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Conserved domains on  [gi|499583918|ref|WP_011264701|]
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excinuclease ABC subunit UvrA [[Mycoplasma] mobile]

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;
6-943 0e+00

excinuclease ABC subunit UvrA;


:

Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 1739.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918   6 DTHNFISIKGAKENNLKNIDVVIPKNKLVVFTGLSGSGKSSLAFNTIYEEGRRRYVDSLGSYARQFLGGTKKPDVHSIDG 85
Cdd:PRK00349   1 MMMDKIIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  86 LSPAISIEQKTTHNNPRSTVGTVTEIHDYLRLLYARIGHPFCSNHKIKITSQKLKDILNTVFSYEKDSKILILAPVISGA 165
Cdd:PRK00349  81 LSPAISIDQKTTSHNPRSTVGTVTEIYDYLRLLYARVGKPHCPNCGRPIEAQTVSQMVDRVLELPEGTRLQILAPVVRGR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 166 KGTHQVLLEKLKKD-FLRLKIDGEIYSLDEEINLDKSKKHDIEIVVDRLILNEENRSRIADGIEIALEYSKGLVNVEILG 244
Cdd:PRK00349 161 KGEHKKLLENLRKQgFVRVRVDGEVYDLDEPPKLDKNKKHTIEVVVDRLVVKEDIRQRLADSIETALKLSDGLVVVEVMD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 245 ---KEKKMFSQLFSCPYGDFEMPKIETKLFSFNSPYGMCEVCKGIGVSLKSDPDLLIPDKTKSILQGAIIPFQNTveTSN 321
Cdd:PRK00349 241 dpeAEELLFSEKFACPVCGFSIPELEPRLFSFNSPYGACPTCDGLGVKLEFDPDLVVPDPELSLAEGAIAPWSRS--SSS 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 322 LDWQEFKALLDYYEISAAKPIEKMTKSELDIIYYGS-KEDINYTNVSVSGNKYTRFNKIEGILTKMERRFLETTSEQLRT 400
Cdd:PRK00349 319 YYFQMLKSLAEHYGFDLDTPWKDLPEEVQDIILYGSgDEEIEFRYKNDRGRTRERKHPFEGVIPNLERRYRETESEYVRE 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 401 WYLKFMSEIQCSKCKGDRLNDYALAVQIEGLNISDFSKLSIEEGLSKILSLEISSFEKEVSTLIVNEIVNRLTFLSDVGL 480
Cdd:PRK00349 399 ELEKYMSERPCPSCKGKRLKPEALAVKVGGKNIGEVSELSIGEALEFFENLKLSEQEAKIAEPILKEIRERLKFLVDVGL 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 481 EYLTLNRTAETLSGGEAQRIRLATQIGSNLTGVLYVLDEPSIGLHQKDNEKLIKTLKHMVEIGNTLIVVEHDDETILEAD 560
Cdd:PRK00349 479 DYLTLSRSAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDEDTIRAAD 558
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 561 YILDIGPKAGNEGGQIVAQGSVEDIKKSKESITGKYLSGELKIEIPTFRRSGSGEIIRVIGAKENNLKNIDVKFPIGKFI 640
Cdd:PRK00349 559 YIVDIGPGAGVHGGEVVASGTPEEIMKNPNSLTGQYLSGKKKIEVPKERRKGNGKFLKLKGARENNLKNVDVEIPLGKFT 638
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 641 AVTGVSGSGKSTLVNEVLIKGI-EFVKGSQVHPGKHKEIKGLHNIDKIIQISQSPIGRTPRSNPATYTTVFDDIRDLFAN 719
Cdd:PRK00349 639 CVTGVSGSGKSTLINETLYKALaRKLNGAKKVPGKHKEIEGLEHLDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAG 718
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 720 TEDARASGFLKGRFSFNVNGGRCDKCSGDGYLKIEMHFLPDVYVVCDHCDGKRYNPETLEIKYKFKNISDVLDMTVSEAF 799
Cdd:PRK00349 719 TPEAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEVKYKGKNIADVLDMTVEEAL 798
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 800 DFFANRAKIREKLETLMDVGLGYIKLGQPATTLSGGEAQRVKLATHLLKKSTGKTLYVLDEPTTGLHSYDVSNLLEVLKR 879
Cdd:PRK00349 799 EFFEAIPKIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELSKRSTGKTLYILDEPTTGLHFEDIRKLLEVLHR 878
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499583918 880 IVNKGDTVIVIEHNLDVIKSVDYIIDLGPGGGTNGGKIVATGTPEQVAEIKESFTGQYLKRMLK 943
Cdd:PRK00349 879 LVDKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVATGTPEEVAKVEASYTGRYLKPVLE 942
 
