:TIGR00630 474 DVGLDYLSLSRAAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTI 553
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  563 RAADWIVDIGPRAGEHGGHVVHSGNYRDLLKNRKSLTGAYLSGRESLPVPAIRRPINrKRQLTVVGAREHNLRGIDVAFP 642
Cdd:TIGR00630 554 RAADYVIDIGPGAGEHGGEVVASGTPEEILANPDSLTGQYLSGRKKIEVPAERRPGN-GKFLTLKGARENNLKNITVSIP 632
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  643 LGVLTAVTGVSGSGKSTLVNDILATVLANKLNGARQVPGRHKRINGLDQLDKLVRVDQSPIGRTPRSNPATYTGVFDKIR 722
Cdd:TIGR00630 633 LGLFTCITGVSGSGKSTLINDTLYPALANRLNGAKTVPGRYTSIEGLEHLDKVIHIDQSPIGRTPRSNPATYTGVFDEIR 712
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  723 TLFAATTEAKVRGYQPGRFSFNVKGGRCEACTGEGTIKIEMNFLPDVYVPCEVCQGARYNRETLEVHYKGKTISEVLDMP 802
Cdd:TIGR00630 713 ELFAETPEAKVRGYTPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMT 792
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  803 IEEAADFFEPVTSIHRYLKTLVDVGLGYVRLGQPAPTLSGGEAQRVKLAAELQKRSAGRTIYILDEPTTGLHFEDIKKLL 882
Cdd:TIGR00630 793 VEEAYEFFEAVPSISRKLQTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKRSTGRTLYILDEPTTGLHFDDIKKLL 872
                         890       900       910       920       930
                  ....*....|....*....|....*....|....*....|....*....|...
gi 494899544  883 GVINGLVDKGNTVIVIEHNLDVIKTADWVIDMGPEGGTGGGTVIAEGTPEDIA 935
Cdd:TIGR00630 873 EVLQRLVDKGNTVVVIEHNLDVIKTADYIIDLGPEGGDGGGTVVASGTPEEVA 925
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
624-931 2.34e-159

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: 468.25  E-value: 2.34e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 624 LTVVGAREHNLRGIDVAFPLGVLTAVTGVSGSGKSTLVNDILATVLANKLNGARQVPGRHKRINGLDQLDKLVRVDQSPI 703
Cdd:cd03271    1 LTLKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPALARRLHLKKEQPGNHDRIEGLEHIDKVIVIDQSPI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 704 GRTPRSNPATYTGVFDKIRTLFaatteakvrgyqpgrfsfnvkggrceactgegtikiemnflpdvyvpCEVCQGARYNR 783
Cdd:cd03271   81 GRTPRSNPATYTGVFDEIRELF-----------------------------------------------CEVCKGKRYNR 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 784 ETLEVHYKGKTISEVLDMPIEEAADFFEPVTSIHRYLKTLVDVGLGYVRLGQPAPTLSGGEAQRVKLAAELQKRSAGRTI 863
Cdd:cd03271  114 ETLEVRYKGKSIADVLDMTVEEALEFFENIPKIARKLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRSTGKTL 193
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494899544 864 YILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNLDVIKTADWVIDMGPEGGTGGGTVIAEGTP 931
Cdd:cd03271  194 YILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLGPEGGDGGGQVVASGTP 261
UvrA_DNA-bind pfam17755
UvrA DNA-binding domain;
295-404 7.78e-48

UvrA DNA-binding domain;


Pssm-ID: 465484 [Multi-domain]  Cd Length: 110  Bit Score: 165.34  E-value: 7.78e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  295 DEELVVPDPDLSLSEGAIAPWSGGHNAdYFLRLMTGLADQMDFDVDTPWKKLPVKARKALLNGSDHQVHVKFRNRYGRTR 374
Cdd:pfam17755   1 DPDLVIPDPSLSLAEGAIAPWGKKRSS-YYFQLLEALAKHYGFDLDTPFKDLPEEQQDIILYGSGEEIIVFYYSRGGRTR 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 494899544  375 SYYTEFEGVMSFLSRRMEQTESDAMKERYE 404
Cdd:pfam17755  80 TYTKPFEGVIPNLERRYRETDSESVREELE 109
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
634-914 4.30e-08

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 54.16  E-value: 4.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 634 LRGIDVAFPLGVLTAVTGVSGSGKSTLVNdILATVLAnKLNGARQVpGRHKRINGLDQldklvrvdqspIGRTPRSNPAT 713
Cdd:NF040873   8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLK-VLAGVLR-PTSGTVRR-AGGARVAYVPQ-----------RSEVPDSLPLT 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 714 ytgvfdkIRTLFAATTEAKvRGyqPGRfsfnvkggrceactgegtikiemnflpdvyvpcevcqgaRYNRETLEVhykgk 793
Cdd:NF040873  74 -------VRDLVAMGRWAR-RG--LWR---------------------------------------RLTRDDRAA----- 99
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 794 tisevldmpIEEAadffepvtsihrylktLVDVGLGYVRlGQPAPTLSGGEAQRVKLAAELQKRSagrTIYILDEPTTGL 873
Cdd:NF040873 100 ---------VDDA----------------LERVGLADLA-GRQLGELSGGQRQRALLAQGLAQEA---DLLLLDEPTTGL 150
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 494899544 874 HFEDIKKLLGVINGLVDKGNTVIVIEHNLDVIKTADWVIDM 914
Cdd:NF040873 151 DAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
GguA NF040905
sugar ABC transporter ATP-binding protein;
865-909 2.09e-03

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 41.70  E-value: 2.09e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 494899544 865 ILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNL-DVIKTAD 909
Cdd:NF040905 162 ILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLnEIRRVAD 207
GguA NF040905
sugar ABC transporter ATP-binding protein;
835-898 7.38e-03

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 40.16  E-value: 7.38e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494899544 835 QPAPTLSGGEAQRVKLAAELqkrSAGRTIYILDEPTTGL----HFEdikkLLGVINGLVDKGNTVIVI 898
Cdd:NF040905 400 QKVGNLSGGNQQKVVLSKWL---FTDPDVLILDEPTRGIdvgaKYE----IYTIINELAAEGKGVIVI 460
 
Name Accession Description Interval E-value
uvrA PRK00349
excinuclease ABC subunit UvrA;
1-951 0e+00

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 1964.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544   1 MVDRLIVRGAREHNLRGIDVDLPRDSLIVFTGLSGSGKSSLAFDTIFAEGQRRYVESLSAYARQFLGQMDKPDVDFIEGL 80
Cdd:PRK00349   2 MMDKIIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  81 SPAVSIDQKSTNRNPRSTVGTITEVYDYLRLLYARAGRAHCPECGAAIAKQTPQQIVDQVLEMDEGTRFQVLAPVVRTRK 160
Cdd:PRK00349  82 SPAISIDQKTTSHNPRSTVGTVTEIYDYLRLLYARVGKPHCPNCGRPIEAQTVSQMVDRVLELPEGTRLQILAPVVRGRK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 161 GEFVDLFADLQTQGFSRARVDGVVHQLTDPPKLKKQEKHDIEVVIDRLVVKSSAKQRLTDSVETGLRLADGIIVLDFVDL 240
Cdd:PRK00349 162 GEHKKLLENLRKQGFVRVRVDGEVYDLDEPPKLDKNKKHTIEVVVDRLVVKEDIRQRLADSIETALKLSDGLVVVEVMDD 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 241 EENDpqrERRFSERMACPNgHPIAIDDLEPRSFSFNTPYGACPDCDGLGIRKEVDEELVVPDPDLSLSEGAIAPWSGGHN 320
Cdd:PRK00349 242 PEAE---ELLFSEKFACPV-CGFSIPELEPRLFSFNSPYGACPTCDGLGVKLEFDPDLVVPDPELSLAEGAIAPWSRSSS 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 321 aDYFLRLMTGLADQMDFDVDTPWKKLPVKARKALLNGS-DHQVHVKFRNRYGRTRSYYTEFEGVMSFLSRRMEQTESDAM 399
Cdd:PRK00349 318 -SYYFQMLKSLAEHYGFDLDTPWKDLPEEVQDIILYGSgDEEIEFRYKNDRGRTRERKHPFEGVIPNLERRYRETESEYV 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 400 KERYEGYMRDIPCPVCQGARLRPEILSVTLDHpvypsKSIADVCALSVADCAEYLSGLQLDSRQKAIAGPVLKEVQARIT 479
Cdd:PRK00349 397 REELEKYMSERPCPSCKGKRLKPEALAVKVGG-----KNIGEVSELSIGEALEFFENLKLSEQEAKIAEPILKEIRERLK 471
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 480 FLLDVGLDYLSLARAAGSLSGGEAQRIRLATQIGSGLAGVLYVLDEPSIGLHQRDNRRLIDTLTRLRDLGNTLIVVEHDE 559
Cdd:PRK00349 472 FLVDVGLDYLTLSRSAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDE 551
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 560 DTIRAADWIVDIGPRAGEHGGHVVHSGNYRDLLKNRKSLTGAYLSGRESLPVPAIRRPINrKRQLTVVGAREHNLRGIDV 639
Cdd:PRK00349 552 DTIRAADYIVDIGPGAGVHGGEVVASGTPEEIMKNPNSLTGQYLSGKKKIEVPKERRKGN-GKFLKLKGARENNLKNVDV 630
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 640 AFPLGVLTAVTGVSGSGKSTLVNDILATVLANKLNGARQVPGRHKRINGLDQLDKLVRVDQSPIGRTPRSNPATYTGVFD 719
Cdd:PRK00349 631 EIPLGKFTCVTGVSGSGKSTLINETLYKALARKLNGAKKVPGKHKEIEGLEHLDKVIDIDQSPIGRTPRSNPATYTGVFD 710
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 720 KIRTLFAATTEAKVRGYQPGRFSFNVKGGRCEACTGEGTIKIEMNFLPDVYVPCEVCQGARYNRETLEVHYKGKTISEVL 799
Cdd:PRK00349 711 PIRELFAGTPEAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEVKYKGKNIADVL 790
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 800 DMPIEEAADFFEPVTSIHRYLKTLVDVGLGYVRLGQPAPTLSGGEAQRVKLAAELQKRSAGRTIYILDEPTTGLHFEDIK 879
Cdd:PRK00349 791 DMTVEEALEFFEAIPKIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELSKRSTGKTLYILDEPTTGLHFEDIR 870
                        890       900       910       920       930       940       950
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494899544 880 KLLGVINGLVDKGNTVIVIEHNLDVIKTADWVIDMGPEGGTGGGTVIAEGTPEDIAEVPESHTGGFLADILD 951
Cdd:PRK00349 871 KLLEVLHRLVDKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVATGTPEEVAKVEASYTGRYLKPVLE 942
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
1-951 0e+00

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


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 1870.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544   1 MVDRLIVRGAREHNLRGIDVDLPRDSLIVFTGLSGSGKSSLAFDTIFAEGQRRYVESLSAYARQFLGQMDKPDVDFIEGL 80
Cdd:COG0178    2 MMDKIRIRGAREHNLKNIDVDIPRNKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  81 SPAVSIDQKSTNRNPRSTVGTITEVYDYLRLLYARAGRAHCPECGAAIAKQTPQQIVDQVLEMDEGTRFQVLAPVVRTRK 160
Cdd:COG0178   82 SPAISIEQKTTSRNPRSTVGTVTEIYDYLRLLFARVGTPHCPICGRPVEKQTVDQIVDRILALPEGTRLQILAPVVRGRK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 161 GEFVDLFADLQTQGFSRARVDGVVHQLTDPPKLKKQEKHDIEVVIDRLVVKSSAKQRLTDSVETGLRLADGIIVLDFVDL 240
Cdd:COG0178  162 GEHKELLEELRKQGFVRVRVDGEVYDLDEEPELDKNKKHTIEVVVDRLVVKEDIRSRLADSVETALKLGDGLVIVEVVDE 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 241 EEndpqrERRFSERMACPNgHPIAIDDLEPRSFSFNTPYGACPDCDGLGIRKEVDEELVVPDPDLSLSEGAIAPWSGGHN 320
Cdd:COG0178  242 GE-----ELLFSEKFACPD-CGISFEELEPRLFSFNSPYGACPTCDGLGRVLEFDPDLVIPDPSLSLAEGAIAPWSGPSS 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 321 AdYFLRLMTGLADQMDFDVDTPWKKLPVKARKALLNGSDHQVHVKFRNrYGRTRSYYTEFEGVMSFLSRRMEQTESDAMK 400
Cdd:COG0178  316 S-YYFQLLEALAKHYGFDLDTPWKDLPEEQRDLILYGSDEKIKFRYKN-RGRRRTYEKPFEGVIPFLERRYRETYSEHVR 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 401 ERYEGYMRDIPCPVCQGARLRPEILSVTLDhpvypSKSIADVCALSVADCAEYLSGLQLDSRQKAIAGPVLKEVQARITF 480
Cdd:COG0178  394 EELSRYMSETPCPACKGARLKPEALAVKIG-----GKNIAELTALSIDEALEFFENLELTEREAEIAERILKEIRSRLGF 468
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 481 LLDVGLDYLSLARAAGSLSGGEAQRIRLATQIGSGLAGVLYVLDEPSIGLHQRDNRRLIDTLTRLRDLGNTLIVVEHDED 560
Cdd:COG0178  469 LVDVGLDYLTLDRSAGTLSGGEAQRIRLATQIGSGLVGVLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDED 548
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 561 TIRAADWIVDIGPRAGEHGGHVVHSGNYRDLLKNRKSLTGAYLSGRESLPVPAIRRPINrKRQLTVVGAREHNLRGIDVA 640
Cdd:COG0178  549 TIRAADYIIDIGPGAGEHGGEVVAQGTPEEILKNPDSLTGQYLSGRKRIPVPKKRRKGN-GKFLTIKGARENNLKNVDVE 627
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 641 FPLGVLTAVTGVSGSGKSTLVNDILATVLANKLNGARQVPGRHKRINGLDQLDKLVRVDQSPIGRTPRSNPATYTGVFDK 720
Cdd:COG0178  628 IPLGVLTCVTGVSGSGKSTLVNDILYPALARKLNGAKEKPGPHDSIEGLEHIDKVIDIDQSPIGRTPRSNPATYTGVFDP 707
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 721 IRTLFAATTEAKVRGYQPGRFSFNVKGGRCEACTGEGTIKIEMNFLPDVYVPCEVCQGARYNRETLEVHYKGKTISEVLD 800
Cdd:COG0178  708 IRELFAQTPEAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLD 787
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 801 MPIEEAADFFEPVTSIHRYLKTLVDVGLGYVRLGQPAPTLSGGEAQRVKLAAELQKRSAGRTIYILDEPTTGLHFEDIKK 880
Cdd:COG0178  788 MTVEEALEFFENIPKIARKLQTLQDVGLGYIKLGQPATTLSGGEAQRVKLASELSKRSTGKTLYILDEPTTGLHFHDIRK 867
                        890       900       910       920       930       940       950
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494899544 881 LLGVINGLVDKGNTVIVIEHNLDVIKTADWVIDMGPEGGTGGGTVIAEGTPEDIAEVPESHTGGFLADILD 951
Cdd:COG0178  868 LLEVLHRLVDKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVAEGTPEEVAKVKASYTGRYLKEYLE 938
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
4-935 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: 1640.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544    4 RLIVRGAREHNLRGIDVDLPRDSLIVFTGLSGSGKSSLAFDTIFAEGQRRYVESLSAYARQFLGQMDKPDVDFIEGLSPA 83
Cdd:TIGR00630   1 KIIVRGAREHNLKNIDVEIPRDKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGVMDKPDVDSIEGLSPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544   84 VSIDQKSTNRNPRSTVGTITEVYDYLRLLYARAGRAHCPECGAAIAKQTPQQIVDQVLEMDEGTRFQVLAPVVRTRKGEF 163
Cdd:TIGR00630  81 ISIDQKTTSHNPRSTVGTITEIYDYLRLLFARVGTPYCPTCGRPISRQTPSQIVDQILALPEGTRVILLAPIVRGRKGEF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  164 VDLFADLQTQGFSRARVDGVVHQLTDPPKLKKQEKHDIEVVIDRLVVKSSAKQRLTDSVETGLRLADGIIVLDFVDLEEN 243
Cdd:TIGR00630 161 RKLLEKLRKQGFARVRVDGEVYPLEDPPKLEKNKKHTIDVVIDRLTVKNENRSRLAESVETALRLGDGLLEVEFDDDEEV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  244 DPQRERRFSERMACPnGHPIAIDDLEPRSFSFNTPYGACPDCDGLGIRKEVDEELVVPDPDLSLSEGAIAPWSGGHNaDY 323
Cdd:TIGR00630 241 AESKEELFSEKFACP-ECGFSLPELEPRLFSFNSPYGACPECSGLGIKQEFDPELIIPDPLLSLNGGAIVPFKKSTT-SY 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  324 FLRLMTGLADQMDFDVDTPWKKLPVKARKALLNGSDHQVHVKF-RNRYGRTRSYYTEFEGVMSFLSRRMEQTESDAMKER 402
Cdd:TIGR00630 319 YRQMFASLAEHLGFDLDTPWKDLPEEAQKAILYGSGEEVIVVKyRNGGGETFRYHKPFEGVIPELERRYLETESESMREY 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  403 YEGYMRDIPCPVCQGARLRPEILSVTLDhpvypSKSIADVCALSVADCAEYLSGLQLDSRQKAIAGPVLKEVQARITFLL 482
Cdd:TIGR00630 399 LEKFMSERPCPSCGGTRLKPEALAVTVG-----GKSIADVSELSIREAHEFFNQLTLTPEEKKIAEEVLKEIRERLGFLI 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  483 DVGLDYLSLARAAGSLSGGEAQRIRLATQIGSGLAGVLYVLDEPSIGLHQRDNRRLIDTLTRLRDLGNTLIVVEHDEDTI 562
Cdd:TIGR00630 474 DVGLDYLSLSRAAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTI 553
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  563 RAADWIVDIGPRAGEHGGHVVHSGNYRDLLKNRKSLTGAYLSGRESLPVPAIRRPINrKRQLTVVGAREHNLRGIDVAFP 642
Cdd:TIGR00630 554 RAADYVIDIGPGAGEHGGEVVASGTPEEILANPDSLTGQYLSGRKKIEVPAERRPGN-GKFLTLKGARENNLKNITVSIP 632
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  643 LGVLTAVTGVSGSGKSTLVNDILATVLANKLNGARQVPGRHKRINGLDQLDKLVRVDQSPIGRTPRSNPATYTGVFDKIR 722
Cdd:TIGR00630 633 LGLFTCITGVSGSGKSTLINDTLYPALANRLNGAKTVPGRYTSIEGLEHLDKVIHIDQSPIGRTPRSNPATYTGVFDEIR 712
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  723 TLFAATTEAKVRGYQPGRFSFNVKGGRCEACTGEGTIKIEMNFLPDVYVPCEVCQGARYNRETLEVHYKGKTISEVLDMP 802
Cdd:TIGR00630 713 ELFAETPEAKVRGYTPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMT 792
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  803 IEEAADFFEPVTSIHRYLKTLVDVGLGYVRLGQPAPTLSGGEAQRVKLAAELQKRSAGRTIYILDEPTTGLHFEDIKKLL 882
Cdd:TIGR00630 793 VEEAYEFFEAVPSISRKLQTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKRSTGRTLYILDEPTTGLHFDDIKKLL 872
                         890       900       910       920       930
                  ....*....|....*....|....*....|....*....|....*....|...
gi 494899544  883 GVINGLVDKGNTVIVIEHNLDVIKTADWVIDMGPEGGTGGGTVIAEGTPEDIA 935
Cdd:TIGR00630 873 EVLQRLVDKGNTVVVIEHNLDVIKTADYIIDLGPEGGDGGGTVVASGTPEEVA 925
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
7-934 0e+00