Name Accession Description Interval E-value
uvrA PRK00349
excinuclease ABC subunit UvrA;
6-943 0e+00

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 1739.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918   6 DTHNFISIKGAKENNLKNIDVVIPKNKLVVFTGLSGSGKSSLAFNTIYEEGRRRYVDSLGSYARQFLGGTKKPDVHSIDG 85
Cdd:PRK00349   1 MMMDKIIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  86 LSPAISIEQKTTHNNPRSTVGTVTEIHDYLRLLYARIGHPFCSNHKIKITSQKLKDILNTVFSYEKDSKILILAPVISGA 165
Cdd:PRK00349  81 LSPAISIDQKTTSHNPRSTVGTVTEIYDYLRLLYARVGKPHCPNCGRPIEAQTVSQMVDRVLELPEGTRLQILAPVVRGR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 166 KGTHQVLLEKLKKD-FLRLKIDGEIYSLDEEINLDKSKKHDIEIVVDRLILNEENRSRIADGIEIALEYSKGLVNVEILG 244
Cdd:PRK00349 161 KGEHKKLLENLRKQgFVRVRVDGEVYDLDEPPKLDKNKKHTIEVVVDRLVVKEDIRQRLADSIETALKLSDGLVVVEVMD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 245 ---KEKKMFSQLFSCPYGDFEMPKIETKLFSFNSPYGMCEVCKGIGVSLKSDPDLLIPDKTKSILQGAIIPFQNTveTSN 321
Cdd:PRK00349 241 dpeAEELLFSEKFACPVCGFSIPELEPRLFSFNSPYGACPTCDGLGVKLEFDPDLVVPDPELSLAEGAIAPWSRS--SSS 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 322 LDWQEFKALLDYYEISAAKPIEKMTKSELDIIYYGS-KEDINYTNVSVSGNKYTRFNKIEGILTKMERRFLETTSEQLRT 400
Cdd:PRK00349 319 YYFQMLKSLAEHYGFDLDTPWKDLPEEVQDIILYGSgDEEIEFRYKNDRGRTRERKHPFEGVIPNLERRYRETESEYVRE 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 401 WYLKFMSEIQCSKCKGDRLNDYALAVQIEGLNISDFSKLSIEEGLSKILSLEISSFEKEVSTLIVNEIVNRLTFLSDVGL 480
Cdd:PRK00349 399 ELEKYMSERPCPSCKGKRLKPEALAVKVGGKNIGEVSELSIGEALEFFENLKLSEQEAKIAEPILKEIRERLKFLVDVGL 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 481 EYLTLNRTAETLSGGEAQRIRLATQIGSNLTGVLYVLDEPSIGLHQKDNEKLIKTLKHMVEIGNTLIVVEHDDETILEAD 560
Cdd:PRK00349 479 DYLTLSRSAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDEDTIRAAD 558
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 561 YILDIGPKAGNEGGQIVAQGSVEDIKKSKESITGKYLSGELKIEIPTFRRSGSGEIIRVIGAKENNLKNIDVKFPIGKFI 640
Cdd:PRK00349 559 YIVDIGPGAGVHGGEVVASGTPEEIMKNPNSLTGQYLSGKKKIEVPKERRKGNGKFLKLKGARENNLKNVDVEIPLGKFT 638
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 641 AVTGVSGSGKSTLVNEVLIKGI-EFVKGSQVHPGKHKEIKGLHNIDKIIQISQSPIGRTPRSNPATYTTVFDDIRDLFAN 719
Cdd:PRK00349 639 CVTGVSGSGKSTLINETLYKALaRKLNGAKKVPGKHKEIEGLEHLDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAG 718
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 720 TEDARASGFLKGRFSFNVNGGRCDKCSGDGYLKIEMHFLPDVYVVCDHCDGKRYNPETLEIKYKFKNISDVLDMTVSEAF 799
Cdd:PRK00349 719 TPEAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEVKYKGKNIADVLDMTVEEAL 798
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 800 DFFANRAKIREKLETLMDVGLGYIKLGQPATTLSGGEAQRVKLATHLLKKSTGKTLYVLDEPTTGLHSYDVSNLLEVLKR 879
Cdd:PRK00349 799 EFFEAIPKIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELSKRSTGKTLYILDEPTTGLHFEDIRKLLEVLHR 878
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499583918 880 IVNKGDTVIVIEHNLDVIKSVDYIIDLGPGGGTNGGKIVATGTPEQVAEIKESFTGQYLKRMLK 943
Cdd:PRK00349 879 LVDKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVATGTPEEVAKVEASYTGRYLKPVLE 942
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
6-945 0e+00

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


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 1613.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918   6 DTHNFISIKGAKENNLKNIDVVIPKNKLVVFTGLSGSGKSSLAFNTIYEEGRRRYVDSLGSYARQFLGGTKKPDVHSIDG 85
Cdd:COG0178    1 MMMDKIRIRGAREHNLKNIDVDIPRNKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  86 LSPAISIEQKTTHNNPRSTVGTVTEIHDYLRLLYARIGHPFCSNHKIKITSQKLKDILNTVFSYEKDSKILILAPVISGA 165
Cdd:COG0178   81 LSPAISIEQKTTSRNPRSTVGTVTEIYDYLRLLFARVGTPHCPICGRPVEKQTVDQIVDRILALPEGTRLQILAPVVRGR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 166 KGTHQVLLEKLKKD-FLRLKIDGEIYSLDEEINLDKSKKHDIEIVVDRLILNEENRSRIADGIEIALEYSKGLVNVEILG 244
Cdd:COG0178  161 KGEHKELLEELRKQgFVRVRVDGEVYDLDEEPELDKNKKHTIEVVVDRLVVKEDIRSRLADSVETALKLGDGLVIVEVVD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 245 KEKKM-FSQLFSCPYGDFEMPKIETKLFSFNSPYGMCEVCKGIGVSLKSDPDLLIPDKTKSILQGAIIPFQNtvETSNLD 323
Cdd:COG0178  241 EGEELlFSEKFACPDCGISFEELEPRLFSFNSPYGACPTCDGLGRVLEFDPDLVIPDPSLSLAEGAIAPWSG--PSSSYY 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 324 WQEFKALLDYYEISAAKPIEKMTKSELDIIYYGSKEDI--NYTNVSVSGNKYTRFnkiEGILTKMERRFLETTSEQLRTW 401
Cdd:COG0178  319 FQLLEALAKHYGFDLDTPWKDLPEEQRDLILYGSDEKIkfRYKNRGRRRTYEKPF---EGVIPFLERRYRETYSEHVREE 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 402 YLKFMSEIQCSKCKGDRLNDYALAVQIEGLNISDFSKLSIEEGLSKILSLEISSFEKEVSTLIVNEIVNRLTFLSDVGLE 481
Cdd:COG0178  396 LSRYMSETPCPACKGARLKPEALAVKIGGKNIAELTALSIDEALEFFENLELTEREAEIAERILKEIRSRLGFLVDVGLD 475
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 482 YLTLNRTAETLSGGEAQRIRLATQIGSNLTGVLYVLDEPSIGLHQKDNEKLIKTLKHMVEIGNTLIVVEHDDETILEADY 561
Cdd:COG0178  476 YLTLDRSAGTLSGGEAQRIRLATQIGSGLVGVLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDTIRAADY 555
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 562 ILDIGPKAGNEGGQIVAQGSVEDIKKSKESITGKYLSGELKIEIPTFRRSGSGEIIRVIGAKENNLKNIDVKFPIGKFIA 641
Cdd:COG0178  556 IIDIGPGAGEHGGEVVAQGTPEEILKNPDSLTGQYLSGRKRIPVPKKRRKGNGKFLTIKGARENNLKNVDVEIPLGVLTC 635
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 642 VTGVSGSGKSTLVNEVLIKGIEFVK-GSQVHPGKHKEIKGLHNIDKIIQISQSPIGRTPRSNPATYTTVFDDIRDLFANT 720
Cdd:COG0178  636 VTGVSGSGKSTLVNDILYPALARKLnGAKEKPGPHDSIEGLEHIDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAQT 715
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 721 EDARASGFLKGRFSFNVNGGRCDKCSGDGYLKIEMHFLPDVYVVCDHCDGKRYNPETLEIKYKFKNISDVLDMTVSEAFD 800
Cdd:COG0178  716 PEAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALE 795
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 801 FFANRAKIREKLETLMDVGLGYIKLGQPATTLSGGEAQRVKLATHLLKKSTGKTLYVLDEPTTGLHSYDVSNLLEVLKRI 880
Cdd:COG0178  796 FFENIPKIARKLQTLQDVGLGYIKLGQPATTLSGGEAQRVKLASELSKRSTGKTLYILDEPTTGLHFHDIRKLLEVLHRL 875
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499583918 881 VNKGDTVIVIEHNLDVIKSVDYIIDLgpgggtnggKIVATGTPEQVAEIKESFTGQYLKRMLKNA 945
Cdd:COG0178  876 VDKGNTVVVIEHNLDVIKTADWIIDLgpeggdgggEIVAEGTPEEVAKVKASYTGRYLKEYLEAA 940
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