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 624.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544    7 VRGAREHNLRGIDVD-LPRDsLIVFTGLSGSGKSSLAFDTIFAEGQRRYVESLSAYARQFLGQMDKPDVDFIEGLSPAVS 85
Cdd:PRK00635    8 LSGITVRNLKNISIEfCPRE-IVLLTGVSGSGKSSLAFDTIYAAGRKRYLSTLPSFFATTLDSLPDPSVEKIEGLSPTIA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544   86 IDQKSTNRNPRSTVGTITEVYDYLRLLYARAGRAHCPECGAAIAKQTPQQIVDQVLEMDEGTRFQVLAPVVRTrkgefvD 165
Cdd:PRK00635   87 VKQNHFSQHSHATVGSTTELNSHLALLFSLEGQARDPVTLHPLTLYSKEKILSTIAAIPDGTQITLLAPLPAK------D 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  166 LFA--DLQTQGFSRARVDGVVHQ----LTDPpklkKQEKHDIEVVIDRLVVKSSAKQRLTDSVETGLRLADGIIVLDFvd 239
Cdd:PRK00635  161 ILAirECLRQGFTKVRIDGEISPiykfLTSG----IPEDVPVDIVVDTLIKNESNTARLKVSLFTALDIGHGECSLHF-- 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  240 leenDPQrERRFSERMACPNGHPiAIDDLEPRSFSFNTPYGACPDCDGLGIRKEVDEELVVpDPDLSLSEGAiAPWSGGH 319
Cdd:PRK00635  235 ----DNQ-KRTFSTQATIPETQQ-TYTPLTPQLFSPHSLEDRCPQCQGSGIFISIDDPSLI-QQNLSIEENC-CPFAGNC 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  320 NADYFLRLMTGLADQMDFDVDTPWKKLPVKARKALLNGSDHQV-HVK-FRNRYGRTRSYYTEFEGVMSFLSrrmEQTESD 397
Cdd:PRK00635  307 STYLYHTIYQSLADSLGFSLSTPWKDLSPEIQNIFLYGKEGLVlPVRlFDGTLGKKTLTHKVWRGVLNEIG---EKVRYS 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  398 AMKERY--EGyMRDIPCPVCQGARLrPEILSVTLDHpvypSKSIADVCALSVADCAEYLSglQLDSRQKAIAgPVLKEVQ 475
Cdd:PRK00635  384 NKPSRYlpKG-TSATSCPRCQGTGL-GDYANAATWH----GKTFAEFQQMSLQELFIFLS--QLPSKSLSIE-EVLQGLK 454
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  476 ARITFLLDVGLDYLSLARAAGSLSGGEAQRIRLATQIGSGLAGVLYVLDEPSIGLHQRDNRRLIDTLTRLRDLGNTLIVV 555
Cdd:PRK00635  455 SRLSILIDLGLPYLTPERALATLSGGEQERTALAKHLGAELIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLV 534
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  556 EHDEDTIRAADWIVDIGPRAGEHGGHVVHSGNYRDLLKNRKSLTGAYLSGRESLPVPAiRRPiNRKRQLTVVGAREHNLR 635
Cdd:PRK00635  535 EHDEQMISLADRIIDIGPGAGIFGGEVLFNGSPREFLAKSDSLTAKYLRQELTIPIPE-KRT-NSLGTLTLSKATKHNLK 612
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  636 GIDVAFPLGVLTAVTGVSGSGKSTLVNDILATVLANKLNGArqvPGRHKRINGlDQLDKLVRVDQSPIGRTPRSNPATYT 715
Cdd:PRK00635  613 DLTISLPLGRLTVVTGVSGSGKSSLINDTLVPAVEEFIEQG---FCSNLSIQW-GAISRLVHITRDLPGRSQRSIPLTYI 688
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  716 GVFDKIRTLFAATTEAKVRGYQPGRFSFNVKGGRCEACTGEGTIKIEMNFLPdvyVPCEVCQGARYNRETLEVHYKGKTI 795
Cdd:PRK00635  689 KAFDDLRELFAEQPRSKRLGLTKSHFSFNTPLGACAECQGLGSITTTDNRTS---IPCPSCLGKRFLPQVLEVRYKGKNI 765
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  796 SEVLDMPIEEAADFFEPVTSIHRYLKTLVDVGLGYVRLGQPAPTLSGGEAQRVKLAAELQKRSAGRTIYILDEPTTGLHF 875
Cdd:PRK00635  766 ADILEMTAYEAEKFFLDEPSIHEKIHALCSLGLDYLPLGRPLSSLSGGEIQRLKLAYELLAPSKKPTLYVLDEPTTGLHT 845
                         890       900       910       920       930
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 494899544  876 EDIKKLLGVINGLVDKGNTVIVIEHNLDVIKTADWVIDMGPEGGTGGGTVIAEGTPEDI 934
Cdd:PRK00635  846 HDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLELGPEGGNLGGYLLASCSPEEL 904
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
624-931 2.34e-159

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: 468.25  E-value: 2.34e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 624 LTVVGAREHNLRGIDVAFPLGVLTAVTGVSGSGKSTLVNDILATVLANKLNGARQVPGRHKRINGLDQLDKLVRVDQSPI 703
Cdd:cd03271    1 LTLKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPALARRLHLKKEQPGNHDRIEGLEHIDKVIVIDQSPI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 704 GRTPRSNPATYTGVFDKIRTLFaatteakvrgyqpgrfsfnvkggrceactgegtikiemnflpdvyvpCEVCQGARYNR 783
Cdd:cd03271   81 GRTPRSNPATYTGVFDEIRELF-----------------------------------------------CEVCKGKRYNR 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 784 ETLEVHYKGKTISEVLDMPIEEAADFFEPVTSIHRYLKTLVDVGLGYVRLGQPAPTLSGGEAQRVKLAAELQKRSAGRTI 863
Cdd:cd03271  114 ETLEVRYKGKSIADVLDMTVEEALEFFENIPKIARKLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRSTGKTL 193
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494899544 864 YILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNLDVIKTADWVIDMGPEGGTGGGTVIAEGTP 931
Cdd:cd03271  194 YILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLGPEGGDGGGQVVASGTP 261
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
5-935 2.52e-94

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 328.33  E-value: 2.52e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544    5 LIVRGAREHNLRGIDVDLPRDSLIVFTGLSGSGKSSLAFDTIFAEGQRRYVESLSAYARQ-FLGQMDKPDVDFIEGLSPA 83
Cdd:PRK00635  941 ITIKNAYQHNLKHIDLSLPRNALTAVTGPSASGKHSLVFDILYAAGNIAYAELFPPYIRQaLIKKTPLPSVDKVTGLSPV 1020
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544   84 VSIDQKSTNRNPRSTVGTITEVYDYLRLLYARAGRAHCPECGAAIAKQTPQQIVDQVLEMDEGTRFQVLAPVvrtRKGEf 163
Cdd:PRK00635 1021 IAIEKTSASKNSNHSVASALEISNGLEKLFARLGHPYSPLSGDALRKITPQTIAEELLTHYTKGYVTITSPI---PKEE- 1096
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  164 vDLFADLQT---QGFSRARVDGVVHQLTDP-PKLKKqekhDIEVVIDRLVVKSSAKQRLTDSVETGLRLADGIivldfvD 239
Cdd:PRK00635 1097 -DLFIYLQEklkEGFLKLYANEQFYDLDEPlPTSLE----NPAIVIQHTKISEKNLSSLLSSLTLAFSLSSSI------C 1165
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  240 LEENDPQRERRFSERMACPNGHPIAIDDLEPRSFSFNTPYGACPDCDGLG----IRKEVDEELVVPDPDLSLSEgAIAPw 315
Cdd:PRK00635 1166 LHIEYAGTSLSLTYRLGWQDSSGNLYPNITTPLLSRDHEEGLCPLCHGKGfilkCSLLPHKEKIAHYTPLSLFT-LFFP- 1243
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  316 sgghnaDYFLRLMTGLADQMDFDVDTPWKKLPVKARKALLNGSdhqvhvkfrnrygrtrsyyTEFEGVMSFLsrrMEQTE 395
Cdd:PRK00635 1244 ------NQDPKPVYPLLKELGIPSIALFQELDTLSFESLCLGT-------------------QQHPGLNALL---MEAML 1295
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  396 SDAMKERYEGYMRDIPCPVCQGARLRpeilsvTLDHPV-YPSKSIADVCALSVADCAEYLSGLQLDSRQkaiagPVLKEV 474
Cdd:PRK00635 1296 MESEEPLPPPLISKTPCNQCQGLGVY------TYAHCVrIHNTSLSDIYQEDVTFLKKFLLTIHDDEEP-----SIIQDL 1364
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  475 QARITFLLDVGLDYLSLARAAGSLSGGEAQRIRLATQIGSGLAGVLYVLDEPSIGLHQRDNRRLIDTLTRLRDLGNTLIV 554
Cdd:PRK00635 1365 LNRLTFIDKVGLSYITLGQEQDTLSDGEHYRLHLAKKISSNLTDIIYLLEDPLSGLHPQDAPTLLQLIKELVTNNNTVIA 1444
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  555 VEHDEDTIRAADWIVDIGPRAGEHGGhvvhsgnyrdllknrksltgaYLSGRESLPVPAIRRPINRKRQLTV---VGARE 631
Cdd:PRK00635 1445 TDRSGSLAEHADHLIHLGPGSGPQGG---------------------YLLSTSALKQSQPDLHNTRSSEETPtlsVSLSI 1503
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  632 HNLRGIDVAFPLGVLTAVTGVSGSGKSTLVndilatvlankLNGARQvPGRHKRINGLDQLDKLVRVDQSPIGRTPRSNP 711
Cdd:PRK00635 1504 HTIQNLNVSAPLHSLVAISGVSGSGKTSLL-----------LEGFYK-QACALIEKGPSVFSEIIFLDSHPQISSQRSDI 1571
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  712 ATYTGVFDKIRTLFAATTEAKVRGYQPGRFSFNVKGGRCEACTGEGTIKIEMNFLPDVYVPCEVCQGARYNRETLEVHYK 791
Cdd:PRK00635 1572 STYFDIAPSLRNFYASLTQAKALNISASMFSTNTKQGQCSDCWGLGYQWIDRAFYALEKRPCPTCSGFRIQPLAQEVVYE 1651
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  792 GKTISEVLDMPIEEAADFFEPVTSIHRYLKTLVDVGLGYVRLGQPAPTLSGGEAQRVKLAAELQKRSAGRTIYILDEPTT 871
Cdd:PRK00635 1652 GKHFGQLLQTPIEEVAETFPFLKKIQKPLQALIDNGLGYLPLGQNLSSLSLSEKIAIKIAKFLYLPPKHPTLFLLDEIAT 1731
                         890       900       910       920       930       940
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494899544  872 GLHFEDIKKLLGVINGLVDKGNTVIVIEHNLDVIKTADWVIDMGPEGGTGGGTVIAEGTPEDIA 935
Cdd:PRK00635 1732 SLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALLKQADYLIEMGPGSGKTGGKILFSGPPKDIS 1795
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
5-117 8.97e-74

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


Pssm-ID: 213237 [Multi-domain]  Cd Length: 226  Bit Score: 242.16  E-value: 8.97e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544   5 LIVRGAREHNLRGIDVDLPRDSLIVFTGLSGSGKSSLAFDTIFAEGQRRYVESLSAYARQFLGQMDKPDVDFIEGLSPAV 84
Cdd:cd03270    1 IIVRGAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLSPAI 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 494899544  85 SIDQKSTNRNPRSTVGTITEVYDYLRLLYARAG 117
Cdd:cd03270   81 AIDQKTTSRNPRSTVGTVTEIYDYLRLLFARVG 113
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
476-586 2.55e-67

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: 224.44  E-value: 2.55e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 476 ARITFLLDVGLDYLSLARAAGSLSGGEAQRIRLATQIGSGLAGVLYVLDEPSIGLHQRDNRRLIDTLTRLRDLGNTLIVV 555
Cdd:cd03270  116 ERLGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVV 195
                         90       100       110
                 ....*....|....*....|....*....|.
gi 494899544 556 EHDEDTIRAADWIVDIGPRAGEHGGHVVHSG 586
Cdd:cd03270  196 EHDEDTIRAADHVIDIGPGAGVHGGEIVAQG 226
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
624-929 6.51e-57

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: 193.69  E-value: 6.51e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 624 LTVVGAREHNLRGIDVAFPLGVLTAVTGVSGSGKSTLVNDILATVLANKLNGARQVPGRHKringldqldkLVRVDQspi 703
Cdd:cd03238    1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKARLISFLPKFSRNK----------LIFIDQ--- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 704 grtprsnpatytgvfdkirtlfaatteakvrgyqpgrfsfnvkggrceactgegtikiemnflpdvyvpcevcqgarynr 783
Cdd:cd03238      --------------------------------------------------------------------------------
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 784 etlevhykgktisevldmpieeaadffepvtsihryLKTLVDVGLGYVRLGQPAPTLSGGEAQRVKLAAELQKRSaGRTI 863
Cdd:cd03238   68 ------------------------------------LQFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEP-PGTL 110
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494899544 864 YILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNLDVIKTADWVIDMGPEGGTGGGTVIAEG 929
Cdd:cd03238  111 FILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDFGPGSGKSGGKVVFSG 176
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
769-953 1.71e-56

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


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 211.42  E-value: 1.71e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 769 VYVPCEVCQGARYNRETLEVHYKGKTISEVLDMPIEEAADFFE--------------PVTSIHRYLKTLVDVGLGYVRLG 834
Cdd:COG0178  401 SETPCPACKGARLKPEALAVKIGGKNIAELTALSIDEALEFFEnleltereaeiaerILKEIRSRLGFLVDVGLDYLTLD 480
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 835 QPAPTLSGGEAQRVKLAAELqkrsaGR----TIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNLDVIKTADW 910
Cdd:COG0178  481 RSAGTLSGGEAQRIRLATQI-----GSglvgVLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDTIRAADY 555
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 494899544 911 VIDMGPEGGTGGGTVIAEGTPEDIAEVPESHTGGFLADILDIE 953
Cdd:COG0178  556 IIDIGPGAGEHGGEVVAQGTPEEILKNPDSLTGQYLSGRKRIP 598
uvrA PRK00349
excinuclease ABC subunit UvrA;
771-953 5.70e-51

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 194.52  E-value: 5.70e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 771 VPCEVCQGARYNRETLEVHYKGKTISEVLDMPIEEAADFFEPVT--------------SIHRYLKTLVDVGLGYVRLGQP 836
Cdd:PRK00349 407 RPCPSCKGKRLKPEALAVKVGGKNIGEVSELSIGEALEFFENLKlseqeakiaepilkEIRERLKFLVDVGLDYLTLSRS 486
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 837 APTLSGGEAQRVKLAAELqkrSAGRT--IYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNLDVIKTADWVIDM 914
Cdd:PRK00349 487 AGTLSGGEAQRIRLATQI---GSGLTgvLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDEDTIRAADYIVDI 563
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 494899544 915 GPEGGTGGGTVIAEGTPEDIAEVPESHTGGFLADILDIE 953
Cdd:PRK00349 564 GPGAGVHGGEVVASGTPEEIMKNPNSLTGQYLSGKKKIE 602
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
406-587 2.30e-50

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: 178.58  E-value: 2.30e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 406 YMRDIPCPVCQGARLRPEILSVTldhpvYPSKSIADVCALSVADCAEYLsglqldsrqKAIAGpvlkeVQARITFLLDVG 485
Cdd:cd03271   97 EIRELFCEVCKGKRYNRETLEVR-----YKGKSIADVLDMTVEEALEFF---------ENIPK-----IARKLQTLCDVG 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 486 LDYLSLARAAGSLSGGEAQRIRLATQIGSGLAG-VLYVLDEPSIGLHQRDNRRLIDTLTRLRDLGNTLIVVEHDEDTIRA 564
Cdd:cd03271  158 LGYIKLGQPATTLSGGEAQRIKLAKELSKRSTGkTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKC 237
                        170       180
                 ....*....|....*....|...
gi 494899544 565 ADWIVDIGPRAGEHGGHVVHSGN 587
Cdd:cd03271  238 ADWIIDLGPEGGDGGGQVVASGT 260
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
770-947 3.71e-49

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


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 188.68  E-value: 3.71e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  770 YVPCEVCQGARYNRETLEVHYKGKTISEVLDMPIEEAADFFEPVT--------------SIHRYLKTLVDVGLGYVRLGQ 835
Cdd:TIGR00630 405 ERPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFNQLTltpeekkiaeevlkEIRERLGFLIDVGLDYLSLSR 484
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  836 PAPTLSGGEAQRVKLAAELQKRSAGrTIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNLDVIKTADWVIDMG 915
Cdd:TIGR00630 485 AAGTLSGGEAQRIRLATQIGSGLTG-VLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVIDIG 563
                         170       180       190
                  ....*....|....*....|....*....|..
gi 494899544  916 PEGGTGGGTVIAEGTPEDIAEVPESHTGGFLA 947
Cdd:TIGR00630 564 PGAGEHGGEVVASGTPEEILANPDSLTGQYLS 595
UvrA_DNA-bind pfam17755
UvrA DNA-binding domain;
295-404 7.78e-48

UvrA DNA-binding domain;


Pssm-ID: 465484 [Multi-domain]  Cd Length: 110  Bit Score: 165.34  E-value: 7.78e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  295 DEELVVPDPDLSLSEGAIAPWSGGHNAdYFLRLMTGLADQMDFDVDTPWKKLPVKARKALLNGSDHQVHVKFRNRYGRTR 374
Cdd:pfam17755   1 DPDLVIPDPSLSLAEGAIAPWGKKRSS-YYFQLLEALAKHYGFDLDTPFKDLPEEQQDIILYGSGEEIIVFYYSRGGRTR 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 494899544  375 SYYTEFEGVMSFLSRRMEQTESDAMKERYE 404
Cdd:pfam17755  80 TYTKPFEGVIPNLERRYRETDSESVREELE 109
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
410-917 1.82e-47

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 185.03  E-value: 1.82e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  410 IPCPVCQGARLRPEILSVTldhpvYPSKSIADVCALSVADCAEYLsglqldsrqkaIAGPVLKEvqaRITFLLDVGLDYL 489
Cdd:PRK00635  741 IPCPSCLGKRFLPQVLEVR-----YKGKNIADILEMTAYEAEKFF-----------LDEPSIHE---KIHALCSLGLDYL 801
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  490 SLARAAGSLSGGEAQRIRLATQIgsgLAGV----LYVLDEPSIGLHQRDNRRLIDTLTRLRDLGNTLIVVEHDEDTIRAA 565
Cdd:PRK00635  802 PLGRPLSSLSGGEIQRLKLAYEL---LAPSkkptLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVA 878
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  566 DWIVDIGPRAGEHGGHVVHSGNYRDLLKNRKSLTGA---YLSGRESLPVPAIRRPINRK-RQLTVVGAREHNLRGIDVAF 641
Cdd:PRK00635  879 DYVLELGPEGGNLGGYLLASCSPEELIHLHTPTAKAlrpYLSSPQELPYLPDPSPKPPVpADITIKNAYQHNLKHIDLSL 958
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  642 PLGVLTAVTGVSGSGKSTLVNDI-----------------------------------LATVLANKLNGARQvPGRHKRI 686
Cdd:PRK00635  959 PRNALTAVTGPSASGKHSLVFDIlyaagniayaelfppyirqalikktplpsvdkvtgLSPVIAIEKTSASK-NSNHSVA 1037
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  687 ------NGLDQLDKLVRVDQSPIGRTP--RSNP---------------ATYTGVFDKIRTLFAATTEAKVRGY------- 736
Cdd:PRK00635 1038 saleisNGLEKLFARLGHPYSPLSGDAlrKITPqtiaeellthytkgyVTITSPIPKEEDLFIYLQEKLKEGFlklyane 1117
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  737 --------------QP------------------------------------------------------GR-------- 740
Cdd:PRK00635 1118 qfydldeplptsleNPaiviqhtkiseknlssllssltlafslsssiclhieyagtslsltyrlgwqdssGNlypnittp 1197
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  741 -FSFNVKGGRCEACTGEGTI-KIEM-----------------NFLPDVYV------------------------------ 771
Cdd:PRK00635 1198 lLSRDHEEGLCPLCHGKGFIlKCSLlphkekiahytplslftLFFPNQDPkpvypllkelgipsialfqeldtlsfeslc 1277
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  772 ---------------------------------PCEVCQGARYNRETLEVHYKGKTISEVLDMPIEEAADFFEP------ 812
Cdd:PRK00635 1278 lgtqqhpglnallmeamlmeseeplppplisktPCNQCQGLGVYTYAHCVRIHNTSLSDIYQEDVTFLKKFLLTihddee 1357
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  813 ---VTSIHRYLKTLVDVGLGYVRLGQPAPTLSGGEAQRVKLAaelQKRSAGRT--IYILDEPTTGLHFEDIKKLLGVING 887
Cdd:PRK00635 1358 psiIQDLLNRLTFIDKVGLSYITLGQEQDTLSDGEHYRLHLA---KKISSNLTdiIYLLEDPLSGLHPQDAPTLLQLIKE 1434
                         730       740       750
                  ....*....|....*....|....*....|
gi 494899544  888 LVDKGNTVIVIEHNLDVIKTADWVIDMGPE 917
Cdd:PRK00635 1435 LVTNNNTVIATDRSGSLAEHADHLIHLGPG 1464
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
450-586 2.08e-47

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: 166.73  E-value: 2.08e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 450 CAEYLSGLQLDSRQKAIagpVLKEVQaritFLLDVGLDYLSLARAAGSLSGGEAQRIRLATQIGSGLAGVLYVLDEPSIG 529
Cdd:cd03238   47 KARLISFLPKFSRNKLI---FIDQLQ----FLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPGTLFILDEPSTG 119
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 494899544 530 LHQRDNRRLIDTLTRLRDLGNTLIVVEHDEDTIRAADWIVDIGPRAGEHGGHVVHSG 586
Cdd:cd03238  120 LHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDFGPGSGKSGGKVVFSG 176
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
626-929 2.45e-46

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: 165.89  E-value: 2.45e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 626 VVGAREHNLRGIDVAFPLGVLTAVTGVSGSGKSTLVNDILATVLANKLNG-----ARQVPGRHKRINgLDQLDKL---VR 697
Cdd:cd03270    3 VRGAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIYAEGQRRYVEslsayARQFLGQMDKPD-VDSIEGLspaIA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 698 VDQSPIGRTPRSNPATYTGVFDKIRTLFAatteakvrgyqpgrfsfnvkggrceactgegtikiemnflpdvyvpcevcq 777
Cdd:cd03270   82 IDQKTTSRNPRSTVGTVTEIYDYLRLLFA--------------------------------------------------- 110
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 778 garynREtlevhykgktisevldmpieeaadffepvtSIHRYLKTLVDVGLGYVRLGQPAPTLSGGEAQRVKLAAELQKR 857
Cdd:cd03270  111 -----RV------------------------------GIRERLGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIGSG 155
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494899544 858 SAGrTIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNLDVIKTADWVIDMGPEGGTGGGTVIAEG 929
Cdd:cd03270  156 LTG-VLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDIGPGAGVHGGEIVAQG 226
UvrA_inter pfam17760
UvrA interaction domain; This domain found in UvrA proteins interacts with the UvrB protein.
131-239 5.42e-46