10-927 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: 1380.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918   10 FISIKGAKENNLKNIDVVIPKNKLVVFTGLSGSGKSSLAFNTIYEEGRRRYVDSLGSYARQFLGGTKKPDVHSIDGLSPA 89
Cdd:TIGR00630   1 KIIVRGAREHNLKNIDVEIPRDKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGVMDKPDVDSIEGLSPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918   90 ISIEQKTTHNNPRSTVGTVTEIHDYLRLLYARIGHPFCSNHKIKITSQKLKDILNTVFSYEKDSKILILAPVISGAKGTH 169
Cdd:TIGR00630  81 ISIDQKTTSHNPRSTVGTITEIYDYLRLLFARVGTPYCPTCGRPISRQTPSQIVDQILALPEGTRVILLAPIVRGRKGEF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  170 QVLLEKLKKD-FLRLKIDGEIYSLDEEINLDKSKKHDIEIVVDRLILNEENRSRIADGIEIALEYSKGLVNVEILG---- 244
Cdd:TIGR00630 161 RKLLEKLRKQgFARVRVDGEVYPLEDPPKLEKNKKHTIDVVIDRLTVKNENRSRLAESVETALRLGDGLLEVEFDDdeev 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  245 --KEKKMFSQLFSCPYGDFEMPKIETKLFSFNSPYGMCEVCKGIGVSLKSDPDLLIPDKTKSILQGAIIPFQNtvETSNL 322
Cdd:TIGR00630 241 aeSKEELFSEKFACPECGFSLPELEPRLFSFNSPYGACPECSGLGIKQEFDPELIIPDPLLSLNGGAIVPFKK--STTSY 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  323 DWQEFKALLDYYEISAAKPIEKMTKSELDIIYYGSKEDINYTNVSVSGNKYTRFNK-IEGILTKMERRFLETTSEQLRTW 401
Cdd:TIGR00630 319 YRQMFASLAEHLGFDLDTPWKDLPEEAQKAILYGSGEEVIVVKYRNGGGETFRYHKpFEGVIPELERRYLETESESMREY 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  402 YLKFMSEIQCSKCKGDRLNDYALAVQIEGLNISDFSKLSIEEGLSKILSLEISSFEKEVSTLIVNEIVNRLTFLSDVGLE 481
Cdd:TIGR00630 399 LEKFMSERPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFNQLTLTPEEKKIAEEVLKEIRERLGFLIDVGLD 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  482 YLTLNRTAETLSGGEAQRIRLATQIGSNLTGVLYVLDEPSIGLHQKDNEKLIKTLKHMVEIGNTLIVVEHDDETILEADY 561
Cdd:TIGR00630 479 YLSLSRAAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADY 558
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  562 ILDIGPKAGNEGGQIVAQGSVEDIKKSKESITGKYLSGELKIEIPTFRRSGSGEIIRVIGAKENNLKNIDVKFPIGKFIA 641
Cdd:TIGR00630 559 VIDIGPGAGEHGGEVVASGTPEEILANPDSLTGQYLSGRKKIEVPAERRPGNGKFLTLKGARENNLKNITVSIPLGLFTC 638
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  642 VTGVSGSGKSTLVNEVLIKGIE-FVKGSQVHPGKHKEIKGLHNIDKIIQISQSPIGRTPRSNPATYTTVFDDIRDLFANT 720
Cdd:TIGR00630 639 ITGVSGSGKSTLINDTLYPALAnRLNGAKTVPGRYTSIEGLEHLDKVIHIDQSPIGRTPRSNPATYTGVFDEIRELFAET 718
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  721 EDARASGFLKGRFSFNVNGGRCDKCSGDGYLKIEMHFLPDVYVVCDHCDGKRYNPETLEIKYKFKNISDVLDMTVSEAFD 800
Cdd:TIGR00630 719 PEAKVRGYTPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEAYE 798
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  801 FFANRAKIREKLETLMDVGLGYIKLGQPATTLSGGEAQRVKLATHLLKKSTGKTLYVLDEPTTGLHSYDVSNLLEVLKRI 880
Cdd:TIGR00630 799 FFEAVPSISRKLQTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKRSTGRTLYILDEPTTGLHFDDIKKLLEVLQRL 878
                         890       900       910       920
                  ....*....|....*....|....*....|....*....|....*..
gi 499583918  881 VNKGDTVIVIEHNLDVIKSVDYIIDLGPGGGTNGGKIVATGTPEQVA 927
Cdd:TIGR00630 879 VDKGNTVVVIEHNLDVIKTADYIIDLGPEGGDGGGTVVASGTPEEVA 925
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
617-923 1.45e-141