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


Pssm-ID: 436020 [Multi-domain]  Cd Length: 109  Bit Score: 160.34  E-value: 5.42e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  131 QTPQQIVDQVLEMDEGTRFQVLAPVVRTRKGEFVDLFADLQTQGFSRARVDGVVHQLTDPPKLKKQEKHDIEVVIDRLVV 210
Cdd:pfam17760   1 QTVDQIVDRILALPEGTKIQILAPVVRGRKGEHKELLDDLRKQGFVRVRVDGEIYDLDDEPKLDKNKKHTIEVVVDRLVV 80
                          90       100
                  ....*....|....*....|....*....
gi 494899544  211 KSSAKQRLTDSVETGLRLADGIIVLDFVD 239
Cdd:pfam17760  81 KEDNRSRLADSVETALKLGKGLVIVLVLD 109
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
770-953 1.22e-29

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 128.02  E-value: 1.22e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  770 YVPCEVCQGARYNRETLEVHYKGKTISEVLDMPIEEAADFFEPVT----SIHRYLK-------TLVDVGLGYVRLGQPAP 838
Cdd:PRK00635  396 ATSCPRCQGTGLGDYANAATWHGKTFAEFQQMSLQELFIFLSQLPskslSIEEVLQglksrlsILIDLGLPYLTPERALA 475
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  839 TLSGGEAQRVKLAAELQKRSAGRTiYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNLDVIKTADWVIDMGPEG 918
Cdd:PRK00635  476 TLSGGEQERTALAKHLGAELIGIT-YILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMISLADRIIDIGPGA 554
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 494899544  919 GTGGGTVIAEGTPEDIAEVPESHTGGFLADILDIE 953
Cdd:PRK00635  555 GIFGGEVLFNGSPREFLAKSDSLTAKYLRQELTIP 589
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
5-149 3.55e-21

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: 94.22  E-value: 3.55e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544   5 LIVRGAREHNLRGIDVDLPRDSLIVFTGLSGSGKSSLAFDTIFAegqrryveslSAYARQFLGQMDKPDVDFIEGL---S 81
Cdd:cd03271    1 LTLKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYP----------ALARRLHLKKEQPGNHDRIEGLehiD 70
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494899544  82 PAVSIDQKSTNRNPRSTVGTITEVYDYLRLLYaragrahCPEC-GAAIAKQTPQ-----QIVDQVLEM--DEGTRF 149
Cdd:cd03271   71 KVIVIDQSPIGRTPRSNPATYTGVFDEIRELF-------CEVCkGKRYNRETLEvrykgKSIADVLDMtvEEALEF 139
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
818-917 1.18e-19

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: 87.03  E-value: 1.18e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 818 RYLKTLVDVGLGYVRLGqpaptLSGGEAQRVKLAAELQKRS-AGRTIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVI 896
Cdd:cd03227   61 GCIVAAVSAELIFTRLQ-----LSGGEKELSALALILALASlKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVI 135
                         90       100
                 ....*....|....*....|.
gi 494899544 897 VIEHNLDVIKTADWVIDMGPE 917
Cdd:cd03227  136 VITHLPELAELADKLIHIKKV 156
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
411-605 7.44e-19

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 92.58  E-value: 7.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  411 PCPVCQGARLRPEILSVtldhpVYPSKSIADVCALSVADCAEYLsglqldsrqkaiagPVLKEVQARITFLLDVGLDYLS 490
Cdd:PRK00635 1632 PCPTCSGFRIQPLAQEV-----VYEGKHFGQLLQTPIEEVAETF--------------PFLKKIQKPLQALIDNGLGYLP 1692
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  491 LARAAGSLSGGEAQRIRLATQIG-SGLAGVLYVLDEPSIGLHQRDNRRLIDTLTRLRDLGNTLIVVEHDEDTIRAADWIV 569
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYlPPKHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALLKQADYLI 1772
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 494899544  570 DIGPRAGEHGGHVVHSGNYRDLLKNRKSLTGAYLSG 605
Cdd:PRK00635 1773 EMGPGSGKTGGKILFSGPPKDISASKDSLLKTYMCN 1808
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
463-574 3.49e-17

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


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 79.71  E-value: 3.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 463 QKAIAGPVLKEVQARITflldVGLDYLSLARAAGSLSGGEAQRIRLATQIG--SGLAGVLYVLDEPSIGLHQRDNRRLID 540
Cdd:cd03227   47 GAQSATRRRSGVKAGCI----VAAVSAELIFTRLQLSGGEKELSALALILAlaSLKPRPLYILDEIDRGLDPRDGQALAE 122
                         90       100       110
                 ....*....|....*....|....*....|....
gi 494899544 541 TLTRLRDLGNTLIVVEHDEDTIRAADWIVDIGPR 574
Cdd:cd03227  123 AILEHLVKGAQVIVITHLPELAELADKLIHIKKV 156
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
7-69 1.37e-16

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: 78.52  E-value: 1.37e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494899544   7 VRGAREHNLRGIDVDLPRDSLIVFTGLSGSGKSSLAFDTIFAEGQRRYVESLSAYARQ---FLGQM 69
Cdd:cd03238    3 VSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKARLISFLPKFSRNkliFIDQL 68
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
838-914 1.24e-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: 75.36  E-value: 1.24e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494899544 838 PTLSGGEAQRVKLAAELQKRsagRTIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNLDVIKTA-DWVIDM 914
Cdd:cd00267   79 PQLSGGQRQRVALARALLLN---PDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAaDRVIVL 153
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
472-598 8.66e-15

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


Pssm-ID: 440739 [Multi-domain]  Cd Length: 230  Bit Score: 74.68  E-value: 8.66e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 472 KEVQARITFLLD-VGLDYLsLARAAGSLSGGEAQRirLAtqigsgLAGVL------YVLDEPSIGLHQRDNRRLIDTLTR 544
Cdd:COG1122  109 EEIRERVEEALElVGLEHL-ADRPPHELSGGQKQR--VA------IAGVLamepevLVLDEPTAGLDPRGRRELLELLKR 179
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 494899544 545 LRDLGNTLIVVEHD-EDTIRAADWIVDIgprageHGGHVVHSGNYRDLLKNRKSL 598
Cdd:COG1122  180 LNKEGKTVIIVTHDlDLVAELADRVIVL------DDGRIVADGTPREVFSDYELL 228
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
623-912 7.31e-14

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: 71.41  E-value: 7.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 623 QLTVVGAREHNLRGIDVAFPLGVLTAVTGVSGSGKSTLVNDILatvlanklngarqvpGRHKRINGLdqldklVRVDQSP 702
Cdd:cd03235    4 DLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAIL---------------GLLKPTSGS------IRVFGKP 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 703 IGRTPRsnpatytgvfdKIrtlfaatteakvrGYQPGRFSFNVkggrceactgegtikiemNFLPDVYvpcEVCQGARYN 782
Cdd:cd03235   63 LEKERK-----------RI-------------GYVPQRRSIDR------------------DFPISVR---DVVLMGLYG 97
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 783 RETLEVHYKGKTISEVldmpiEEAadffepvtsihryLKTlvdVGLGYV---RLGQpaptLSGGEAQRVKLA-AELQKRS 858
Cdd:cd03235   98 HKGLFRRLSKADKAKV-----DEA-------------LER---VGLSELadrQIGE----LSGGQQQRVLLArALVQDPD 152
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 494899544 859 agrtIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNLD-VIKTADWVI 912
Cdd:cd03235  153 ----LLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGlVLEYFDRVL 203
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
821-934 7.61e-14

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


Pssm-ID: 440739 [Multi-domain]  Cd Length: 230  Bit Score: 71.98  E-value: 7.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 821 KTLVDVGLGYVRlGQPAPTLSGGEAQRVKLAAELqkrsAGRT-IYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIE 899
Cdd:COG1122  117 EALELVGLEHLA-DRPPHELSGGQKQRVAIAGVL----AMEPeVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVT 191
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 494899544 900 HNLD-VIKTADWVIDM--GpeggtgggTVIAEGTPEDI 934
Cdd:COG1122  192 HDLDlVAELADRVIVLddG--------RIVADGTPREV 221
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
821-912 1.06e-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: 70.96  E-value: 1.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 821 KTLVDVGLgYVRLGQPAPTLSGGEAQRVKLAAELqkrSAGRTIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEH 900
Cdd:cd03225  117 EALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVL---AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTH 192
                         90
                 ....*....|...
gi 494899544 901 NLD-VIKTADWVI 912
Cdd:cd03225  193 DLDlLLELADRVI 205
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
472-934 1.08e-13

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: 74.94  E-value: 1.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 472 KEVQARITFLLD-VGLDYLsLARAAGSLSGGEAQRIRLATQIGSGLAgvLYVLDEPSIGL---HQRDNRRLIDTLTRlrD 547
Cdd:COG1123  117 AEARARVLELLEaVGLERR-LDRYPHQLSGGQRQRVAIAMALALDPD--LLIADEPTTALdvtTQAEILDLLRELQR--E 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 548 LGNTLIVVEHD-EDTIRAADWIVDIgprageHGGHVVHSGNYRDLLKNRKSLTGAYLSGRESLPVPAIRR---PINRKRQ 623
Cdd:COG1123  192 RGTTVLLITHDlGVVAEIADRVVVM------DDGRIVEDGPPEEILAAPQALAAVPRLGAARGRAAPAAAaaePLLEVRN 265
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 624 LTVV-----GAREHNLRGIDVAFPLGVLTAVTGVSGSGKSTLvndilatvlanklngarqvpGRHkrINGLDQLDK-LVR 697
Cdd:COG1123  266 LSKRypvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTL--------------------ARL--LLGLLRPTSgSIL 323
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 698 VDQSPIGRTPRSNPATYTGvfdKIRTLFaatteakvrgyQ-PGRfSFNvkggrceactgegtikiemnflpdvyvpcevc 776
Cdd:COG1123  324 FDGKDLTKLSRRSLRELRR---RVQMVF-----------QdPYS-SLN-------------------------------- 356
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 777 qgaryNRETLevhykGKTISEVLD----MPIEEAADffepvtsihRYLKTLVDVGLGYVRLGQPAPTLSGGEAQRVKLAA 852
Cdd:COG1123  357 -----PRMTV-----GDIIAEPLRlhglLSRAERRE---------RVAELLERVGLPPDLADRYPHELSGGQRQRVAIAR 417
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 853 ELqkrSAGRTIYILDEPTTGL----------HFEDIKKLLGVinglvdkgnTVIVIEHNLDVIKT-ADWVIDM--Gpegg 919
Cdd:COG1123  418 AL---ALEPKLLILDEPTSALdvsvqaqilnLLRDLQRELGL---------TYLFISHDLAVVRYiADRVAVMydG---- 481
                        490
                 ....*....|....*
gi 494899544 920 tgggTVIAEGTPEDI 934
Cdd:COG1123  482 ----RIVEDGPTEEV 492
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
826-935 2.35e-13

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: 70.54  E-value: 2.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 826 VGLGYVRlGQPAPTLSGGEAQRVKLAAELqkrsAGR-TIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNLDV 904
Cdd:cd03219  131 VGLADLA-DRPAGELSYGQQRRLEIARAL----ATDpKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDV 205
                         90       100       110
                 ....*....|....*....|....*....|....
gi 494899544 905 IKT-AD--WVIDMGpeggtgggTVIAEGTPEDIA 935
Cdd:cd03219  206 VMSlADrvTVLDQG--------RVIAEGTPDEVR 231
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
464-571 4.92e-13

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


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 67.66  E-value: 4.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 464 KAIAGpVLKEVQARITFL-LDVGLDYLSLARA----AGSLSGGEAQRIRLATQIGsgLAGVLYVLDEPSIGLHQRDNRRL 538
Cdd:cd00267   43 RAIAG-LLKPTSGEILIDgKDIAKLPLEELRRrigyVPQLSGGQRQRVALARALL--LNPDLLLLDEPTSGLDPASRERL 119
                         90       100       110
                 ....*....|....*....|....*....|....
gi 494899544 539 IDTLTRLRDLGNTLIVVEHDEDTI-RAADWIVDI 571
Cdd:cd00267  120 LELLRELAEEGRTVIIVTHDPELAeLAADRVIVL 153
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
472-569 1.43e-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: 67.88  E-value: 1.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 472 KEVQARITFLLD-VGLDYLsLARAAGSLSGGEAQRirLAtqigsgLAGVL------YVLDEPSIGLHQRDNRRLIDTLTR 544
Cdd:cd03225  109 EEIEERVEEALElVGLEGL-RDRSPFTLSGGQKQR--VA------IAGVLamdpdiLLLDEPTAGLDPAGRRELLELLKK 179
                         90       100
                 ....*....|....*....|....*.
gi 494899544 545 LRDLGNTLIVVEHDEDTIRA-ADWIV 569
Cdd:cd03225  180 LKAEGKTIIIVTHDLDLLLElADRVI 205
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
839-915 9.87e-12

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: 65.36  E-value: 9.87e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494899544 839 TLSGGEAQRVKLAAELqkrSAGRTIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNLDVI-KTADWVIDMG 915
Cdd:cd03226  126 SLSGGQKQRLAIAAAL---LSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLaKVCDRVLLLA 200
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
622-936 1.69e-11

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: 67.86  E-value: 1.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 622 RQLTVVGAREHN-LRGIDVAFPLGVLTAVTGVSGSGKSTLVNDILatvlanklngarqvpGRHK------RING--LDQL 692
Cdd:COG4988  340 EDVSFSYPGGRPaLDGLSLTIPPGERVALVGPSGAGKSTLLNLLL---------------GFLPpysgsiLINGvdLSDL 404
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 693 D------KLVRVDQSPigrtprsnpatytgvfdkirTLFAATteakVRgyqpgrfsFNVKGGRCEActgegtikiemnfl 766
Cdd:COG4988  405 DpaswrrQIAWVPQNP--------------------YLFAGT----IR--------ENLRLGRPDA-------------- 438
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 767 pdvyvpcevcqgarynretlevhykgkTISEvldmpIEEAADffepVTSIHRYLKTLVDvGLGYvRLGQPAPTLSGGEAQ 846
Cdd:COG4988  439 ---------------------------SDEE-----LEAALE----AAGLDEFVAALPD-GLDT-PLGEGGRGLSGGQAQ 480
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 847 RVKLA-AELQKRSagrtIYILDEPTTGLHFEDIKKLLGVINGLVdKGNTVIVIEHNLDVIKTADWVIDMgpeggtGGGTV 925
Cdd:COG4988  481 RLALArALLRDAP----LLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQADRILVL------DDGRI 549
                        330
                 ....*....|.
gi 494899544 926 IAEGTPEDIAE 936
Cdd:COG4988  550 VEQGTHEELLA 560
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
485-594 2.53e-11

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: 67.48  E-value: 2.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 485 GLDYLSLARAAGsLSGGEAQRIRLATQIgsgLAGV-LYVLDEPSIGLHQRDNRRLIDTLTRLRDlGNTLIVVEHDEDTIR 563
Cdd:COG4988  462 GLDTPLGEGGRG-LSGGQAQRLALARAL---LRDApLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLA 536
                         90       100       110
                 ....*....|....*....|....*....|.
gi 494899544 564 AADWIVDIgprageHGGHVVHSGNYRDLLKN 594
Cdd:COG4988  537 QADRILVL------DDGRIVEQGTHEELLAK 561
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
839-934 3.26e-11

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 64.34  E-value: 3.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 839 TLSGGEAQRVKLA-AELQKRSagrtIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNLD-VIKTADWVIDMGP 916
Cdd:COG1121  139 ELSGGQQQRVLLArALAQDPD----LLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGaVREYFDRVLLLNR 214
                         90
                 ....*....|....*...
gi 494899544 917 EggtgggtVIAEGTPEDI 934
Cdd:COG1121  215 G-------LVAHGPPEEV 225
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
816-936 3.31e-11

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 64.31  E-value: 3.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 816 IHRYLKTlvdVGLGYVRlGQPAPTLSGGEAQRVKLAAELQKRSAgrtIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTV 895
Cdd:COG1131  112 IDELLEL---FGLTDAA-DRKVGTLSGGMKQRLGLALALLHDPE---LLILDEPTSGLDPEARRELWELLRELAAEGKTV 184
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 494899544 896 IVIEHNLDVI-KTADWV--IDMGpeggtgggTVIAEGTPEDIAE 936
Cdd:COG1131  185 LLSTHYLEEAeRLCDRVaiIDKG--------RIVADGTPDELKA 220
cbiO PRK13644
energy-coupling factor transporter ATPase;
787-960 7.95e-10

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 60.77  E-value: 7.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 787 EVHYKGKTISEVLDMPIEEAAdfFEPVTSIHRYLKTLVDVGLGYVRLGQPApTLSGGEAQRVKLAAELqkrSAGRTIYIL 866
Cdd:PRK13644  87 ETQFVGRTVEEDLAFGPENLC--LPPIEIRKRVDRALAEIGLEKYRHRSPK-TLSGGQGQCVALAGIL---TMEPECLIF 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 867 DEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNLDVIKTADWVIDMgpeggtGGGTVIAEGTPEDIAEVPESHTGGF- 945
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVM------DRGKIVLEGEPENVLSDVSLQTLGLt 234
                        170
                 ....*....|....*
gi 494899544 946 LADILDIEESVATAG 960
Cdd:PRK13644 235 PPSLIELAENLKMHG 249
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
840-912 1.52e-09

ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213197 [Multi-domain]  Cd Length: 173  Bit Score: 58.18  E-value: 1.52e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494899544 840 LSGGEAQRVKLAAELQKRSAgrtIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNLDVI-KTADWVI 912
Cdd:cd03230   96 LSGGMKQRLALAQALLHDPE---LLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAeRLCDRVA 166
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
840-934 2.38e-09

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 59.64  E-value: 2.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 840 LSGGEAQRVKLAAELQKRSagrTIYILDEPTTGLHFEDIKKLLGVINGLVDKGN-TVIVIEHNLDVIKTADWVIDMgpeg 918
Cdd:PRK13635 141 LSGGQKQRVAIAGVLALQP---DIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQADRVIVM---- 213
                         90
                 ....*....|....*.
gi 494899544 919 gtGGGTVIAEGTPEDI 934
Cdd:PRK13635 214 --NKGEILEEGTPEEI 227
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
840-914 2.38e-09

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 57.39  E-value: 2.38e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494899544 840 LSGGEAQRVKLA-AELQKRSagrtIYILDEPTTGLhfeDI---KKLLGVINGLvDKGNTVIVIEHNLDVIKTADWVIDM 914
Cdd:cd03228   97 LSGGQRQRIAIArALLRDPP----ILILDEATSAL---DPeteALILEALRAL-AKGKTVIVIAHRLSTIRDADRIIVL 167
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
818-940 2.43e-09

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: 61.07  E-value: 2.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 818 RYLKTLVDVGLGyVRLGQPAPTLSGGEAQRVKLAAELQKRSAgrtIYILDEPTTGLHFEDIKKLLGVINGLV-DKGNTVI 896
Cdd:COG1123  122 RVLELLEAVGLE-RRLDRYPHQLSGGQRQRVAIAMALALDPD---LLIADEPTTALDVTTQAEILDLLRELQrERGTTVL 197
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 494899544 897 VIEHNLDVI-KTADWVIDMgpeggtGGGTVIAEGTPEDIAEVPES 940
Cdd:COG1123  198 LITHDLGVVaEIADRVVVM------DDGRIVEDGPPEEILAAPQA 236
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
472-569 4.30e-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: 57.54  E-value: 4.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 472 KEVQARITFLLD-VGLDYLSlARAAGSLSGGEAQRIRLAtQIgsgLAG--VLYVLDEPSIGLHQRDNRRLIDTLTRLRDL 548
Cdd:cd03235  107 KADKAKVDEALErVGLSELA-DRQIGELSGGQQQRVLLA-RA---LVQdpDLLLLDEPFAGVDPKTQEDIYELLRELRRE 181
                         90       100
                 ....*....|....*....|..
gi 494899544 549 GNTLIVVEHDEDTI-RAADWIV 569
Cdd:cd03235  182 GMTILVVTHDLGLVlEYFDRVL 203
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
840-912 5.22e-09

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: 56.28  E-value: 5.22e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494899544 840 LSGGEAQRVKLAAELqkrSAGRTIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNLD-VIKTADWVI 912
Cdd:cd03216   83 LSVGERQMVEIARAL---ARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDeVFEIADRVT 153
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
835-934 8.43e-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: 57.36  E-value: 8.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 835 QPAPTLSGGEAQRVKLAAELqkrsAGRT-IYILDEPTTGLhfeDIK---KLLGVINGLV-DKGNTVIVIEHNLD-VIKTA 908
Cdd:COG1120  133 RPVDELSGGERQRVLIARAL----AQEPpLLLLDEPTSHL---DLAhqlEVLELLRRLArERGRTVVMVLHDLNlAARYA 205
                         90       100
                 ....*....|....*....|....*...
gi 494899544 909 DWVIDM--GpeggtgggTVIAEGTPEDI 934
Cdd:COG1120  206 DRLVLLkdG--------RIVAQGPPEEV 225
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
840-914 1.01e-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: 55.69  E-value: 1.01e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494899544 840 LSGGEAQRVKLAAELQKRsagRTIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNLDVIKTADWVIDM 914
Cdd:cd03246   97 LSGGQRQRLGLARALYGN---PRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVL 168
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
456-569 1.02e-08

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: 57.06  E-value: 1.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 456 GLQLDSRQKAIAGPV---LKEVQARITFLLD-VGLDYLsLARAAGSLSGGEAQRIrlatQIGSGLAG---VLyVLDEPSI 528
Cdd:cd03219   99 AAQARTGSGLLLARArreEREARERAEELLErVGLADL-ADRPAGELSYGQQRRL----EIARALATdpkLL-LLDEPAA 172
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 494899544 529 GLHQRDNRRLIDTLTRLRDLGNTLIVVEHDEDTIRA-ADWIV 569
Cdd:cd03219  173 GLNPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVT 214
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
792-916 1.09e-08