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: 422.02  E-value: 1.45e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 617 IRVIGAKENNLKNIDVKFPIGKFIAVTGVSGSGKSTLVNEVLIKGIE-FVKGSQVHPGKHKEIKGLHNIDKIIQISQSPI 695
Cdd:cd03271    1 LTLKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPALArRLHLKKEQPGNHDRIEGLEHIDKVIVIDQSPI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 696 GRTPRSNPATYTTVFDDIRDLFantedarasgflkgrfsfnvnggrcdkcsgdgylkiemhflpdvyvvCDHCDGKRYNP 775
Cdd:cd03271   81 GRTPRSNPATYTGVFDEIRELF-----------------------------------------------CEVCKGKRYNR 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 776 ETLEIKYKFKNISDVLDMTVSEAFDFFANRAKIREKLETLMDVGLGYIKLGQPATTLSGGEAQRVKLATHLLKKSTGKTL 855
Cdd:cd03271  114 ETLEVRYKGKSIADVLDMTVEEALEFFENIPKIARKLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRSTGKTL 193
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499583918 856 YVLDEPTTGLHSYDVSNLLEVLKRIVNKGDTVIVIEHNLDVIKSVDYIIDLGPGGGTNGGKIVATGTP 923
Cdd:cd03271  194 YILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLGPEGGDGGGQVVASGTP 261
UvrA_inter pfam17760
UvrA interaction domain; This domain found in UvrA proteins interacts with the UvrB protein.
137-244 1.26e-42