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 56.36  E-value: 1.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 792 GKTISEVLDMPieeaADFFEPVTSIHRYLKTLVDVGLGYVRLGQPAPTLSGGEAQRVKLAAELQKRsagRTIYILDEPTT 871
Cdd:COG4619   87 GGTVRDNLPFP----FQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQ---PDVLLLDEPTS 159
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 494899544 872 GLHFEDIKKLLGVINGLV-DKGNTVIVIEHNLDVIKT-ADWVIDMGP 916
Cdd:COG4619  160 ALDPENTRRVEELLREYLaEEGRAVLWVSHDPEQIERvADRVLTLEA 206
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
839-913 2.13e-08

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 57.87  E-value: 2.13e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494899544 839 TLSGGEAQRVKLAAELQKRSagrTIYILDEPTTGLhfeDIKKLLGV---INGLVDKGNTVIVIEHNLDVIktaDWVID 913
Cdd:COG1245  212 ELSGGELQRVAIAAALLRDA---DFYFFDEPSSYL---DIYQRLNVarlIRELAEEGKYVLVVEHDLAIL---DYLAD 280
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
496-595 2.58e-08

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];


Pssm-ID: 441875 [Multi-domain]  Cd Length: 711  Bit Score: 57.92  E-value: 2.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 496 GSLSGGEAQRIrlatqigsGLAGVLY------VLDEPSIGLHQRDNRRLIDTLTRLRDlGNTLIVVEHDEDTIRAADWIV 569
Cdd:COG2274  610 SNLSGGQRQRL--------AIARALLrnprilILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIRLADRII 680
                         90       100
                 ....*....|....*....|....*.
gi 494899544 570 DIgprageHGGHVVHSGNYRDLLKNR 595
Cdd:COG2274  681 VL------DKGRIVEDGTHEELLARK 700
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
484-604 2.61e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 56.57  E-value: 2.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 484 VGLDYLSLARAAGSLSGGEAQRIrlatqigsGLAGVL------YVLDEPSIGLHQRDNRRLIDTLTRL-RDLGNTLIVVE 556
Cdd:PRK13634 132 VGLPEELLARSPFELSGGQMRRV--------AIAGVLamepevLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVT 203
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 494899544 557 HD-EDTIRAADWIVDIgprageHGGHVVHSGNYRDLLKNRKSLTGAYLS 604
Cdd:PRK13634 204 HSmEDAARYADQIVVM------HKGTVFLQGTPREIFADPDELEAIGLD 246
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
607-914 2.81e-08

thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD


Pssm-ID: 274323 [Multi-domain]  Cd Length: 529  Bit Score: 57.68  E-value: 2.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  607 ESLPVPAIRRPINRKRQLTVV-GAREHNLRGIDVAFPLGVLTAVTGVSGSGKSTLVNDILatvlanklnGARQVPGRHKR 685
Cdd:TIGR02857 310 GKAPVTAAPASSLEFSGVSVAyPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLL---------GFVDPTEGSIA 380
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  686 ING--LDQLDKLVRVDQ-SPIGRTPrsnpatytgvfdkirTLFAATTEAKVRGYQPgrfsfnvkggrceactgegtikie 762
Cdd:TIGR02857 381 VNGvpLADADADSWRDQiAWVPQHP---------------FLFAGTIAENIRLARP------------------------ 421
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  763 mnflpdvyvpcevcqgarynretlevhykgktisEVLDMPIEEAADffepVTSIHRYLKTLvdvGLGY-VRLGQPAPTLS 841
Cdd:TIGR02857 422 ----------------------------------DASDAEIREALE----RAGLDEFVAAL---PQGLdTPIGEGGAGLS 460
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494899544  842 GGEAQRVKLAAELQKrsaGRTIYILDEPTTGLHFEDIKKLLGVINGLVdKGNTVIVIEHNLDVIKTADWVIDM 914
Cdd:TIGR02857 461 GGQAQRLALARAFLR---DAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALAALADRIVVL 529
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
835-956 2.88e-08

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 55.79  E-value: 2.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 835 QPAPTLSGGEAQRVKLAAELQKRSAgrtIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNLD-VIKTADWVID 913
Cdd:PRK11231 134 RRLTDLSGGQRQRAFLAMVLAQDTP---VVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNqASRYCDHLVV 210
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 494899544 914 MgpeggtGGGTVIAEGTPEDIAevpeshTGGFLADILDIEESV 956
Cdd:PRK11231 211 L------ANGHVMAQGTPEEVM------TPGLLRTVFDVEAEI 241
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
431-571 3.57e-08

thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD


Pssm-ID: 274323 [Multi-domain]  Cd Length: 529  Bit Score: 57.30  E-value: 3.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  431 HPVYPSKSIADVCALSVADCAEylsglqLDSRQKAIAGPVLKEVQAritflLDVGLDYLSLARAAGsLSGGEAQRIRLAT 510
Cdd:TIGR02857 404 HPFLFAGTIAENIRLARPDASD------AEIREALERAGLDEFVAA-----LPQGLDTPIGEGGAG-LSGGQAQRLALAR 471
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494899544  511 QIGSGlAGVLyVLDEPSIGLHQRDNRRLIDTLTRLRDlGNTLIVVEHDEDTIRAADWIVDI 571
Cdd:TIGR02857 472 AFLRD-APLL-LLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAALADRIVVL 529
cbiO PRK13640
energy-coupling factor transporter ATPase;
821-939 3.86e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 55.96  E-value: 3.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 821 KTLVDVGLGYVRLGQPApTLSGGEAQRVKLAAELqkrSAGRTIYILDEPTTGLHFEDIKKLLGVINGLVDKGN-TVIVIE 899
Cdd:PRK13640 126 DVLADVGMLDYIDSEPA-NLSGGQKQRVAIAGIL---AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNlTVISIT 201
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 494899544 900 HNLDVIKTADWVI--DMGpeggtgggTVIAEGTPEDIAEVPE 939
Cdd:PRK13640 202 HDIDEANMADQVLvlDDG--------KLLAQGSPVEIFSKVE 235
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
634-914 4.30e-08

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 54.16  E-value: 4.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 634 LRGIDVAFPLGVLTAVTGVSGSGKSTLVNdILATVLAnKLNGARQVpGRHKRINGLDQldklvrvdqspIGRTPRSNPAT 713
Cdd:NF040873   8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLK-VLAGVLR-PTSGTVRR-AGGARVAYVPQ-----------RSEVPDSLPLT 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 714 ytgvfdkIRTLFAATTEAKvRGyqPGRfsfnvkggrceactgegtikiemnflpdvyvpcevcqgaRYNRETLEVhykgk 793
Cdd:NF040873  74 -------VRDLVAMGRWAR-RG--LWR---------------------------------------RLTRDDRAA----- 99
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 794 tisevldmpIEEAadffepvtsihrylktLVDVGLGYVRlGQPAPTLSGGEAQRVKLAAELQKRSagrTIYILDEPTTGL 873
Cdd:NF040873 100 ---------VDDA----------------LERVGLADLA-GRQLGELSGGQRQRALLAQGLAQEA---DLLLLDEPTTGL 150
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 494899544 874 HFEDIKKLLGVINGLVDKGNTVIVIEHNLDVIKTADWVIDM 914
Cdd:NF040873 151 DAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
839-903 5.04e-08

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: 53.59  E-value: 5.04e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 839 TLSGGEAQRVKLAAEL-QKrsagRTIYILDEPTTGLhfeDIK---KLLGVINGLVD-KGNTVIVIEHNLD 903
Cdd:cd03214   97 ELSGGERQRVLLARALaQE----PPILLLDEPTSHL---DIAhqiELLELLRRLAReRGKTVVMVLHDLN 159
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
825-914 7.85e-08

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: 52.45  E-value: 7.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 825 DVGLGYVrlgqpaPTLSGGEAQRVKLAAELQKRSagrTIYILDEPTTGLhfeDIKKLLGVINGLVDKGNTVIVIEHNLDV 904
Cdd:cd03221   62 TVKIGYF------EQLSGGEKMRLALAKLLLENP---NLLLLDEPTNHL---DLESIEALEEALKEYPGTVILVSHDRYF 129
                         90
                 ....*....|.
gi 494899544 905 I-KTADWVIDM 914
Cdd:cd03221  130 LdQVATKIIEL 140
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
491-594 8.10e-08

ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.


Pssm-ID: 213191 [Multi-domain]  Cd Length: 222  Bit Score: 53.98  E-value: 8.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 491 LARAAGSLSGGEAQRirLAtqIGSGLAG--VLYVLDEPSIGLHQRDNRRLIDTLTRLRDLGNTLIVVEHDedtIRAADWI 568
Cdd:cd03224  126 RKQLAGTLSGGEQQM--LA--IARALMSrpKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQN---ARFALEI 198
                         90       100
                 ....*....|....*....|....*...
gi 494899544 569 VDigpRAG--EHgGHVVHSGNYRDLLKN 594
Cdd:cd03224  199 AD---RAYvlER-GRVVLEGTAAELLAD 222
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
788-952 8.27e-08

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


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 54.34  E-value: 8.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 788 VHYKGKTISEVLDMPIEeaaDFFEPVTS---IHRYLKTLVDVGLGYVRL-GQPAPTLSGGEAQRVKLAAELQKRSagrTI 863
Cdd:cd03237   63 VSYKPQYIKADYEGTVR---DLLSSITKdfyTHPYFKTEIAKPLQIEQIlDREVPELSGGELQRVAIAACLSKDA---DI 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 864 YILDEPTTGLHFEDIKKLLGVINGLVDKGN-TVIVIEHnlDVIkTADWVIDmgpeggtggGTVIAEGTP--EDIAEVPES 940
Cdd:cd03237  137 YLLDEPSAYLDVEQRLMASKVIRRFAENNEkTAFVVEH--DII-MIDYLAD---------RLIVFEGEPsvNGVANPPQS 204
                        170
                 ....*....|....*
gi 494899544 941 HTGG---FLAdILDI 952
Cdd:cd03237  205 LRSGmnrFLK-NLDI 218
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
634-914 9.41e-08

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


Pssm-ID: 213222 [Multi-domain]  Cd Length: 218  Bit Score: 53.65  E-value: 9.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 634 LRGIDVAFPLGVLTAVTGVSGSGKSTLVNdILAtvlanklngarqvpgrhkrinGLDQLDK-LVRVDQSPIGRTPrsnpa 712
Cdd:cd03255   20 LKGVSLSIEKGEFVAIVGPSGSGKSTLLN-ILG---------------------GLDRPTSgEVRVDGTDISKLS----- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 713 tytgvfDKIRTLFAATTEAKVrgYQpgrfSFNVkggrceactgegtikiemnfLPDVyvpcevcqgarynretlevhykg 792
Cdd:cd03255   73 ------EKELAAFRRRHIGFV--FQ----SFNL--------------------LPDL----------------------- 97
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 793 kTISEVLDMPIEEAAdffEPVTSIHRYLKTLVD-VGLGYvRLGQPAPTLSGGEAQRVKLAAELQKRSAgrtIYILDEPTT 871
Cdd:cd03255   98 -TALENVELPLLLAG---VPKKERRERAEELLErVGLGD-RLNHYPSELSGGQQQRVAIARALANDPK---IILADEPTG 169
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 494899544 872 GLHFEDIKKLLGVINGLVDK-GNTVIVIEHNLDVIKTADWVIDM 914
Cdd:cd03255  170 NLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEYADRIIEL 213
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
840-905 1.07e-07

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


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 54.29  E-value: 1.07e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494899544 840 LSGGEAQRVKLAAELQKRSagrTIYILDEPTTGLhfeDIKKLLG---VINGLVDKGNTVIVIEHNLDVI 905
Cdd:cd03236  140 LSGGELQRVAIAAALARDA---DFYFFDEPSSYL---DIKQRLNaarLIRELAEDDNYVLVVEHDLAVL 202
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
823-934 1.31e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 54.47  E-value: 1.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 823 LVDVGLGYVRLGQPAPTLSGGEAQRVKLAAELQKRSagrTIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNL 902
Cdd:PRK13631 160 LNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQP---EILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTM 236
                         90       100       110
                 ....*....|....*....|....*....|...
gi 494899544 903 D-VIKTADWVIDMgpeggtGGGTVIAEGTPEDI 934
Cdd:PRK13631 237 EhVLEVADEVIVM------DKGKILKTGTPYEI 263
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
833-934 1.37e-07

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 53.69  E-value: 1.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 833 LGQPAPTLSGGEAQRVKLAAEL-----QKRSAGRTIyILDEPTTGLhfeDI---KKLLGVINGLVDKGNTVIVIEHNLD- 903
Cdd:COG4138  120 LSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEGQLL-LLDEPMNSL---DVaqqAALDRLLRELCQQGITVVMSSHDLNh 195
                         90       100       110
                 ....*....|....*....|....*....|...
gi 494899544 904 VIKTAD--WVIDMGpeggtgggTVIAEGTPEDI 934
Cdd:COG4138  196 TLRHADrvWLLKQG--------KLVASGETAEV 220
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
792-871 2.00e-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: 51.49  E-value: 2.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  792 GKTISEVLDMPIEEAADFFEPVTS-IHRYLKTLVDVGLGYVRLGQPAPTLSGGEAQRVKLAAELQKRSagrTIYILDEPT 870
Cdd:pfam00005  73 RLTVRENLRLGLLLKGLSKREKDArAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKP---KLLLLDEPT 149

                  .
gi 494899544  871 T 871
Cdd:pfam00005 150 A 150
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
817-939 2.50e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 53.27  E-value: 2.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 817 HRYLKTLVDVGLGYVRLGQPApTLSGGEAQRVKLAAELQKRSagrTIYILDEPTTGLHFEDIKKLLGVINGLVDK-GNTV 895
Cdd:PRK13652 116 HRVSSALHMLGLEELRDRVPH-HLSGGEKKRVAIAGVIAMEP---QVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTV 191
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 494899544 896 IVIEHNLDVI-KTADWVIDMgpeggtGGGTVIAEGTPEDIAEVPE 939
Cdd:PRK13652 192 IFSTHQLDLVpEMADYIYVM------DKGRIVAYGTVEEIFLQPD 230
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
839-914 2.78e-07

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


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 52.09  E-value: 2.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 839 TLSGGEAQRVKLAAELQKRSAgrtIYILDEP------TTGLH-FEDikkllgVINGLVDKGNTVIVIEHNLDVIKTADWV 911
Cdd:cd03250  127 NLSGGQKQRISLARAVYSDAD---IYLLDDPlsavdaHVGRHiFEN------CILGLLLNNKTRILVTHQLQLLPHADQI 197

                 ...
gi 494899544 912 IDM 914
Cdd:cd03250  198 VVL 200
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
812-934 2.88e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 52.83  E-value: 2.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 812 PVTSIHRYL-KTLVDVGLgYVRLGQPAPTLSGGEAQRVKLAAELqkrSAGRTIYILDEPTTGLHFEDIKKLLGVINGL-V 889
Cdd:PRK13648 115 PYDEMHRRVsEALKQVDM-LERADYEPNALSGGQKQRVAIAGVL---ALNPSVIILDEATSMLDPDARQNLLDLVRKVkS 190
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 494899544 890 DKGNTVIVIEHNLDVIKTADWVIDMGpeggtgGGTVIAEGTPEDI 934
Cdd:PRK13648 191 EHNITIISITHDLSEAMEADHVIVMN------KGTVYKEGTPTEI 229
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
832-936 3.09e-07

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: 52.05  E-value: 3.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 832 RLGQPAPTLSGGEAQRVKLA-AELQKRSagrtIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNLDVI-KTAD 909
Cdd:cd03224  125 RRKQLAGTLSGGEQQMLAIArALMSRPK----LLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFAlEIAD 200
                         90       100
                 ....*....|....*....|....*....
gi 494899544 910 --WVIDMGpeggtgggTVIAEGTPEDIAE 936
Cdd:cd03224  201 raYVLERG--------RVVLEGTAAELLA 221
cbiO PRK13645
energy-coupling factor transporter ATPase;
460-599 3.47e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 53.09  E-value: 3.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 460 DSRQKAIA-GPV-----LKEVQARITFLLD-VGLDYLSLARAAGSLSGGEAQRIRLATQIGsgLAGVLYVLDEPSIGLHQ 532
Cdd:PRK13645 106 ETIEKDIAfGPVnlgenKQEAYKKVPELLKlVQLPEDYVKRSPFELSGGQKRRVALAGIIA--MDGNTLVLDEPTGGLDP 183
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494899544 533 RDNRRLIDTLTRL-RDLGNTLIVVEHDEDTI-RAADWIVDIgprageHGGHVVHSGNYRDLLKNRKSLT 599
Cdd:PRK13645 184 KGEEDFINLFERLnKEYKKRIIMVTHNMDQVlRIADEVIVM------HEGKVISIGSPFEIFSNQELLT 246
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
833-913 4.04e-07

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 54.04  E-value: 4.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 833 LGQPAPTLSGGEAQRVKLAAELQKrsaGRTIYILDEPTTGLhfeDIKKLLGVINGLVD--KGNTVIVIEHNLDVIktaDW 910
Cdd:PRK13409 206 LDRDISELSGGELQRVAIAAALLR---DADFYFFDEPTSYL---DIRQRLNVARLIRElaEGKYVLVVEHDLAVL---DY 276

                 ...
gi 494899544 911 VID 913
Cdd:PRK13409 277 LAD 279
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
803-932 4.36e-07

ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213220 [Multi-domain]  Cd Length: 236  Bit Score: 51.85  E-value: 4.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 803 IEEAADffepVTSIHRYLKTLVDvglGY-VRLGQPAPTLSGGEAQRVKLAAELQKRSAgrtIYILDEPTTGLHFEDIKKL 881
Cdd:cd03253  107 VIEAAK----AAQIHDKIMRFPD---GYdTIVGERGLKLSGGEKQRVAIARAILKNPP---ILLLDEATSALDTHTEREI 176
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 494899544 882 LGVINgLVDKGNTVIVIEHNLDVIKTADWVIDMGpeggtgGGTVIAEGTPE 932
Cdd:cd03253  177 QAALR-DVSKGRTTIVIAHRLSTIVNADKIIVLK------DGRIVERGTHE 220
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
818-903 4.47e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 52.78  E-value: 4.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 818 RYLKtLVDVGLGYVrlgQPAP-TLSGGEAQRVKLAAELQKRSagrTIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVI 896
Cdd:PRK13651 147 KYIE-LVGLDESYL---QRSPfELSGGQKRRVALAGILAMEP---DFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTII 219

                 ....*..
gi 494899544 897 VIEHNLD 903
Cdd:PRK13651 220 LVTHDLD 226
cbiO PRK13637
energy-coupling factor transporter ATPase;
818-934 4.88e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 52.36  E-value: 4.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 818 RYLKTLVDVGLGYVRLGQPAP-TLSGGEAQRVKLAAELQKRSagrTIYILDEPTTGLHFEDIKKLLGVINGLVDK-GNTV 895
Cdd:PRK13637 122 RVKRAMNIVGLDYEDYKDKSPfELSGGQKRRVAIAGVVAMEP---KILILDEPTAGLDPKGRDEILNKIKELHKEyNMTI 198
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 494899544 896 IVIEHNL-DVIKTADWVIDMgpeggtGGGTVIAEGTPEDI 934
Cdd:PRK13637 199 ILVSHSMeDVAKLADRIIVM------NKGKCELQGTPREV 232
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
839-936 4.91e-07

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];


Pssm-ID: 441875 [Multi-domain]  Cd Length: 711  Bit Score: 53.68  E-value: 4.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 839 TLSGGEAQRVKLA-AELQKRSagrtIYILDEPTTGLHFEDIKKLLGVINGLvDKGNTVIVIEHNLDVIKTADWVIDM--G 915
Cdd:COG2274  611 NLSGGQRQRLAIArALLRNPR----ILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRLSTIRLADRIIVLdkG 685
                         90       100
                 ....*....|....*....|.
gi 494899544 916 peggtgggTVIAEGTPEDIAE 936
Cdd:COG2274  686 --------RIVEDGTHEELLA 698
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
823-916 4.93e-07

ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443308 [Multi-domain]  Cd Length: 206  Bit Score: 51.33  E-value: 4.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 823 LVDVGLGYvRLGQPAPTLSGGEAQRVKLAAELqkrSAGRTIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNL 902
Cdd:COG4133  116 LEAVGLAG-LADLPVRQLSAGQKRRVALARLL---LSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQP 191
                         90
                 ....*....|....
gi 494899544 903 DVIkTADWVIDMGP 916
Cdd:COG4133  192 LEL-AAARVLDLGD 204
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
840-936 5.67e-07

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: 51.90  E-value: 5.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 840 LSGGEAQRVKLAaelqkrsagRTI-----YIL-DEPTTGLhfeD------IKKLlgvINGLVDK-GNTVIVIEHNLD-VI 905
Cdd:COG1127  142 LSGGMRKRVALA---------RALaldpeILLyDEPTAGL---DpitsavIDEL---IRELRDElGLTSVVVTHDLDsAF 206
                         90       100       110
                 ....*....|....*....|....*....|...
gi 494899544 906 KTADWVI--DMGpeggtgggTVIAEGTPEDIAE 936
Cdd:COG1127  207 AIADRVAvlADG--------KIIAEGTPEELLA 231
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
816-934 6.32e-07

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: 52.05  E-value: 6.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  816 IHRYLKTlvdVGLGYVRLGQPApTLSGGEAQRVKLAAELQKRSAgrtIYILDEPTTGLHFEDIKKLLGVINGLVDKGN-T 894
Cdd:TIGR04520 117 VDEALKL---VGMEDFRDREPH-LLSGGQKQRVAIAGVLAMRPD---IIILDEATSMLDPKGRKEVLETIRKLNKEEGiT 189
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 494899544  895 VIVIEHNLDVIKTADWVIDM--GpeggtgggTVIAEGTPEDI 934
Cdd:TIGR04520 190 VISITHDMEEAVLADRVIVMnkG--------KIVAEGTPREI 223
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
498-569 7.35e-07

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 50.07  E-value: 7.35e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494899544 498 LSGGEAQRIRLA------TQIgsglagvlYVLDEPSIGLHQRDNRRLIDTLTRLRDlGNTLIVVEHDEDTIRAADWIV 569
Cdd:cd03228   97 LSGGQRQRIAIArallrdPPI--------LILDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIRDADRII 165
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
491-578 9.26e-07

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


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 50.68  E-value: 9.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 491 LARAAGSLSGGE------AQRIRLATQIGSGLaGVLyVLDEPSIGLhQRDNRR--LIDTLTRLRDLGN-TLIVVEHDEDT 561
Cdd:cd03240  109 LLDMRGRCSGGEkvlaslIIRLALAETFGSNC-GIL-ALDEPTTNL-DEENIEesLAEIIEERKSQKNfQLIVITHDEEL 185
                         90
                 ....*....|....*..
gi 494899544 562 IRAADWIVDIGPRAGEH 578
Cdd:cd03240  186 VDAADHIYRVEKDGRQK 202
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
838-933 1.19e-06

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 50.88  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 838 PTLSGGEAQRVKLA---AEL-QKRSAGRTIYILDEPTTGLhfeDIK---KLLGVINGLVDKGNTVIVIEH--NL-----D 903
Cdd:COG4559  132 QTLSGGEQQRVQLArvlAQLwEPVDGGPRWLFLDEPTSAL---DLAhqhAVLRLARQLARRGGGVVAVLHdlNLaaqyaD 208
                         90       100       110
                 ....*....|....*....|....*....|
gi 494899544 904 VIktadWVIDMGpeggtgggTVIAEGTPED 933
Cdd:COG4559  209 RI----LLLHQG--------RLVAQGTPEE 226
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
838-902 1.27e-06

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 50.93  E-value: 1.27e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494899544 838 PTLSGGEAQRVKLA---AELQKRSAGRTIYILDEPTTGLhfeDIK---KLLGVINGLVDKGN-TVIVIEHNL 902
Cdd:PRK13548 133 PQLSGGEQQRVQLArvlAQLWEPDGPPRWLLLDEPTSAL---DLAhqhHVLRLARQLAHERGlAVIVVLHDL 201
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
467-623 1.29e-06

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 52.42  E-value: 1.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 467 AGPVLKEVQAR-ITFLLDVGL----DYlslarAAGSLSGGEAQRIRLATQIGSGlaGVLYVLDEPSIGLHQRDNRRLIDT 541
Cdd:PRK10535 114 AGLERKQRLLRaQELLQRLGLedrvEY-----QPSQLSGGQQQRVSIARALMNG--GQVILADEPTGALDSHSGEEVMAI 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 542 LTRLRDLGNTLIVVEHDEDTIRAADWIVDIgprageHGGHVVHSGNYrdllknRKSLTGAYLSGRESLPVPAIRRPINRK 621
Cdd:PRK10535 187 LHQLRDRGHTVIIVTHDPQVAAQAERVIEI------RDGEIVRNPPA------QEKVNVAGGTEPVVNTASGWRQFVSGF 254

                 ..
gi 494899544 622 RQ 623
Cdd:PRK10535 255 RE 256
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
785-905 1.30e-06

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 52.12  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 785 TLEVHYKGKTISEVLDMPIEeaaDFFEPVTSIHR--YLKTLVDVGLGYVRL-GQPAPTLSGGEAQRVKLAAELQKRSagr 861
Cdd:PRK13409 399 ELKISYKPQYIKPDYDGTVE---DLLRSITDDLGssYYKSEIIKPLQLERLlDKNVKDLSGGELQRVAIAACLSRDA--- 472
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 494899544 862 TIYILDEPTTGLHFEDIKKLLGVINGLVD-KGNTVIVIEHNLDVI 905
Cdd:PRK13409 473 DLYLLDEPSAHLDVEQRLAVAKAIRRIAEeREATALVVDHDIYMI 517
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
803-915 1.39e-06

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: 50.62  E-value: 1.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 803 IEEAADFFEpvtsIHRYLKTLVDvglGY-VRLGQPAPTLSGGEAQRVKLAAELQKRSAgrtIYILDEPTTGLHFEDIKKL 881
Cdd:cd03249  109 VEEAAKKAN----IHDFIMSLPD---GYdTLVGERGSQLSGGQKQRIAIARALLRNPK---ILLLDEATSALDAESEKLV 178
                         90       100       110
                 ....*....|....*....|....*....|....
gi 494899544 882 LGVINGLVdKGNTVIVIEHNLDVIKTADWVIDMG 915
Cdd:cd03249  179 QEALDRAM-KGRTTIVIAHRLSTIRNADLIAVLQ 211
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
498-571 1.51e-06

ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.


Pssm-ID: 213213 [Multi-domain]  Cd Length: 173  Bit Score: 49.14  E-value: 1.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 498 LSGGEAQRIrlatqigsGLAGVLY------VLDEPSIGLHQRDNRRLIDTLTRLRDLGNTLIVVEHDEDTIRAADWIVDI 571
Cdd:cd03246   97 LSGGQRQRL--------GLARALYgnprilVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVL 168
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
6-52 1.63e-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: 48.90  E-value: 1.63e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 494899544   6 IVRGAREHNLRGIDVDLPRDSLIVFTGLSGSGKSSLAFDTIFAEGQR 52
Cdd:cd03227    2 IVLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGA 48
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
839-936 2.75e-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: 49.86  E-value: 2.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 839 TLSGGEAQRVKLAAELQKRSAgrtIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNLDVI-KTADWV--IDMG 915
Cdd:COG4555  132 ELSTGMKKKVALARALVHDPK---VLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVeALCDRVviLHKG 208
                         90       100
                 ....*....|....*....|.
gi 494899544 916 peggtgggTVIAEGTPEDIAE 936
Cdd:COG4555  209 --------KVVAQGSLDELRE 221
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
818-934 2.97e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 50.08  E-value: 2.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 818 RYLKTLVDVGL-GYVRlgQPAPTLSGGEAQRVKLAAELQKRSagrTIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVI 896
Cdd:PRK13639 117 RVKEALKAVGMeGFEN--KPPHHLSGGQKKRVAIAGILAMKP---EIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITII 191
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 494899544 897 VIEHNLDVIKT-ADWVIDMGpeggtgGGTVIAEGTPEDI 934
Cdd:PRK13639 192 ISTHDVDLVPVyADKVYVMS------DGKIIKEGTPKEV 224
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
480-573 3.33e-06

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 49.04  E-value: 3.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 480 FLLDVGLDYLSLARAAGSLSGGEAQRIRLAtqigSGLA---GVLyVLDEPSIGLHQrDNRRLIDTLTR--LRDLGNTLIV 554
Cdd:COG4619  113 LLERLGLPPDILDKPVERLSGGERQRLALI----RALLlqpDVL-LLDEPTSALDP-ENTRRVEELLReyLAEEGRAVLW 186
                         90       100
                 ....*....|....*....|
gi 494899544 555 VEHDEDTI-RAADWIVDIGP 573
Cdd:COG4619  187 VSHDPEQIeRVADRVLTLEA 206
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
840-934 3.60e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 49.60  E-value: 3.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 840 LSGGEAQRVKLAAELQKRSAgrtIYILDEPTTGLHFEDIKKLLGVINGLVDKGN-TVIVIEHNLDVIKTADWVIDMgpeg 918
Cdd:PRK13632 143 LSGGQKQRVAIASVLALNPE---IIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAILADKVIVF---- 215
                         90
                 ....*....|....*.
gi 494899544 919 gtGGGTVIAEGTPEDI 934
Cdd:PRK13632 216 --SEGKLIAQGKPKEI 229
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
832-914 3.80e-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: 48.87  E-value: 3.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 832 RLGQPAPTLSGGEAQRVKLAAELQKRSagrTIYILDEPTTGL--HFEDIKKLLGVINGLVDKGNTVIVIEHNLDVIKTAD 909
Cdd:cd03290  133 EIGERGINLSGGQRQRICVARALYQNT---NIVFLDDPFSALdiHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPHAD 209

                 ....*
gi 494899544 910 WVIDM 914
Cdd:cd03290  210 WIIAM 214
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
818-914 4.06e-06

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 48.89  E-value: 4.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 818 RYLKTLVDVGLGYvRLGQPAPTLSGGEAQRVKLAAELQKRSAgrtIYILDEPTTGLHFEDIKKLLGVINGLVDK-GNTVI 896
Cdd:COG1136  124 RARELLERVGLGD-RLDHRPSQLSGGQQQRVAIARALVNRPK---LILADEPTGNLDSKTGEEVLELLRELNRElGTTIV 199
                         90
                 ....*....|....*...
gi 494899544 897 VIEHNLDVIKTADWVIDM 914
Cdd:COG1136  200 MVTHDPELAARADRVIRL 217
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
472-615 4.10e-06

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: 50.67  E-value: 4.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 472 KEVQARITFLLD-VGLDYLSLARAAGSLSGGEAQRIRLAtqigSGLAG---VLyVLDEPSIGLHQRDNRRLIDTLTRLRD 547
Cdd:COG1123  378 AERRERVAELLErVGLPPDLADRYPHELSGGQRQRVAIA----RALALepkLL-ILDEPTSALDVSVQAQILNLLRDLQR 452
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494899544 548 -LGNTLIVVEHDEDTIRA-ADWIVDIgprageHGGHVVHSGNYRDLLKNRKS-LTGAYLSgreslPVPAIR 615
Cdd:COG1123  453 eLGLTYLFISHDLAVVRYiADRVAVM------YDGRIVEDGPTEEVFANPQHpYTRALLA-----AVPSLD 512
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
820-934 4.32e-06

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: 49.04  E-value: 4.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 820 LKTLVDVGLGYVRLGQPApTLSGGEAQRVKLAaelqkrsagRTI-----YIL-DEPTTGLhfeDiKKLLGVINGLV---- 889
Cdd:cd03261  118 LEKLEAVGLRGAEDLYPA-ELSGGMKKRVALA---------RALaldpeLLLyDEPTAGL---D-PIASGVIDDLIrslk 183
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 494899544 890 -DKGNTVIVIEHNLD-VIKTADWVIDMGPeggtggGTVIAEGTPEDI 934
Cdd:cd03261  184 kELGLTSIMVTHDLDtAFAIADRIAVLYD------GKIVAEGTPEEL 224
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
835-934 4.32e-06

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 49.62  E-value: 4.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 835 QPAPTLSGGEAQRVKLAAELQKRSagrTIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNLDVI---KTADWV 911
Cdd:PRK13638 132 QPIQCLSHGQKKRVAIAGALVLQA---RYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIyeiSDAVYV 208
                         90       100
                 ....*....|....*....|...
gi 494899544 912 IDMGpeggtgggTVIAEGTPEDI 934
Cdd:PRK13638 209 LRQG--------QILTHGAPGEV 223
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
790-903 4.72e-06

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: 48.43  E-value: 4.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 790 YKGKTISEVL-------DMPIEEAAdffepvTSIHRYLKTLVDVGLGYVRLGQpaptLSGGEAQRVKLAAELQKRSAgrt 862
Cdd:cd03269   82 YPKMKVIDQLvylaqlkGLKKEEAR------RRIDEWLERLELSEYANKRVEE----LSKGNQQKVQFIAAVIHDPE--- 148
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 494899544 863 IYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNLD 903
Cdd:cd03269  149 LLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQME 189
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
484-598 5.16e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 49.31  E-value: 5.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 484 VGLDYLSLARAAGSLSGGEAQRIrlatqigsGLAGVL------YVLDEPSIGLHQRDNRRLIDTLTRLRDLGNTLIVVEH 557
Cdd:PRK13651 152 VGLDESYLQRSPFELSGGQKRRV--------ALAGILamepdfLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 494899544 558 DEDTI--RAADWIVdigpragEHGGHVVHSGNYRDLLKNRKSL 598
Cdd:PRK13651 224 DLDNVleWTKRTIF-------FKDGKIIKDGDTYDILSDNKFL 259
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
497-560 6.02e-06

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


Pssm-ID: 213193 [Multi-domain]  Cd Length: 205  Bit Score: 48.02  E-value: 6.02e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494899544 497 SLSGGEAQRIRLATQIGSGLAgvLYVLDEPSIGLHQRDNRRLIDTLTRLRDLGNTLIVVEHDED 560
Cdd:cd03226  126 SLSGGQKQRLAIAAALLSGKD--LLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYE 187
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
466-571 6.80e-06

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: 48.25  E-value: 6.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 466 IAGPVLKEVQARITFLLD-VGLDYLsLARAAGSLSGGEAQRIRLAtqigSGLAG----VLyvLDEPSIGLHQRDNRRLID 540
Cdd:cd03255  109 LAGVPKKERRERAEELLErVGLGDR-LNHYPSELSGGQQQRVAIA----RALANdpkiIL--ADEPTGNLDSETGKEVME 181
                         90       100       110
                 ....*....|....*....|....*....|..
gi 494899544 541 TLTRL-RDLGNTLIVVEHDEDTIRAADWIVDI 571
Cdd:cd03255  182 LLRELnKEAGTTIVVVTHDPELAEYADRIIEL 213
cbiO PRK13650
energy-coupling factor transporter ATPase;
826-914 9.13e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 48.57  E-value: 9.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 826 VGLGYVRLGQPApTLSGGEAQRVKLAAELQKRSAgrtIYILDEPTTGLHFEDIKKLLGVINGLVDKGN-TVIVIEHNLDV 904
Cdd:PRK13650 128 VGMQDFKEREPA-RLSGGQKQRVAIAGAVAMRPK---IIILDEATSMLDPEGRLELIKTIKGIRDDYQmTVISITHDLDE 203
                         90
                 ....*....|
gi 494899544 905 IKTADWVIDM 914
Cdd:PRK13650 204 VALSDRVLVM 213
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
787-906 9.48e-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: 47.52  E-value: 9.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 787 EVHYKGKTIsevLDMPIEEAAD------FFEPVT----SIHRYLKTlVDVGLgyvrlgqpaptlSGGEAQRVKLaaeLQK 856
Cdd:cd03217   58 EILFKGEDI---TDLPPEERARlgiflaFQYPPEipgvKNADFLRY-VNEGF------------SGGEKKRNEI---LQL 118
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 494899544 857 RSAGRTIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHN---LDVIK 906
Cdd:cd03217  119 LLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYqrlLDYIK 171
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
839-933 9.99e-06

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 49.39  E-value: 9.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 839 TLSGGEAQRVKLA-AELQKRSagrtIYILDEPTTGLHFEDIKKLLGVINGLVdKGNTVIVIEHNLDVIKTADW--VIDMG 915
Cdd:COG1132  476 NLSGGQRQRIAIArALLKDPP----ILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLSTIRNADRilVLDDG 550
                         90
                 ....*....|....*...
gi 494899544 916 peggtgggTVIAEGTPED 933
Cdd:COG1132  551 --------RIVEQGTHEE 560
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
829-911 1.11e-05

ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 443660 [Multi-domain]  Cd Length: 563  Bit Score: 49.36  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 829 GY-VRLGQPAPTLSGGEAQRVKLAaelqkrsagRTIY------ILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHN 901
Cdd:COG4618  456 GYdTRIGEGGARLSGGQRQRIGLA---------RALYgdprlvVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHR 526
                         90
                 ....*....|
gi 494899544 902 LDVIKTADWV 911
Cdd:COG4618  527 PSLLAAVDKL 536
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
473-577 1.13e-05

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 47.79  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 473 EVQARITFLLDVGLDYLSLARAAGSLSGGEAQRIRLATQIgSGLAGVLyVLDEPSIGLHQRDNRRLIDTLTRL-RDLGNT 551
Cdd:PRK10247 113 DPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNL-QFMPKVL-LLDEITSALDESNKHNVNEIIHRYvREQNIA 190
                         90       100
                 ....*....|....*....|....*.
gi 494899544 552 LIVVEHDEDTIRAADWIVDIGPRAGE 577
Cdd:PRK10247 191 VLWVTHDKDEINHADKVITLQPHAGE 216
cbiO PRK13645
energy-coupling factor transporter ATPase;
802-934 1.15e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 48.47  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 802 PIEEAADFFEPVTSIHRYLKtLVDVGLGYVRlgQPAPTLSGGEAQRVKLAAELQKRsaGRTIyILDEPTTGLH---FEDI 878
Cdd:PRK13645 116 PVNLGENKQEAYKKVPELLK-LVQLPEDYVK--RSPFELSGGQKRRVALAGIIAMD--GNTL-VLDEPTGGLDpkgEEDF 189
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 494899544 879 KKLLGVINGlvDKGNTVIVIEHNLD-VIKTADWVIDMgpeggtGGGTVIAEGTPEDI 934
Cdd:PRK13645 190 INLFERLNK--EYKKRIIMVTHNMDqVLRIADEVIVM------HEGKVISIGSPFEI 238
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
835-958 1.19e-05

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 48.68  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 835 QPAPTLSGGEAQRVKLAAELQKRSAgrtIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNLDV-IKTADWVId 913
Cdd:PRK09536 135 RPVTSLSGGERQRVLLARALAQATP---VLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLaARYCDELV- 210
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 494899544 914 mgpeggtgggtVIAEGTPEDIAEVPESHTGGFLADILDIEESVAT 958
Cdd:PRK09536 211 -----------LLADGRVRAAGPPADVLTADTLRAAFDARTAVGT 244
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
498-559 1.33e-05

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 47.47  E-value: 1.33e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494899544 498 LSGGEAQRIRLATQIgSGLAGVLYVlDEPSIGLHQRDNRRLIDTLTRL-RDLGNTLIVVEHDE 559
Cdd:PRK10584 147 LSGGEQQRVALARAF-NGRPDVLFA-DEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDL 207
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
823-914 1.36e-05

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 48.95  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 823 LVDVGLGYvRLGQPAPTLSGGEAQRVKLAAELQKrsaGRTIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNL 902
Cdd:PRK10535 129 LQRLGLED-RVEYQPSQLSGGQQQRVSIARALMN---GGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDP 204
                         90
                 ....*....|..
gi 494899544 903 DVIKTADWVIDM 914
Cdd:PRK10535 205 QVAAQAERVIEI 216
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
818-916 1.40e-05

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 47.40  E-value: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 818 RYLKTLVDVGLGYVRLGQPAPTLSGGEAQRVKLAAELQKRSagrTIYILDEPTTGLHFEDIKKLLGVINGLV-DKGNTVI 896
Cdd:PRK10247 116 IFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMP---KVLLLDEITSALDESNKHNVNEIIHRYVrEQNIAVL 192
                         90       100
                 ....*....|....*....|
gi 494899544 897 VIEHNLDVIKTADWVIDMGP 916
Cdd:PRK10247 193 WVTHDKDEINHADKVITLQP 212
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
472-594 1.46e-05

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: 47.68  E-value: 1.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 472 KEVQARITFLL-DVGLDYLSLA-RAAGSLSGGEAQRIRLAtqigSGLAG--VLYVLDEPSIGLHQRDNRRLIDTLTRL-R 546
Cdd:cd03295  108 EKIRERADELLaLVGLDPAEFAdRYPHELSGGQQQRVGVA----RALAAdpPLLLMDEPFGALDPITRDQLQEEFKRLqQ 183
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 494899544 547 DLGNTLIVVEHD-EDTIRAADWIVDIgprageHGGHVVHSGNYRDLLKN 594
Cdd:cd03295  184 ELGKTIVFVTHDiDEAFRLADRIAIM------KNGEIVQVGTPDEILRS 226
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
496-568 1.49e-05

ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 443660 [Multi-domain]  Cd Length: 563  Bit Score: 48.59  E-value: 1.49e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494899544 496 GSLSGGEAQRIrlatqigsGLAGVLY------VLDEPSIGLHQRDNRRLIDTLTRLRDLGNTLIVVEHDEDTIRAADWI 568
Cdd:COG4618  466 ARLSGGQRQRI--------GLARALYgdprlvVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAVDKL 536
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
784-905 1.52e-05

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 48.63  E-value: 1.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 784 ETLEVHYKGKTISEVLDMPIEE-----AADFFEpvTSihrYLKTLVDVGLGYVRL-GQPAPTLSGGEAQRVKLAAELQkR 857
Cdd:COG1245  399 EDLKISYKPQYISPDYDGTVEEflrsaNTDDFG--SS---YYKTEIIKPLGLEKLlDKNVKDLSGGELQRVAIAACLS-R 472
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 494899544 858 SAgrTIYILDEPTTGLHFEDIKKLLGVINGLVD-KGNTVIVIEHNLDVI 905
Cdd:COG1245  473 DA--DLYLLDEPSAHLDVEQRLAVAKAIRRFAEnRGKTAMVVDHDIYLI 519
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
833-914 1.63e-05

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: 47.48  E-value: 1.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 833 LGQPAPTLSGGEAQRVKLAAELQKRSagrTIYILDEPTTGLHFEDIKKLLGVINGLVDkGNTVIVIEHNLDVIKTADWVI 912
Cdd:cd03252  132 VGEQGAGLSGGQRQRIAIARALIHNP---RILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKNADRII 207

                 ..
gi 494899544 913 DM 914
Cdd:cd03252  208 VM 209
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
798-914 1.63e-05

ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.