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


Pssm-ID: 436020 [Multi-domain]  Cd Length: 109  Bit Score: 150.71  E-value: 1.26e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  137 QKLKDILNTVFSYEKDSKILILAPVISGAKGTHQVLLEKLKKD-FLRLKIDGEIYSLDEEINLDKSKKHDIEIVVDRLIL 215
Cdd:pfam17760   1 QTVDQIVDRILALPEGTKIQILAPVVRGRKGEHKELLDDLRKQgFVRVRVDGEIYDLDDEPKLDKNKKHTIEVVVDRLVV 80
                          90       100
                  ....*....|....*....|....*....
gi 499583918  216 NEENRSRIADGIEIALEYSKGLVNVEILG 244
Cdd:pfam17760  81 KEDNRSRLADSVETALKLGKGLVIVLVLD 109
 
Name Accession Description Interval E-value
uvrA PRK00349
excinuclease ABC subunit UvrA;
6-943 0e+00

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 1739.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918   6 DTHNFISIKGAKENNLKNIDVVIPKNKLVVFTGLSGSGKSSLAFNTIYEEGRRRYVDSLGSYARQFLGGTKKPDVHSIDG 85
Cdd:PRK00349   1 MMMDKIIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  86 LSPAISIEQKTTHNNPRSTVGTVTEIHDYLRLLYARIGHPFCSNHKIKITSQKLKDILNTVFSYEKDSKILILAPVISGA 165
Cdd:PRK00349  81 LSPAISIDQKTTSHNPRSTVGTVTEIYDYLRLLYARVGKPHCPNCGRPIEAQTVSQMVDRVLELPEGTRLQILAPVVRGR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 166 KGTHQVLLEKLKKD-FLRLKIDGEIYSLDEEINLDKSKKHDIEIVVDRLILNEENRSRIADGIEIALEYSKGLVNVEILG 244
Cdd:PRK00349 161 KGEHKKLLENLRKQgFVRVRVDGEVYDLDEPPKLDKNKKHTIEVVVDRLVVKEDIRQRLADSIETALKLSDGLVVVEVMD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 245 ---KEKKMFSQLFSCPYGDFEMPKIETKLFSFNSPYGMCEVCKGIGVSLKSDPDLLIPDKTKSILQGAIIPFQNTveTSN 321
Cdd:PRK00349 241 dpeAEELLFSEKFACPVCGFSIPELEPRLFSFNSPYGACPTCDGLGVKLEFDPDLVVPDPELSLAEGAIAPWSRS--SSS 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 322 LDWQEFKALLDYYEISAAKPIEKMTKSELDIIYYGS-KEDINYTNVSVSGNKYTRFNKIEGILTKMERRFLETTSEQLRT 400
Cdd:PRK00349 319 YYFQMLKSLAEHYGFDLDTPWKDLPEEVQDIILYGSgDEEIEFRYKNDRGRTRERKHPFEGVIPNLERRYRETESEYVRE 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 401 WYLKFMSEIQCSKCKGDRLNDYALAVQIEGLNISDFSKLSIEEGLSKILSLEISSFEKEVSTLIVNEIVNRLTFLSDVGL 480
Cdd:PRK00349 399 ELEKYMSERPCPSCKGKRLKPEALAVKVGGKNIGEVSELSIGEALEFFENLKLSEQEAKIAEPILKEIRERLKFLVDVGL 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 481 EYLTLNRTAETLSGGEAQRIRLATQIGSNLTGVLYVLDEPSIGLHQKDNEKLIKTLKHMVEIGNTLIVVEHDDETILEAD 560
Cdd:PRK00349 479 DYLTLSRSAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDEDTIRAAD 558
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 561 YILDIGPKAGNEGGQIVAQGSVEDIKKSKESITGKYLSGELKIEIPTFRRSGSGEIIRVIGAKENNLKNIDVKFPIGKFI 640
Cdd:PRK00349 559 YIVDIGPGAGVHGGEVVASGTPEEIMKNPNSLTGQYLSGKKKIEVPKERRKGNGKFLKLKGARENNLKNVDVEIPLGKFT 638
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 641 AVTGVSGSGKSTLVNEVLIKGI-EFVKGSQVHPGKHKEIKGLHNIDKIIQISQSPIGRTPRSNPATYTTVFDDIRDLFAN 719
Cdd:PRK00349 639 CVTGVSGSGKSTLINETLYKALaRKLNGAKKVPGKHKEIEGLEHLDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAG 718
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 720 TEDARASGFLKGRFSFNVNGGRCDKCSGDGYLKIEMHFLPDVYVVCDHCDGKRYNPETLEIKYKFKNISDVLDMTVSEAF 799
Cdd:PRK00349 719 TPEAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEVKYKGKNIADVLDMTVEEAL 798
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 800 DFFANRAKIREKLETLMDVGLGYIKLGQPATTLSGGEAQRVKLATHLLKKSTGKTLYVLDEPTTGLHSYDVSNLLEVLKR 879
Cdd:PRK00349 799 EFFEAIPKIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELSKRSTGKTLYILDEPTTGLHFEDIRKLLEVLHR 878
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499583918 880 IVNKGDTVIVIEHNLDVIKSVDYIIDLGPGGGTNGGKIVATGTPEQVAEIKESFTGQYLKRMLK 943
Cdd:PRK00349 879 LVDKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVATGTPEEVAKVEASYTGRYLKPVLE 942
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
6-945 0e+00

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


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 1613.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918   6 DTHNFISIKGAKENNLKNIDVVIPKNKLVVFTGLSGSGKSSLAFNTIYEEGRRRYVDSLGSYARQFLGGTKKPDVHSIDG 85
Cdd:COG0178    1 MMMDKIRIRGAREHNLKNIDVDIPRNKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  86 LSPAISIEQKTTHNNPRSTVGTVTEIHDYLRLLYARIGHPFCSNHKIKITSQKLKDILNTVFSYEKDSKILILAPVISGA 165
Cdd:COG0178   81 LSPAISIEQKTTSRNPRSTVGTVTEIYDYLRLLFARVGTPHCPICGRPVEKQTVDQIVDRILALPEGTRLQILAPVVRGR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 166 KGTHQVLLEKLKKD-FLRLKIDGEIYSLDEEINLDKSKKHDIEIVVDRLILNEENRSRIADGIEIALEYSKGLVNVEILG 244
Cdd:COG0178  161 KGEHKELLEELRKQgFVRVRVDGEVYDLDEEPELDKNKKHTIEVVVDRLVVKEDIRSRLADSVETALKLGDGLVIVEVVD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 245 KEKKM-FSQLFSCPYGDFEMPKIETKLFSFNSPYGMCEVCKGIGVSLKSDPDLLIPDKTKSILQGAIIPFQNtvETSNLD 323
Cdd:COG0178  241 EGEELlFSEKFACPDCGISFEELEPRLFSFNSPYGACPTCDGLGRVLEFDPDLVIPDPSLSLAEGAIAPWSG--PSSSYY 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 324 WQEFKALLDYYEISAAKPIEKMTKSELDIIYYGSKEDI--NYTNVSVSGNKYTRFnkiEGILTKMERRFLETTSEQLRTW 401
Cdd:COG0178  319 FQLLEALAKHYGFDLDTPWKDLPEEQRDLILYGSDEKIkfRYKNRGRRRTYEKPF---EGVIPFLERRYRETYSEHVREE 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 402 YLKFMSEIQCSKCKGDRLNDYALAVQIEGLNISDFSKLSIEEGLSKILSLEISSFEKEVSTLIVNEIVNRLTFLSDVGLE 481
Cdd:COG0178  396 LSRYMSETPCPACKGARLKPEALAVKIGGKNIAELTALSIDEALEFFENLELTEREAEIAERILKEIRSRLGFLVDVGLD 475
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 482 YLTLNRTAETLSGGEAQRIRLATQIGSNLTGVLYVLDEPSIGLHQKDNEKLIKTLKHMVEIGNTLIVVEHDDETILEADY 561
Cdd:COG0178  476 YLTLDRSAGTLSGGEAQRIRLATQIGSGLVGVLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDTIRAADY 555
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 562 ILDIGPKAGNEGGQIVAQGSVEDIKKSKESITGKYLSGELKIEIPTFRRSGSGEIIRVIGAKENNLKNIDVKFPIGKFIA 641