Pssm-ID: 213229 [Multi-domain]  Cd Length: 213  Bit Score: 47.14  E-value: 1.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 798 VLDMPIEEAadffepvtsIHRYLKTLVDVGLGYVRLGQPApTLSGGEAQRVKLAAELqkrsAGRTIYIL-DEPTTGLHFE 876
Cdd:cd03262  104 VKGMSKAEA---------EERALELLEKVGLADKADAYPA-QLSGGQQQRVAIARAL----AMNPKVMLfDEPTSALDPE 169
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 494899544 877 DIKKLLGVINGLVDKGNTVIVIEHNLDVI-KTADWVIDM 914
Cdd:cd03262  170 LVGEVLDVMKDLAEEGMTMVVVTHEMGFArEVADRVIFM 208
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
826-956 1.70e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 47.71  E-value: 1.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 826 VGLGYVRLGQPAPTLSGGEAQRVKLAAELQKRSagrTIYILDEPTTGLHFEDIKKLLGVINGLVDKGN-TVIVIEHNL-D 903
Cdd:PRK13634 132 VGLPEELLARSPFELSGGQMRRVAIAGVLAMEP---EVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGlTTVLVTHSMeD 208
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 494899544 904 VIKTADWVIDMgpeggtGGGTVIAEGTPEDIAEVPEShtggfLADI-LDIEESV 956
Cdd:PRK13634 209 AARYADQIVVM------HKGTVFLQGTPREIFADPDE-----LEAIgLDLPETV 251
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
840-956 2.08e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 47.39  E-value: 2.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 840 LSGGEAQRVKLAAELQKRSagrTIYILDEPTTGLHFEDIKKLLGVINGLVDK-GNTVIVIEHNLDVIKTADWVIDMgpeg 918
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRP---ECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVEADRIIVM---- 217
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 494899544 919 gtGGGTVIAEGTPEDI-AEVPESHTGGF-------LA------------DILDIEESV 956
Cdd:PRK13633 218 --DSGKVVMEGTPKEIfKEVEMMKKIGLdvpqvteLAyelkkegvdipsDILTIDEMV 273
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
803-915 2.09e-05

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 48.48  E-value: 2.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 803 IEEAA------DFFEPVtsihrylktlvDVGLGYVrLGQPAPTLSGGEAQRVKLAAELQKRSAgrtIYILDEPTTGLHFE 876
Cdd:PRK11176 450 IEEAArmayamDFINKM-----------DNGLDTV-IGENGVLLSGGQRQRIAIARALLRDSP---ILILDEATSALDTE 514
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 494899544 877 DIKKLLGVINGLvDKGNTVIVIEHNLDVIKTAD--WVIDMG 915
Cdd:PRK11176 515 SERAIQAALDEL-QKNRTSLVIAHRLSTIEKADeiLVVEDG 554
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
840-914 2.10e-05

ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.


Pssm-ID: 213214 [Multi-domain]  Cd Length: 178  Bit Score: 46.15  E-value: 2.10e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494899544 840 LSGGEAQRVKLAAELQKRSAgrtIYILDEPTTGLHFEDIKKLLGVINGlVDKGNTVIVIEHNLDVIKTADWVIDM 914
Cdd:cd03247   99 FSGGERQRLALARILLQDAP---IVLLDEPTVGLDPITERQLLSLIFE-VLKDKTLIWITHHLTGIEHMDKILFL 169
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
493-558 2.17e-05

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 47.18  E-value: 2.17e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494899544 493 RAAGSLSGGEAQRIRLATQIGSglAGVLYVLDEPSIGLHQRDNRRLIDTLTRLRDLGNTLIVVEHD 558
Cdd:PRK15056 138 RQIGELSGGQKKRVFLARAIAQ--QGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHN 201
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
817-906 2.25e-05

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 48.00  E-value: 2.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 817 HRYLKTLVDVGLGyVRLGQPAPTLSGGEAQRVKLAAELQKRSagrTIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVI 896
Cdd:PRK13549 122 LRAQKLLAQLKLD-INPATPVGNLGLGQQQLVEIAKALNKQA---RLLILDEPTASLTESETAVLLDIIRDLKAHGIACI 197
                         90
                 ....*....|
gi 494899544 897 VIEHNLDVIK 906
Cdd:PRK13549 198 YISHKLNEVK 207
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
492-605 2.25e-05

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 46.80  E-value: 2.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 492 ARAAGSLSGGEAQRIrlatQIGSGLAGV--LYVLDEPSIGLHQRDNRRLIDTLTRLRDLGNTLIVVEHDED-TIRAAD-- 566
Cdd:PRK11614 132 IQRAGTMSGGEQQML----AIGRALMSQprLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANqALKLADrg 207
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 494899544 567 WIVDigpragehGGHVVHSGNYRDLLKNrKSLTGAYLSG 605
Cdd:PRK11614 208 YVLE--------NGHVVLEDTGDALLAN-EAVRSAYLGG 237
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
832-916 2.41e-05

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


Pssm-ID: 443809 [Multi-domain]  Cd Length: 229  Bit Score: 46.66  E-value: 2.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 832 RLGQPAP-TLSGGEAQRVKLAAELQKRsagRTIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNLDVIKT-AD 909
Cdd:COG4778  144 RLWDLPPaTFSGGEQQRVNIARGFIAD---PPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAvAD 220

                 ....*..
gi 494899544 910 WVIDMGP 916
Cdd:COG4778  221 RVVDVTP 227
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
833-938 2.61e-05

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 46.85  E-value: 2.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 833 LGQPAPTLSGGEAQRVKLAAE-LQKRSAGR---TIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNLD-VIKT 907
Cdd:PRK03695 120 LGRSVNQLSGGEWQRVRLAAVvLQVWPDINpagQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNhTLRH 199
                         90       100       110
                 ....*....|....*....|....*....|...
gi 494899544 908 AD--WVIDMGpeggtgggTVIAEGTPEDIAEVP 938
Cdd:PRK03695 200 ADrvWLLKQG--------KLLASGRRDEVLTPE 224
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
493-586 2.66e-05

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 46.93  E-value: 2.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 493 RAAGSLSGGEAQRIRLATQIGSGLAGVLyvLDEPSIGL---HQRDnrrLIDTLTRLRDLGNTLIVVEHD-EDTIRAADWI 568
Cdd:PRK11231 134 RRLTDLSGGQRQRAFLAMVLAQDTPVVL--LDEPTTYLdinHQVE---LMRLMRELNTQGKTVVTVLHDlNQASRYCDHL 208
                         90
                 ....*....|....*...
gi 494899544 569 VDIgprageHGGHVVHSG 586
Cdd:PRK11231 209 VVL------ANGHVMAQG 220
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
803-915 2.85e-05

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.


Pssm-ID: 213198 [Multi-domain]  Cd Length: 201  Bit Score: 45.95  E-value: 2.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 803 IEEAADFFEPVTSIHRYLKTLVDVGLGYVRlGQPAPTLSGGEAQRVKLAAELqkrSAGRTIYILDEPTTGLHFEDIKKLL 882
Cdd:cd03231   90 VLENLRFWHADHSDEQVEEALARVGLNGFE-DRPVAQLSAGQQRRVALARLL---LSGRPLWILDEPTTALDKAGVARFA 165
                         90       100       110
                 ....*....|....*....|....*....|....
gi 494899544 883 GVINGLVDKGNTVIVIEH-NLDVIKTADWVIDMG 915
Cdd:cd03231  166 EAMAGHCARGGMVVLTTHqDLGLSEAGARELDLG 199
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
840-913 2.93e-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: 45.64  E-value: 2.93e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494899544 840 LSGGEAQRVKLAAELQKRSagrTIYILDEPTTGLHFEDIKKLLGVINGLVDKGN-TVIVIEHNLDVIktaDWVID 913
Cdd:cd03222   72 LSGGELQRVAIAAALLRNA---TFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVL---DYLSD 140
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
833-934 3.06e-05

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 46.43  E-value: 3.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 833 LGQpapTLSGGEAQRVKLAAELqkrSAGRTIYILDEPTTG---LHFEDIKKllgVINGLVDKGNTVIVIEHN----LDVI 905
Cdd:PRK10895 134 MGQ---SLSGGERRRVEIARAL---AANPKFILLDEPFAGvdpISVIDIKR---IIEHLRDSGLGVLITDHNvretLAVC 204
                         90       100
                 ....*....|....*....|....*....
gi 494899544 906 KTAdWVIDMGpeggtgggTVIAEGTPEDI 934
Cdd:PRK10895 205 ERA-YIVSQG--------HLIAHGTPTEI 224
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
472-560 3.80e-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: 45.86  E-value: 3.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 472 KEVQARITFLLD-VGLDYLSLARAAGsLSGGEAQRIRLATQIGSglAGVLYVLDEPSIGLHQRDNRRLIDTLTRLRDLGN 550
Cdd:cd03292  111 REIRKRVPAALElVGLSHKHRALPAE-LSGGEQQRVAIARAIVN--SPTILIADEPTGNLDPDTTWEIMNLLKKINKAGT 187
                         90
                 ....*....|
gi 494899544 551 TLIVVEHDED 560
Cdd:cd03292  188 TVVVATHAKE 197
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
490-593 3.95e-05

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: 47.43  E-value: 3.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  490 SLARAAGSLSGGEAQRIRLATQIGSGlAGVLyVLDEPSIGLHQRDNRRLIDTLTRLRDlgNTLIVVEHDEDTIRAADWIV 569
Cdd:TIGR01193 604 ELSEEGSSISGGQKQRIALARALLTD-SKVL-ILDESTSNLDTITEKKIVNNLLNLQD--KTIIFVAHRLSVAKQSDKII 679
                          90       100
                  ....*....|....*....|....
gi 494899544  570 digprAGEHGGhVVHSGNYRDLLK 593
Cdd:TIGR01193 680 -----VLDHGK-IIEQGSHDELLD 697
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
492-569 4.12e-05

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: 44.73  E-value: 4.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 492 ARAAG-----SLSGGEAQRIRLATQIGSGlAGVLyVLDEPSIGLHQRDNRRLIDTLTRLRDLGNTLIVVEHDEDTIRA-A 565
Cdd:cd03216   72 ARRAGiamvyQLSVGERQMVEIARALARN-ARLL-ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiA 149

                 ....
gi 494899544 566 DWIV 569
Cdd:cd03216  150 DRVT 153
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
453-566 4.15e-05

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 46.08  E-value: 4.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 453 YLSGLQLDSRQKAIAGPVLKEVQARitflldVGLDYLsLARAAGSLSGGEAQRIRLAT---QIGSGL--AGVLYVLDEPS 527
Cdd:PRK03695  89 YLTLHQPDKTRTEAVASALNEVAEA------LGLDDK-LGRSVNQLSGGEWQRVRLAAvvlQVWPDInpAGQLLLLDEPM 161
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 494899544 528 IGL---HQRDNRRLIDTLTRlrdLGNTLIVVEHD-EDTIRAAD 566
Cdd:PRK03695 162 NSLdvaQQAALDRLLSELCQ---QGIAVVMSSHDlNHTLRHAD 201
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
783-914 4.65e-05

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: 45.96  E-value: 4.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 783 RETLEVHYKGKTISEvldmpIEEAAdffepvtsihryLKTLVDVGLGYVRLGQPAPTLSGGEAQRVKLAAELqkrSAGRT 862
Cdd:cd03257  106 AEPLRIHGKLSKKEA-----RKEAV------------LLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARAL---ALNPK 165
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 494899544 863 IYILDEPTTGLhfeDIKKLLGVINGLVD----KGNTVIVIEHNLDVIK-TADWVIDM 914
Cdd:cd03257  166 LLIADEPTSAL---DVSVQAQILDLLKKlqeeLGLTLLFITHDLGVVAkIADRVAVM 219
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
839-911 5.49e-05

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 46.94  E-value: 5.49e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494899544 839 TLSGGEAQRVklaaELQK---RSAgrTIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNLDVIKT-ADWV 911
Cdd:COG3845  141 DLSVGEQQRV----EILKalyRGA--RILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAiADRV 211
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
482-591 5.57e-05

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 46.76  E-value: 5.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 482 LDVGLDYLSLARAAGsLSGGEAQRIRLATQIGSglAGVLYVLDEPSIGLHQRDNRRLIDTLTRLRdLGNTLIVVEHDEDT 561
Cdd:PRK11174 471 LPQGLDTPIGDQAAG-LSVGQAQRLALARALLQ--PCQLLLLDEPTASLDAHSEQLVMQALNAAS-RRQTTLMVTHQLED 546
                         90       100       110
                 ....*....|....*....|....*....|..
gi 494899544 562 IRAAD--WIVDigpragehGGHVVHSGNYRDL 591
Cdd:PRK11174 547 LAQWDqiWVMQ--------DGQIVQQGDYAEL 570
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
827-950 5.91e-05

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 46.76  E-value: 5.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 827 GLGYVrLGQPAPTLSGGEAQRVKLA-AELQKRSagrtIYILDEPTTGLhfeDIKKLLGVINGLVD--KGNTVIVIEHNLD 903
Cdd:PRK11174 474 GLDTP-IGDQAAGLSVGQAQRLALArALLQPCQ----LLLLDEPTASL---DAHSEQLVMQALNAasRRQTTLMVTHQLE 545
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 494899544 904 VIKTAD--WVIDMGpeggtgggTVIAEGTPEDIaevpeSHTGGFLADIL 950
Cdd:PRK11174 546 DLAQWDqiWVMQDG--------QIVQQGDYAEL-----SQAGGLFATLL 581
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
818-940 6.88e-05

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 45.73  E-value: 6.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 818 RYLKTLVDVGLGYVRLGQPAPTLSGGEAQRVKLAAELQKRSagrTIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIV 897
Cdd:PRK10619 131 RAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEP---EVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVV 207
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 494899544 898 IEHNLDVIK-TADWVIDMgpeggtGGGTVIAEGTPEDIAEVPES 940
Cdd:PRK10619 208 VTHEMGFARhVSSHVIFL------HQGKIEEEGAPEQLFGNPQS 245
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
834-934 7.98e-05

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 45.36  E-value: 7.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 834 GQPAPTLSGGEAQRVKLAAELQKRSAgrtIYILDEPTTGL---HFEDIKKLLGVINGlvDKGNTVIVIEHNLD-VIKTAD 909
Cdd:PRK10253 138 DQSVDTLSGGQRQRAWIAMVLAQETA---IMLLDEPTTWLdisHQIDLLELLSELNR--EKGYTLAAVLHDLNqACRYAS 212
                         90       100
                 ....*....|....*....|....*
gi 494899544 910 WVIDMgpeggtGGGTVIAEGTPEDI 934
Cdd:PRK10253 213 HLIAL------REGKIVAQGAPKEI 231
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
816-906 9.17e-05

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 45.97  E-value: 9.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  816 IHRYLKTLVDVGLGYVRLGQPAPTLSGGEAQRVKLAAELQKRSagrTIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTV 895
Cdd:TIGR02633 118 YLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQA---RLLILDEPSSSLTEKETEILLDIIRDLKAHGVAC 194
                          90
                  ....*....|.
gi 494899544  896 IVIEHNLDVIK 906
Cdd:TIGR02633 195 VYISHKLNEVK 205
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
484-593 1.14e-04

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 45.16  E-value: 1.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 484 VGLDYLSlARAAGSLSGGEAQRIRLATQIGSGLAGVLyvLDEPSIGL---HQRDNRRLIDTLTRLRDLgnTLIVVEHDED 560
Cdd:PRK10575 135 VGLKPLA-HRLVDSLSGGERQRAWIAMLVAQDSRCLL--LDEPTSALdiaHQVDVLALVHRLSQERGL--TVIAVLHDIN 209
                         90       100       110
                 ....*....|....*....|....*....|....
gi 494899544 561 -TIRAADWIVDIgprageHGGHVVHSGNYRDLLK 593
Cdd:PRK10575 210 mAARYCDYLVAL------RGGEMIAQGTPAELMR 237
cbiO PRK13649
energy-coupling factor transporter ATPase;
840-934 1.14e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 45.12  E-value: 1.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 840 LSGGEAQRVKLAAELQKRSagrTIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNL-DVIKTADWVIDMgpeg 918
Cdd:PRK13649 146 LSGGQMRRVAIAGILAMEP---KILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMdDVANYADFVYVL---- 218
                         90
                 ....*....|....*.
gi 494899544 919 gtGGGTVIAEGTPEDI 934
Cdd:PRK13649 219 --EKGKLVLSGKPKDI 232
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
840-900 1.17e-04

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


Pssm-ID: 213180 [Multi-domain]  Cd Length: 194  Bit Score: 44.08  E-value: 1.17e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494899544 840 LSGGEAQRVKLAAELQKRSagrTIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEH 900
Cdd:cd03213  112 LSGGERKRVSIALELVSNP---SLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIH 169
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
817-898 1.23e-04

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


Pssm-ID: 213231 [Multi-domain]  Cd Length: 211  Bit Score: 44.11  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 817 HRYLKTLVDVGLGYVRlGQPAPTLSGGEAQRVKLAAELQKRSAgrtIYILDEPTTGLhfeDIKKLLGVINGLVDKGNTVI 896
Cdd:cd03264  109 ARVDEVLELVNLGDRA-KKKIGSLSGGMRRRVGIAQALVGDPS---ILIVDEPTAGL---DPEERIRFRNLLSELGEDRI 181

                 ..
gi 494899544 897 VI 898
Cdd:cd03264  182 VI 183
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
840-914 1.50e-04

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


Pssm-ID: 213196 [Multi-domain]  Cd Length: 178  Bit Score: 43.71  E-value: 1.50e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494899544 840 LSGGEAQRVKLAAELQKRSagrTIYILDEPTTGLHFEDIKKLLGVINGLVDK-GNTVIVIEHNLDVIKT-ADWVIDM 914
Cdd:cd03229  101 LSGGQQQRVALARALAMDP---DVLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARlADRVVVL 174
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
840-907 1.54e-04

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


Pssm-ID: 213259 [Multi-domain]  Cd Length: 214  Bit Score: 43.94  E-value: 1.54e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494899544 840 LSGGEAQRVKLAAELQKRSagrTIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNLDVIKT 907
Cdd:cd03292  137 LSGGEQQRVAIARAIVNSP---TILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDT 201
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
823-905 1.58e-04

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: 44.31  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 823 LVDVGLGYVRlGQPAPTLSGGEAQRVKLAAELQKRSAgrtIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIV-IEHN 901
Cdd:COG1119  127 LELLGLAHLA-DRPFGTLSQGEQRRVLIARALVKDPE---LLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVlVTHH 202

                 ....
gi 494899544 902 LDVI 905
Cdd:COG1119  203 VEEI 206
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
790-937 1.66e-04

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 45.18  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  790 YKGKTISEVLDMPIEEAAdfFEPVTSIHRYLKTLVDVGLGYvRLGQPAPTLSGGEAQRVKLAAELQKRSagrTIYILDEP 869
Cdd:TIGR03269 122 YGDDTVLDNVLEALEEIG--YEGKEAVGRAVDLIEMVQLSH-RITHIARDLSGGEKQRVVLARQLAKEP---FLFLADEP 195
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494899544  870 TTGLHFEDIKKLL-GVINGLVDKGNTVIVIEHNLDVI-KTADWVI--DMGpeggtgggTVIAEGTPEDIAEV 937
Cdd:TIGR03269 196 TGTLDPQTAKLVHnALEEAVKASGISMVLTSHWPEVIeDLSDKAIwlENG--------EIKEEGTPDEVVAV 259
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
495-602 1.71e-04

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: 44.07  E-value: 1.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 495 AGSLSGGEAQRIRLATqigsglAGV----LYVLDEPSIGLHQRDNRRLIDTLTRLRdLGNTLIVVEHDEDTIRAADWIVD 570
Cdd:cd03249  137 GSQLSGGQKQRIAIAR------ALLrnpkILLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRLSTIRNADLIAV 209
                         90       100       110
                 ....*....|....*....|....*....|..
gi 494899544 571 IgprageHGGHVVHSGNYRDLLKNRksltGAY 602
Cdd:cd03249  210 L------QNGQVVEQGTHDELMAQK----GVY 231
cbiO PRK13641
energy-coupling factor transporter ATPase;
820-939 1.73e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 44.43  E-value: 1.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 820 LKTLVDVGLGYVRLGQPAPTLSGGEAQRVKLAAELQKRSagrTIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIE 899
Cdd:PRK13641 126 LKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEP---EILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVT 202
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 494899544 900 HNL-DVIKTADWVIDMgpeggtGGGTVIAEGTPEDIAEVPE 939
Cdd:PRK13641 203 HNMdDVAEYADDVLVL------EHGKLIKHASPKEIFSDKE 237
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
829-914 1.77e-04

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: 44.14  E-value: 1.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 829 GY-VRLGQPAPTLSGGEAQRVKLAAELQKRSAgrtIYILDEPTTGLHFEDIKKLLGVINGLVdKGNTVIVIEHNLDVIKT 907
Cdd:cd03251  127 GYdTVIGERGVKLSGGQRQRIAIARALLKDPP---ILILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLSTIEN 202

                 ....*..
gi 494899544 908 ADWVIDM 914
Cdd:cd03251  203 ADRIVVL 209
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
839-953 1.92e-04

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: 43.86  E-value: 1.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 839 TLSGGEAQRVKLAAELQKRSagrTIYILDEPTTGLHFEDIKKLLGVINGLVDK-GNTVIVIEHNLDVIKT-ADWVIDMgp 916
Cdd:cd03299  129 TLSGGEQQRVAIARALVVNP---KILLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWAlADKVAIM-- 203
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 494899544 917 eggtGGGTVIAEGTPEDIAEVPEShtgGFLADILDIE 953
Cdd:cd03299  204 ----LNGKLIQVGKPEEVFKKPKN---EFVAEFLGFN 233
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
826-912 2.03e-04

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 43.98  E-value: 2.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 826 VGLGYvrLGQPAP-TLSGGEAQRVKLA-AELQKRSagrtIYILDEPTT----GLHFEdikkLLGVINGLVDK-GNTVIVI 898
Cdd:COG3840  117 VGLAG--LLDRLPgQLSGGQRQRVALArCLVRKRP----ILLLDEPFSaldpALRQE----MLDLVDELCRErGLTVLMV 186
                         90
                 ....*....|....*
gi 494899544 899 EHNL-DVIKTADWVI 912
Cdd:COG3840  187 THDPeDAARIADRVL 201
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
823-911 2.11e-04

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 45.01  E-value: 2.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 823 LVDVGLGyVRLGQPAPTLSGGEAQRVKLAAELQKRSagrTIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNL 902
Cdd:COG1129  125 LARLGLD-IDPDTPVGDLSVAQQQLVEIARALSRDA---RVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRL 200
                         90
                 ....*....|
gi 494899544 903 D-VIKTADWV 911
Cdd:COG1129  201 DeVFEIADRV 210
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
822-916 2.32e-04

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 43.32  E-value: 2.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 822 TLVDVGLGYVrLGQPAPTLSGGEAQRVKLAAELqkrSAGRTIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHN 901
Cdd:PRK13539 111 ALEAVGLAPL-AHLPFGYLSAGQKRRVALARLL---VSNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATHI 186
                         90
                 ....*....|....*
gi 494899544 902 LDVIKTADwVIDMGP 916
Cdd:PRK13539 187 PLGLPGAR-ELDLGP 200
cbiO PRK13641
energy-coupling factor transporter ATPase;
478-604 2.46e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 44.05  E-value: 2.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 478 ITFLLDVGLDYLSLARAAGSLSGGEAQRIrlatqigsGLAGVL------YVLDEPSIGLHQRDNRRLIDTLTRLRDLGNT 551
Cdd:PRK13641 126 LKWLKKVGLSEDLISKSPFELSGGQMRRV--------AIAGVMayepeiLCLDEPAAGLDPEGRKEMMQLFKDYQKAGHT 197
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 494899544 552 LIVVEHDEDTIraADWIVDIgpRAGEHgGHVVHSGNYRDLLKNRKSLTGAYLS 604
Cdd:PRK13641 198 VILVTHNMDDV--AEYADDV--LVLEH-GKLIKHASPKEIFSDKEWLKKHYLD 245
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
840-898 3.00e-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: 42.80  E-value: 3.00e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 494899544 840 LSGGEAQRVKLAAELqkrSAGRTIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVI 898
Cdd:cd03215  105 LSGGNQQKVVLARWL---ARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLI 160
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
816-912 3.10e-04

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: 42.97  E-value: 3.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 816 IHRYLKTLVDVGLGYVRLG----QPAPTLSGGEAQRVKLAAELqkrsAGR-TIYILDEPTTGLHFEDIKKLLGVINGLVD 890
Cdd:cd03268   99 LLGIRKKRIDEVLDVVGLKdsakKKVKGFSLGMKQRLGIALAL----LGNpDLLILDEPTNGLDPDGIKELRELILSLRD 174
                         90       100
                 ....*....|....*....|....
gi 494899544 891 KGNTVIVIEHNL-DVIKTAD-WVI 912
Cdd:cd03268  175 QGITVLISSHLLsEIQKVADrIGI 198
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
840-912 3.18e-04

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 44.57  E-value: 3.18e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494899544 840 LSGGEAQRVKLAAELQKRSAgrtIYILDEPTTGLHFEDIKKLLGVINGLVdKGNTVIVIEHNLDVIKTADWVI 912
Cdd:PRK13657 472 LSGGERQRLAIARALLKDPP---ILILDEATSALDVETEAKVKAALDELM-KGRTTFIIAHRLSTVRNADRIL 540
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
472-606 3.55e-04

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 43.36  E-value: 3.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 472 KEVQARITFLLDVGLDYLS----LARAAGSLSGGEAQRIRLAtqigSGLAGVLYVL--DEPSIGLHQRDNRRLIDTLTRL 545
Cdd:PRK14247 117 KELQERVRWALEKAQLWDEvkdrLDAPAGKLSGGQQQRLCIA----RALAFQPEVLlaDEPTANLDPENTAKIESLFLEL 192
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494899544 546 RDLGNTLIVVEHDEDTIRAADWIvdigprAGEHGGHVVHSGNYRDLLKN-RKSLTGAYLSGR 606
Cdd:PRK14247 193 KKDMTIVLVTHFPQQAARISDYV------AFLYKGQIVEWGPTREVFTNpRHELTEKYVTGR 248
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
840-949 3.94e-04

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 43.06  E-value: 3.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 840 LSGGEAQRVKLAaelqkRS-AGRTIYIL-DEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNL----DViktADWVID 913
Cdd:COG1126  137 LSGGQQQRVAIA-----RAlAMEPKVMLfDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMgfarEV---ADRVVF 208
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 494899544 914 M--GpeggtgggTVIAEGTPEDIAEVPESH-TGGFLADI 949
Cdd:COG1126  209 MdgG--------RIVEEGPPEEFFENPQHErTRAFLSKV 239
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
840-914 3.95e-04

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 43.08  E-value: 3.95e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494899544 840 LSGGEAQRVKLAAELQKRSagrTIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNLDVI-KTADWVIDM 914
Cdd:COG4161  142 LSGGQQQRVAIARALMMEP---QVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFArKVASQVVYM 214
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
464-577 4.02e-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: 42.94  E-value: 4.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 464 KAIAGPVLKEVQARITFLLD-VGLDYLSLARAaGSLSGGEAQRIrlatqigsGLAGVLY-----VL-DEPSIGLHQRDNR 536
Cdd:cd03256  111 RSLFGLFPKEEKQRALAALErVGLLDKAYQRA-DQLSGGQQQRV--------AIARALMqqpklILaDEPVASLDPASSR 181
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 494899544 537 RLIDTLTRL-RDLGNTLIVVEHDEDTIRA-ADWIvdIGPRAGE 577
Cdd:cd03256  182 QVMDLLKRInREEGITVIVSLHQVDLAREyADRI--VGLKDGR 222
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
840-914 4.56e-04

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 43.08  E-value: 4.56e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494899544 840 LSGGEAQRVKLAAELQKRSAgrtIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNLDVI-KTADWVIDM 914
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQ---VLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVArKTASRVVYM 214
cbiO PRK13643
energy-coupling factor transporter ATPase;
840-934 5.28e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 43.18  E-value: 5.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 840 LSGGEAQRVKLAAELQKRSAgrtIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNL-DVIKTADWVIDMgpeg 918
Cdd:PRK13643 145 LSGGQMRRVAIAGILAMEPE---VLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMdDVADYADYVYLL---- 217
                         90
                 ....*....|....*.
gi 494899544 919 gtGGGTVIAEGTPEDI 934
Cdd:PRK13643 218 --EKGHIISCGTPSDV 231
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
823-905 5.45e-04

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: 42.87  E-value: 5.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 823 LVDVGLGYVRLGQPAPTLSGGEAQRVKLA-AELQKRSagrtIYILDEPTTGLhfeDI---KKLLGVINGL-VDKGNTVIV 897
Cdd:COG1124  122 LEQVGLPPSFLDRYPHQLSGGQRQRVAIArALILEPE----LLLLDEPTSAL---DVsvqAEILNLLKDLrEERGLTYLF 194

                 ....*...
gi 494899544 898 IEHNLDVI 905
Cdd:COG1124  195 VSHDLAVV 202
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
485-602 5.89e-04

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 43.61  E-value: 5.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 485 GLDYLsLARAAGSLSGGEAQRIRLA------TQIgsglagvlYVLDEPSIGLhqrDN---RRLIDTLTRLRDlGNTLIVV 555
Cdd:COG1132  465 GYDTV-VGERGVNLSGGQRQRIAIArallkdPPI--------LILDEATSAL---DTeteALIQEALERLMK-GRTTIVI 531
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 494899544 556 EHDEDTIRAADWIVDIgprageHGGHVVHSGNYRDLLKNRksltGAY 602
Cdd:COG1132  532 AHRLSTIRNADRILVL------DDGRIVEQGTHEELLARG----GLY 568
cbiO PRK13646
energy-coupling factor transporter ATPase;
801-934 7.83e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 42.46  E-value: 7.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 801 MPIEEAADffepvtsihRYLKTLVDVGLGYVRLGQPAPTLSGGEAQRVKLAAELqkrSAGRTIYILDEPTTGLHFEDIKK 880
Cdd:PRK13646 116 MNLDEVKN---------YAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSIL---AMNPDIIVLDEPTAGLDPQSKRQ 183
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 494899544 881 LLGVINGL-VDKGNTVIVIEHNL-DVIKTADWVIDMgpeggtGGGTVIAEGTPEDI 934
Cdd:PRK13646 184 VMRLLKSLqTDENKTIILVSHDMnEVARYADEVIVM------KEGSIVSQTSPKEL 233
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
823-900 7.88e-04

heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]


Pssm-ID: 273491 [Multi-domain]  Cd Length: 198  Bit Score: 41.58  E-value: 7.88e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494899544  823 LVDVGL-GYVRLgqPAPTLSGGEAQRVKLAAELqkrSAGRTIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEH 900
Cdd:TIGR01189 112 LAAVGLtGFEDL--PAAQLSAGQQRRLALARLW---LSRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
AAA_29 pfam13555
P-loop containing region of AAA domain;
632-687 7.92e-04

P-loop containing region of AAA domain;


Pssm-ID: 433304 [Multi-domain]  Cd Length: 61  Bit Score: 38.35  E-value: 7.92e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 494899544  632 HNLRGIDVAFPLGVLTAVTGVSGSGKSTLVnDILATVLanklngarqVPGRHKRIN 687
Cdd:pfam13555  10 GTFDGHTIPIDPRGNTLLTGPSGSGKSTLL-DAIQTLL---------VPAKRARFN 55
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
823-873 8.28e-04

White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.


Pssm-ID: 213201 [Multi-domain]  Cd Length: 226  Bit Score: 41.87  E-value: 8.28e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 494899544 823 LVDVGLGYVRlGQPAPTLSGGEAQRVKLAAELQKRSAgrtIYILDEPTTGL 873
Cdd:cd03234  128 LRDLALTRIG-GNLVKGISGGERRRVSIAVQLLWDPK---VLILDEPTSGL 174
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
826-906 8.35e-04

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 41.96  E-value: 8.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 826 VGLGYvRLGQPAPTLSGGEAQRVKLAaelqkRS-AGR-TIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNLD 903
Cdd:COG2884  125 VGLSD-KAKALPHELSGGEQQRVAIA-----RAlVNRpELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLE 198

                 ...
gi 494899544 904 VIK 906
Cdd:COG2884  199 LVD 201
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
634-677 8.47e-04

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


Pssm-ID: 213180 [Multi-domain]  Cd Length: 194  Bit Score: 41.38  E-value: 8.47e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 494899544 634 LRGIDVAFPLGVLTAVTGVSGSGKSTLVNdilatVLANKLNGAR 677
Cdd:cd03213   25 LKNVSGKAKPGELTAIMGPSGAGKSTLLN-----ALAGRRTGLG 63
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
493-577 8.56e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 8.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 493 RAAGSLSGGEaqRI------RLATQIGsgLAG--VLYVLDEPSIGLHQRDNRRLIDTLTR-LRDLGNtLIVVEHDEDTIR 563
Cdd:PRK03918 784 RPLTFLSGGE--RIalglafRLALSLY--LAGniPLLILDEPTPFLDEERRRKLVDIMERyLRKIPQ-VIIVSHDEELKD 858
                         90
                 ....*....|....
gi 494899544 564 AADWIVDIGPRAGE 577
Cdd:PRK03918 859 AADYVIRVSLEGGV 872
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
836-905 8.85e-04

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


Pssm-ID: 433102 [Multi-domain]  Cd Length: 303  Bit Score: 42.38  E-value: 8.85e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  836 PAPTLSGGEAQRVKLAAELQKRSAGRTIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNLDVI 905
Cdd:pfam13304 233 PAFELSDGTKRLLALLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLLL 302
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
498-569 8.98e-04

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


Pssm-ID: 213196 [Multi-domain]  Cd Length: 178  Bit Score: 41.40  E-value: 8.98e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494899544 498 LSGGEAQRIRLATQIGSGlAGVLyVLDEPSIGLHQRDNRRLIDTLTRLRD-LGNTLIVVEHD-EDTIRAADWIV 569
Cdd:cd03229  101 LSGGQQQRVALARALAMD-PDVL-LLDEPTSALDPITRREVRALLKSLQAqLGITVVLVTHDlDEAARLADRVV 172
PLN03211 PLN03211
ABC transporter G-25; Provisional
840-900 9.75e-04

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 42.94  E-value: 9.75e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494899544 840 LSGGEAQRVKLAAELQkrsAGRTIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEH 900
Cdd:PLN03211 207 ISGGERKRVSIAHEML---INPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
463-569 9.86e-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: 41.94  E-value: 9.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 463 QKAIAGPVLKEVQARITFLLD-VGLDYLSlARAAGSLSGGEAQRIRLAtqigSGLA---GVLyVLDEPSIGLHQRDNRRL 538
Cdd:cd03296  102 KPRSERPPEAEIRAKVHELLKlVQLDWLA-DRYPAQLSGGQRQRVALA----RALAvepKVL-LLDEPFGALDAKVRKEL 175
                         90       100       110
                 ....*....|....*....|....*....|...
gi 494899544 539 IDTLTRLRD-LGNTLIVVEHD-EDTIRAADWIV 569
Cdd:cd03296  176 RRWLRRLHDeLHVTTVFVTHDqEEALEVADRVV 208
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
481-915 1.09e-03

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 42.50  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  481 LLDVGLDYLSLARAAGSLSGGEAQRIRLATQIGSGLAgvLYVLDEPSIGLHQRDNRRLIDTLTRLRDLGNTLIVVEHDED 560
Cdd:TIGR02633 125 LRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQAR--LLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLN 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  561 TIRA-ADWIVDIgpRAGEHGGHVVHSGNYRDLLKNR---KSLTGAYLS-----GRESLPVPAIR--RPINRKRQltvvga 629
Cdd:TIGR02633 203 EVKAvCDTICVI--RDGQHVATKDMSTMSEDDIITMmvgREITSLYPHepheiGDVILEARNLTcwDVINPHRK------ 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  630 rehnlRGIDVAFPL--GVLTAVTGVSGSGKSTLVNDILATVlanklngarqvPGRHkringldqlDKLVRVDQSPIG-RT 706
Cdd:TIGR02633 275 -----RVDDVSFSLrrGEILGVAGLVGAGRTELVQALFGAY-----------PGKF---------EGNVFINGKPVDiRN 329
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  707 PRsnpatytgvfDKIRTLFAATTEAKVRgyqpgrfsfnvkggrceactgEGTIkiemnflPDVYVPCEVcqgarynreTL 786
Cdd:TIGR02633 330 PA----------QAIRAGIAMVPEDRKR---------------------HGIV-------PILGVGKNI---------TL 362
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  787 EVHYKGKTISEvldmpIEEAADffepVTSIHRYLKTLvdvglgYVRLGQP---APTLSGGEAQRVKLAAELQKRSagrTI 863
Cdd:TIGR02633 363 SVLKSFCFKMR-----IDAAAE----LQIIGSAIQRL------KVKTASPflpIGRLSGGNQQKAVLAKMLLTNP---RV 424
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 494899544  864 YILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNL-DVIKTADWVIDMG 915
Cdd:TIGR02633 425 LILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELaEVLGLSDRVLVIG 477
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
823-900 1.09e-03

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 41.62  E-value: 1.09e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494899544 823 LVDVGLGyVRLGQPAPTLSGGEAQRVKLAAELQKRSagrTIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEH 900
Cdd:PRK09493 121 LAKVGLA-ERAHHYPSELSGGQQQRVAIARALAVKP---KLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTH 194
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
472-569 1.11e-03

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: 41.35  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 472 KEVQARITFLLD-VGLDYLsLARAAGSLSGGEAQRIRLATQIGSGLAgvLYVLDEPSIGLHQRDNRRLIDTLTRL-RDLG 549
Cdd:cd03259  105 AEIRARVRELLElVGLEGL-LNRYPHELSGGQQQRVALARALAREPS--LLLLDEPLSALDAKLREELREELKELqRELG 181
                         90       100
                 ....*....|....*....|.
gi 494899544 550 NTLIVVEHD-EDTIRAADWIV 569
Cdd:cd03259  182 ITTIYVTHDqEEALALADRIA 202
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
472-564 1.12e-03

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 41.58  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 472 KEVQARITFLLD-VGLdyLSLARA-AGSLSGGEAQRIRLATQIgsglagV----LYVLDEPSIGLHQRDNRRLIDTLTRL 545
Cdd:COG2884  112 KEIRRRVREVLDlVGL--SDKAKAlPHELSGGEQQRVAIARAL------VnrpeLLLADEPTGNLDPETSWEIMELLEEI 183
                         90
                 ....*....|....*....
gi 494899544 546 RDLGNTLIVVEHDEDTIRA 564
Cdd:COG2884  184 NRRGTTVLIATHDLELVDR 202
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
496-593 1.12e-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: 41.72  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 496 GSLSGGEAQRIRLATQIGsgLAGVLYVLDEPSIGLHQRDNRRLIDTLTRLRD-LGNTLIVVEHDEDTIRA-ADWIVDIgp 573
Cdd:cd03261  135 AELSGGMKKRVALARALA--LDPELLLYDEPTAGLDPIASGVIDDLIRSLKKeLGLTSIMVTHDLDTAFAiADRIAVL-- 210
                         90       100
                 ....*....|....*....|
gi 494899544 574 rageHGGHVVHSGNYRDLLK 593
Cdd:cd03261  211 ----YDGKIVAEGTPEELRA 226
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
460-569 1.20e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 42.14  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 460 DSRQKAIA-GPV---LKEVQAR---ITFLLDVGLDYLSLARAAGSLSGGEAQRIrlatqigsGLAGVL------YVLDEP 526
Cdd:PRK13631 132 DTIEKDIMfGPValgVKKSEAKklaKFYLNKMGLDDSYLERSPFGLSGGQKRRV--------AIAGILaiqpeiLIFDEP 203
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 494899544 527 SIGLHQRDNRRLIDTLTRLRDLGNTLIVVEHD-EDTIRAADWIV 569
Cdd:PRK13631 204 TAGLDPKGEHEMMQLILDAKANNKTVFVITHTmEHVLEVADEVI 247
PLN03140 PLN03140
ABC transporter G family member; Provisional
634-666 1.27e-03

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 42.91  E-value: 1.27e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 494899544  634 LRGIDVAFPLGVLTAVTGVSGSGKSTLVnDILA 666
Cdd:PLN03140  896 LREVTGAFRPGVLTALMGVSGAGKTTLM-DVLA 927
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
430-595 1.29e-03

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 42.36  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 430 DHPVYPSKSIADVCALSVADCAEYLSGLQLDSRQKAIAGPVLKEV---------------QARITFLLD-VGLDYLSLAR 493
Cdd:COG0488   69 EPPLDDDLTVLDTVLDGDAELRALEAELEELEAKLAEPDEDLERLaelqeefealggweaEARAEEILSgLGFPEEDLDR 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 494 AAGSLSGGeaQRIRLAtqigsgLAGVLY------VLDEPSIGLhqrDnrrlIDTL----TRLRDLGNTLIVVEHDEDTI- 562
Cdd:COG0488  149 PVSELSGG--WRRRVA------LARALLsepdllLLDEPTNHL---D----LESIewleEFLKNYPGTVLVVSHDRYFLd 213
                        170       180       190
                 ....*....|....*....|....*....|...
gi 494899544 563 RAADWIVDIgpragEHGGHVVHSGNYRDLLKNR 595
Cdd:COG0488  214 RVATRILEL-----DRGKLTLYPGNYSAYLEQR 241
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
491-558 1.30e-03

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: 41.58  E-value: 1.30e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494899544 491 LARAAGSLSGGEAQRIRLATQIGSglAGVLYVLDEPS--IGLHQRDN-RRLIdtlTRLRDLGNTLIVVEHD 558
Cdd:cd03236  133 LDRNIDQLSGGELQRVAIAAALAR--DADFYFFDEPSsyLDIKQRLNaARLI---RELAEDDNYVLVVEHD 198
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
840-909 1.35e-03

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


Pssm-ID: 444078 [Multi-domain]  Cd Length: 605  Bit Score: 42.50  E-value: 1.35e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494899544 840 LSGGEAQRVKLAAELQKRSAgrtIYILDEPTTGL--HFE-DIKKLLgvinGLVDKGNTVIVIEHNLDVIKTAD 909
Cdd:COG5265  495 LSGGEKQRVAIARTLLKNPP---ILIFDEATSALdsRTErAIQAAL----REVARGRTTLVIAHRLSTIVDAD 560
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
835-914 1.42e-03

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 42.35  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 835 QPAPTLSGGEAQRVKLAAELQKRSAgrtIYILDEPTTGLHF---EDIKKLlgvINGLVDKGNTVIVIEHNLD-VIKTADW 910
Cdd:PRK15439 399 QAARTLSGGNQQKVLIAKCLEASPQ---LLIVDEPTRGVDVsarNDIYQL---IRSIAAQNVAVLFISSDLEeIEQMADR 472

                 ....
gi 494899544 911 VIDM 914
Cdd:PRK15439 473 VLVM 476
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
497-592 1.45e-03

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 42.26  E-value: 1.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 497 SLSGGEAQRIRLATQIgsgL--AGVLyVLDEPSIGLHQRDNRRLIDTLTRLRDlGNTLIVVEHDEDTIRAADWIVDIgpr 574
Cdd:PRK13657 471 QLSGGERQRLAIARAL---LkdPPIL-ILDEATSALDVETEAKVKAALDELMK-GRTTFIIAHRLSTVRNADRILVF--- 542
                         90
                 ....*....|....*...
gi 494899544 575 agEHgGHVVHSGNYRDLL 592
Cdd:PRK13657 543 --DN-GRVVESGSFDELV 557
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
832-900 1.48e-03

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 42.34  E-value: 1.48e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494899544  832 RLGQPAPT--LSGGEAQRVKLAAELQKRSagrTIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEH 900
Cdd:TIGR00955 157 RIGVPGRVkgLSGGERKRLAFASELLTDP---PLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
cbiO PRK13642
energy-coupling factor transporter ATPase;
816-939 1.58e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 41.62  E-value: 1.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 816 IHRYLKTLVDVGLGYVRLGQPApTLSGGEAQRVKLAAELQKRSagrTIYILDEPTTGLHFEDIKKLLGVINGLVDKGN-T 894
Cdd:PRK13642 118 IKRVDEALLAVNMLDFKTREPA-RLSGGQKQRVAVAGIIALRP---EIIILDESTSMLDPTGRQEIMRVIHEIKEKYQlT 193
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 494899544 895 VIVIEHNLDVIKTADWVIDMgpeggtGGGTVIAEGTPEDIAEVPE 939
Cdd:PRK13642 194 VLSITHDLDEAASSDRILVM------KAGEIIKEAAPSELFATSE 232
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
481-586 1.59e-03

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 41.30  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 481 LLDVGLDYLSlARAAGSLSGGEAQRIRLA---TQI--GSGLAGVLYvLDEPSIGL---HQrdnrrlIDTLTRLRDL---- 548
Cdd:PRK13548 119 LAQVDLAHLA-GRDYPQLSGGEQQRVQLArvlAQLwePDGPPRWLL-LDEPTSALdlaHQ------HHVLRLARQLaher 190
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 494899544 549 GNTLIVVEHDED-TIRAADWIVDIgprageHGGHVVHSG 586
Cdd:PRK13548 191 GLAVIVVLHDLNlAARYADRIVLL------HQGRLVADG 223
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
482-602 1.64e-03

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 42.31  E-value: 1.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 482 LDVGLDYLsLARAAGSLSGGEAQRIRLATQIgsgL--AGVLyVLDEPSIGLHQRDNRRL---IDTLTRLRdlgnTLIVVE 556
Cdd:PRK11176 466 MDNGLDTV-IGENGVLLSGGQRQRIAIARAL---LrdSPIL-ILDEATSALDTESERAIqaaLDELQKNR----TSLVIA 536
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 494899544 557 HDEDTIRAADWIVDIgpragEHgGHVVHSGNYRDLLKNRksltGAY 602
Cdd:PRK11176 537 HRLSTIEKADEILVV-----ED-GEIVERGTHAELLAQN----GVY 572
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
466-594 1.67e-03

ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213225 [Multi-domain]  Cd Length: 233  Bit Score: 41.03  E-value: 1.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 466 IAGPVLKEVQARITFLLD-VGLDYLSLARAAgSLSGGEAQRIRLATQIGSGLAGVLyvLDEPSIGLHQRDNRRLIDTLTR 544
Cdd:cd03258  109 IAGVPKAEIEERVLELLElVGLEDKADAYPA-QLSGGQKQRVGIARALANNPKVLL--CDEATSALDPETTQSILALLRD 185
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 494899544 545 L-RDLGNTLIVVEHDEDTIRA-ADWIVDIgprageHGGHVVHSGNYRDLLKN 594
Cdd:cd03258  186 InRELGLTIVLITHEMEVVKRiCDRVAVM------EKGEVVEEGTVEEVFAN 231
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
783-934 1.80e-03

Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213232 [Multi-domain]  Cd Length: 220  Bit Score: 40.82  E-value: 1.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 783 RETLEVH-----YKGktisEVLDMPIEEAADFFEPVTSIHRYLKTLvdvglgyvrlgqpaptlSGGEAQRVKLAAELQKR 857
Cdd:cd03265   91 WENLYIHarlygVPG----AERRERIDELLDFVGLLEAADRLVKTY-----------------SGGMRRRLEIARSLVHR 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 858 SagrTIYILDEPTTGLHFEDIKKLLGVINGLVDK-GNTVIVIEHNLD-VIKTADWV--IDMGpeggtgggTVIAEGTPED 933
Cdd:cd03265  150 P---EVLFLDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEeAEQLCDRVaiIDHG--------RIIAEGTPEE 218

                 .
gi 494899544 934 I 934
Cdd:cd03265  219 L 219
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
830-911 1.95e-03

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 41.19  E-value: 1.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 830 YVRLGQPAPTLSGGEAQRVKLAAELQKRSagrTIYILDEPTTGLHF---EDIKKLLGVINglvdKGNTVIVIEHN-LDVI 905
Cdd:PRK14246 144 YDRLNSPASQLSGGQQQRLTIARALALKP---KVLLMDEPTSMIDIvnsQAIEKLITELK----NEIAIVIVSHNpQQVA 216

                 ....*.
gi 494899544 906 KTADWV 911
Cdd:PRK14246 217 RVADYV 222
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
840-914 2.08e-03

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 40.89  E-value: 2.08e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494899544 840 LSGGEAQRVKLAAELQKRSAgrtIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNLDVIK-TADWVIDM 914
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPE---VILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARdVADRAIFM 217
GguA NF040905
sugar ABC transporter ATP-binding protein;
865-909 2.09e-03

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 41.70  E-value: 2.09e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 494899544 865 ILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNL-DVIKTAD 909
Cdd:NF040905 162 ILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLnEIRRVAD 207
CP_lyasePhnL TIGR02324
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ...
499-573 2.44e-03

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


Pssm-ID: 131377 [Multi-domain]  Cd Length: 224  Bit Score: 40.45  E-value: 2.44e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494899544  499 SGGEAQRIRLATQIGSGLAGVLyvLDEPSIGLHQRDNRRLIDTLTRLRDLGNTLIVVEHDEDTIRA-ADWIVDIGP 573
Cdd:TIGR02324 151 SGGEQQRVNIARGFIADYPILL--LDEPTASLDAANRQVVVELIAEAKARGAALIGIFHDEEVRELvADRVMDVTP 224
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
816-941 2.46e-03

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 41.94  E-value: 2.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  816 IHRYLKTLVDvglGYVRL-GQPAPTLSGGEAQRVKLAAELQKRSagrTIYILDEPTTGLHFEDIKKLLGVINGLvdKGN- 893
Cdd:PTZ00265  558 IHDFVSALPD---KYETLvGSNASKLSGGQKQRISIARAIIRNP---KILILDEATSSLDNKSEYLVQKTINNL--KGNe 629
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 494899544  894 --TVIVIEHNLDVIKTAD--WVIDMGPEGGTGGGTVIAEGTPEDIAEVPESH 941
Cdd:PTZ00265  630 nrITIIIAHRLSTIRYANtiFVLSNRERGSTVDVDIIGEDPTKDNKENNNKN 681
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
840-902 2.79e-03

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 40.64  E-value: 2.79e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494899544 840 LSGGEAQRVKLAAELQKRsaGRTIyILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNL 902
Cdd:PRK15056 143 LSGGQKKRVFLARAIAQQ--GQVI-LLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNL 202
cbiO PRK13646
energy-coupling factor transporter ATPase;
471-624 2.83e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 40.92  E-value: 2.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 471 LKEVQAR-ITFLLDVGLDYLSLARAAGSLSGGEAQRIrlatQIGSGLA--GVLYVLDEPSIGLHQRDNRRLIDTLTRLR- 546
Cdd:PRK13646 118 LDEVKNYaHRLLMDLGFSRDVMSQSPFQMSGGQMRKI----AIVSILAmnPDIIVLDEPTAGLDPQSKRQVMRLLKSLQt 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 547 DLGNTLIVVEHD-EDTIRAADWIVDIgprageHGGHVVHSGNYRDLLKNRKSLTGAYLsgreSLP-VPAIRRPINRKRQL 624
Cdd:PRK13646 194 DENKTIILVSHDmNEVARYADEVIVM------KEGSIVSQTSPKELFKDKKKLADWHI----GLPeIVQLQYDFEQKYQT 263
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
833-912 2.95e-03

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


Pssm-ID: 213234 [Multi-domain]  Cd Length: 236  Bit Score: 40.39  E-value: 2.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 833 LGQPAPTLSGGEAQRVKLAAELQKRSagrTIYILDEPTTGLHF---EDIKKLLGVINGlvDKGNTVIVIEHNL-DVIKTA 908
Cdd:cd03267  147 LDTPVRQLSLGQRMRAEIAAALLHEP---EILFLDEPTIGLDVvaqENIRNFLKEYNR--ERGTTVLLTSHYMkDIEALA 221

                 ....
gi 494899544 909 DWVI 912
Cdd:cd03267  222 RRVL 225
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
498-592 3.08e-03

ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213220 [Multi-domain]  Cd Length: 236  Bit Score: 40.29  E-value: 3.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 498 LSGGEAQRIRLATQIGSGlAGVLyVLDEPSIGLHQRDNRRLIDTLTRLRDlGNTLIVVEHDEDTIRAADWIVDIgprage 577
Cdd:cd03253  138 LSGGEKQRVAIARAILKN-PPIL-LLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTIVNADKIIVL------ 208
                         90
                 ....*....|....*
gi 494899544 578 HGGHVVHSGNYRDLL 592
Cdd:cd03253  209 KDGRIVERGTHEELL 223
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
833-937 3.22e-03

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 41.55  E-value: 3.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544  833 LGQPAPTLSGGEAQRVKLAAELQKRSagrTIYILDEPTTGLHFEDIKKLLGVINGLVDKGN-TVIVIEHNLDVIKTADWV 911
Cdd:PTZ00265 1352 VGPYGKSLSGGQKQRIAIARALLREP---KILLLDEATSSLDSNSEKLIEKTIVDIKDKADkTIITIAHRIASIKRSDKI 1428
                          90       100
                  ....*....|....*....|....*..
gi 494899544  912 IDM-GPEggTGGGTVIAEGTPEDIAEV 937
Cdd:PTZ00265 1429 VVFnNPD--RTGSFVQAHGTHEELLSV 1453
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
466-558 3.29e-03

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: 40.18  E-value: 3.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 466 IAGPVLKEVQARITFLLD---VGLDYLSLARAAGSLSGGEAQRIRLAtqigSGLAG--VLYVLDEPSIGLHQRDNRRLID 540
Cdd:cd03257  111 IHGKLSKKEARKEAVLLLlvgVGLPEEVLNRYPHELSGGQRQRVAIA----RALALnpKLLIADEPTSALDVSVQAQILD 186
                         90
                 ....*....|....*....
gi 494899544 541 TLTRLRD-LGNTLIVVEHD 558
Cdd:cd03257  187 LLKKLQEeLGLTLLFITHD 205
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
826-906 3.29e-03

ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213225 [Multi-domain]  Cd Length: 233  Bit Score: 40.26  E-value: 3.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 826 VGLGYVRLGQPApTLSGGEAQRVKLAAELqkrSAGRTIYILDEPTTGLHFE---DIKKLLGVIN---GLvdkgnTVIVIE 899
Cdd:cd03258  128 VGLEDKADAYPA-QLSGGQKQRVGIARAL---ANNPKVLLCDEATSALDPEttqSILALLRDINrelGL-----TIVLIT 198

                 ....*..
gi 494899544 900 HNLDVIK 906
Cdd:cd03258  199 HEMEVVK 205
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
833-898 3.36e-03

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 41.16  E-value: 3.36e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494899544 833 LGQPAPTLSGGEAQRVKLAAELqkrSAGRTIYILDEPTTGLhfeDI--KK-LLGVINGLVDKGNTVIVI 898
Cdd:COG1129  388 PEQPVGNLSGGNQQKVVLAKWL---ATDPKVLILDEPTRGI---DVgaKAeIYRLIRELAAEGKAVIVI 450
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
497-571 3.54e-03

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: 39.48  E-value: 3.54e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494899544 497 SLSGGEAQRIRLATQIGSglAGVLYVLDEPSIGLHQRDNRRLIDTLTRLRDLGN-TLIVVEHDedtIRAADWIVDI 571
Cdd:cd03222   71 DLSGGELQRVAIAAALLR--NATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHD---LAVLDYLSDR 141
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
495-559 4.39e-03

thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.


Pssm-ID: 274331 [Multi-domain]  Cd Length: 530  Bit Score: 40.81  E-value: 4.39e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494899544  495 AGSLSGGEAQRIRLATQIGSGlAGVLyVLDEPSIGLHQRDNRRLIDTLtRLRDLGNTLIVVEHDE 559
Cdd:TIGR02868 469 GARLSGGERQRLALARALLAD-APIL-LLDEPTEHLDAETADELLEDL-LAALSGRTVVLITHHL 530
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
472-569 4.48e-03

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 40.47  E-value: 4.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 472 KEVQARITFLLD-VGLDYLsLARAAGSLSGGEAQRIRLAtqigSGLA---GVLyVLDEPSIGLhqrDNR---RLIDTLTR 544
Cdd:COG3842  110 AEIRARVAELLElVGLEGL-ADRYPHQLSGGQQQRVALA----RALApepRVL-LLDEPLSAL---DAKlreEMREELRR 180
                         90       100
                 ....*....|....*....|....*..
gi 494899544 545 L-RDLGNTLIVVEHD-EDTIRAADWIV 569
Cdd:COG3842  181 LqRELGITFIYVTHDqEEALALADRIA 207
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
839-934 4.87e-03

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 39.77  E-value: 4.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 839 TLSGGEAQRVKLAAELQKRSagRTIyILDEPTTGLHFEDIKKLLGVINGLV-DKGNTVIVIEHNLDVI-KTADWVIDM-G 915
Cdd:PRK10575 147 SLSGGERQRAWIAMLVAQDS--RCL-LLDEPTSALDIAHQVDVLALVHRLSqERGLTVIAVLHDINMAaRYCDYLVALrG 223
                         90
                 ....*....|....*....
gi 494899544 916 PEggtgggtVIAEGTPEDI 934
Cdd:PRK10575 224 GE-------MIAQGTPAEL 235
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
830-915 4.94e-03

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 39.86  E-value: 4.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 830 YVRLGQPAPTLSGGEAQRVKLAAELQKRSagrTIYILDEPTTGLHFEDIKKLLGVINGLVDKGNTVIVIEHNLD-VIKTA 908
Cdd:PRK11614 128 HERRIQRAGTMSGGEQQMLAIGRALMSQP---RLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANqALKLA 204

                 ....*....
gi 494899544 909 D--WVIDMG 915
Cdd:PRK11614 205 DrgYVLENG 213
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
840-914 4.95e-03

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 40.46  E-value: 4.95e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494899544 840 LSGGEAQRVKLAAELQKRSAgrtIYILDEPTTGLHFEDIKKLLGVINGLVDKGN-TVIVIEHNLDVI-KTADWVIDM 914
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPE---LLIADEPTTALDVSVQAQILQLLRELQQELNmGLLFITHNLSIVrKLADRVAVM 230
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
499-573 5.00e-03

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


Pssm-ID: 443809 [Multi-domain]  Cd Length: 229  Bit Score: 39.72  E-value: 5.00e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494899544 499 SGGEAQRIRLAtqigSGLAGV--LYVLDEPSIGLHQRDNRRLIDTLTRLRDLGNTLIVVEHDEDTIRA-ADWIVDIGP 573
Cdd:COG4778  154 SGGEQQRVNIA----RGFIADppLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAvADRVVDVTP 227
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
466-558 5.26e-03

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 39.41  E-value: 5.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 466 IAGPVLKEVQAR-ITFLLDVGLDYLSLARAAgSLSGGEAQRIRLATQIGSGLAGVLyvLDEPSIGLHQRDNRRLIDTLTR 544
Cdd:PRK11629 114 IGKKKPAEINSRaLEMLAAVGLEHRANHRPS-ELSGGERQRVAIARALVNNPRLVL--ADEPTGNLDARNADSIFQLLGE 190
                         90
                 ....*....|....*
gi 494899544 545 L-RDLGNTLIVVEHD 558
Cdd:PRK11629 191 LnRLQGTAFLVVTHD 205
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
840-912 5.34e-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: 5.34e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494899544  840 LSGGEAQRVKLAAELQKRSagrTIYILDEPTTGLHFEdIKKLLGVINGLvdKGNTVIVIEHNLDVIKTADWVI 912
Cdd:TIGR00958 618 LSGGQKQRIAIARALVRKP---RVLILDEATSALDAE-CEQLLQESRSR--ASRTVLLIAHRLSTVERADQIL 684
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
491-586 5.73e-03

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: 39.27  E-value: 5.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 491 LARAAGSLSGGEAQRIRLATQIGSGLAGVLyvLDEPSIGLHQRDNRRLIDTLTRLRDLGNTLIVVEHDEDTI-RAADWIV 569
Cdd:cd03266  130 LDRRVGGFSTGMRQKVAIARALVHDPPVLL--LDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVeRLCDRVV 207
                         90
                 ....*....|....*..
gi 494899544 570 DIgprageHGGHVVHSG 586
Cdd:cd03266  208 VL------HRGRVVYEG 218
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
840-915 5.77e-03

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 40.30  E-value: 5.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 840 LSGGEAQRVKLAAELQKRSagrTIYILDEPTTGL----HFEdIKKLlgvINGLVDKGNTVIVIEHNL-DVIKTADWVIDM 914
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNP---KILILDEPTRGIdvgaKYE-IYKL---INQLVQQGVAIIVISSELpEVLGLSDRVLVM 478

                 .
gi 494899544 915 G 915
Cdd:PRK13549 479 H 479
cbiO PRK13649
energy-coupling factor transporter ATPase;
481-593 5.89e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 39.73  E-value: 5.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 481 LLDVGLDYLSLARAAGSLSGGEAQRIrlatqigsGLAGVL------YVLDEPSIGLHQRDNRRLIDTLTRLRDLGNTLIV 554
Cdd:PRK13649 129 LALVGISESLFEKNPFELSGGQMRRV--------AIAGILamepkiLVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVL 200
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 494899544 555 VEH-DEDTIRAADWIVDIgprageHGGHVVHSGNYRDLLK 593
Cdd:PRK13649 201 VTHlMDDVANYADFVYVL------EKGKLVLSGKPKDIFQ 234
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
498-602 6.03e-03

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: 39.52  E-value: 6.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 498 LSGGEAQRIRLATQIgsgLAGV-LYVLDEPSIGLHQRDNRRLIDTLTRLRDlGNTLIVVEHDEDTIRAADWIVDIgprag 576
Cdd:cd03251  139 LSGGQRQRIAIARAL---LKDPpILILDEATSALDTESERLVQAALERLMK-NRTTFVIAHRLSTIENADRIVVL----- 209
                         90       100
                 ....*....|....*....|....*.
gi 494899544 577 EHGGhVVHSGNYRDLLknrkSLTGAY 602
Cdd:cd03251  210 EDGK-IVERGTHEELL----AQGGVY 230
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
821-912 6.31e-03

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


Pssm-ID: 213265 [Multi-domain]  Cd Length: 211  Bit Score: 39.01  E-value: 6.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 821 KTLVDVGLGYVRLGQPApTLSGGEAQRVKLAAELQKRsagRTIYILDEPTTGLHFEDIKKLLGVINGL-VDKGNTVIVIE 899
Cdd:cd03298  111 VALARVGLAGLEKRLPG-ELSGGERQRVALARVLVRD---KPVLLLDEPFAALDPALRAEMLDLVLDLhAETKMTVLMVT 186
                         90
                 ....*....|....
gi 494899544 900 HNL-DVIKTADWVI 912
Cdd:cd03298  187 HQPeDAKRLAQRVV 200
GguA NF040905
sugar ABC transporter ATP-binding protein;
835-898 7.38e-03

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 40.16  E-value: 7.38e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494899544 835 QPAPTLSGGEAQRVKLAAELqkrSAGRTIYILDEPTTGL----HFEdikkLLGVINGLVDKGNTVIVI 898
Cdd:NF040905 400 QKVGNLSGGNQQKVVLSKWL---FTDPDVLILDEPTRGIdvgaKYE----IYTIINELAAEGKGVIVI 460
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
490-558 7.44e-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: 7.44e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494899544 490 SLARAAGSLSGGEAQRIrlatQIGSGLA--GVLYVLDEPSIGL--HQRDN-RRLIDTLTRlrdLGNTLIVVEHD 558
Cdd:COG1245  205 ILDRDISELSGGELQRV----AIAAALLrdADFYFFDEPSSYLdiYQRLNvARLIRELAE---EGKYVLVVEHD 271
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
472-598 7.47e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 39.20  E-value: 7.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 472 KEVQARITFLLD-VGLDYLsLARAAGSLSGGEAQRIrlatQIGSGLA--GVLYVLDEPSIGLHQRDNRRLIDTLTRLRDL 548
Cdd:PRK13632 117 KKMKDIIDDLAKkVGMEDY-LDKEPQNLSGGQKQRV----AIASVLAlnPEIIIFDESTSMLDPKGKREIKKIMVDLRKT 191
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 494899544 549 GN-TLIVVEHDEDTIRAADWIVDIGpragehGGHVVHSGNYRDLLKNRKSL 598
Cdd:PRK13632 192 RKkTLISITHDMDEAILADKVIVFS------EGKLIAQGKPKEILNNKEIL 236
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
634-666 8.14e-03

Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213199 [Multi-domain]  Cd Length: 192  Bit Score: 38.76  E-value: 8.14e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 494899544 634 LRGIDVAFPLGVLTAVTGVSGSGKSTLVnDILA 666
Cdd:cd03232   23 LNNISGYVKPGTLTALMGESGAGKTTLL-DVLA 54
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
463-558 9.77e-03

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 38.94  E-value: 9.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494899544 463 QKAIAGPVLKEVQAriTFLLDVGLDylslaraagSLSGGEAQRIRLATQIGSglAGVLYVLDEPSIGLHQRDNRRLIDTL 542
Cdd:PRK09544  97 KKEDILPALKRVQA--GHLIDAPMQ---------KLSGGETQRVLLARALLN--RPQLLVLDEPTQGVDVNGQVALYDLI 163
                         90
                 ....*....|....*..
gi 494899544 543 TRLR-DLGNTLIVVEHD 558
Cdd:PRK09544 164 DQLRrELDCAVLMVSHD 180
 
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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