Cdd:COG0178  556 IIDIGPGAGEHGGEVVAQGTPEEILKNPDSLTGQYLSGRKRIPVPKKRRKGNGKFLTIKGARENNLKNVDVEIPLGVLTC 635
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 642 VTGVSGSGKSTLVNEVLIKGIEFVK-GSQVHPGKHKEIKGLHNIDKIIQISQSPIGRTPRSNPATYTTVFDDIRDLFANT 720
Cdd:COG0178  636 VTGVSGSGKSTLVNDILYPALARKLnGAKEKPGPHDSIEGLEHIDKVIDIDQSPIGRTPRSNPATYTGVFDPIRELFAQT 715
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 721 EDARASGFLKGRFSFNVNGGRCDKCSGDGYLKIEMHFLPDVYVVCDHCDGKRYNPETLEIKYKFKNISDVLDMTVSEAFD 800
Cdd:COG0178  716 PEAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALE 795
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 801 FFANRAKIREKLETLMDVGLGYIKLGQPATTLSGGEAQRVKLATHLLKKSTGKTLYVLDEPTTGLHSYDVSNLLEVLKRI 880
Cdd:COG0178  796 FFENIPKIARKLQTLQDVGLGYIKLGQPATTLSGGEAQRVKLASELSKRSTGKTLYILDEPTTGLHFHDIRKLLEVLHRL 875
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499583918 881 VNKGDTVIVIEHNLDVIKSVDYIIDLgpgggtnggKIVATGTPEQVAEIKESFTGQYLKRMLKNA 945
Cdd:COG0178  876 VDKGNTVVVIEHNLDVIKTADWIIDLgpeggdgggEIVAEGTPEEVAKVKASYTGRYLKEYLEAA 940
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
10-927 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: 1380.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918   10 FISIKGAKENNLKNIDVVIPKNKLVVFTGLSGSGKSSLAFNTIYEEGRRRYVDSLGSYARQFLGGTKKPDVHSIDGLSPA 89
Cdd:TIGR00630   1 KIIVRGAREHNLKNIDVEIPRDKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGVMDKPDVDSIEGLSPA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918   90 ISIEQKTTHNNPRSTVGTVTEIHDYLRLLYARIGHPFCSNHKIKITSQKLKDILNTVFSYEKDSKILILAPVISGAKGTH 169
Cdd:TIGR00630  81 ISIDQKTTSHNPRSTVGTITEIYDYLRLLFARVGTPYCPTCGRPISRQTPSQIVDQILALPEGTRVILLAPIVRGRKGEF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  170 QVLLEKLKKD-FLRLKIDGEIYSLDEEINLDKSKKHDIEIVVDRLILNEENRSRIADGIEIALEYSKGLVNVEILG---- 244
Cdd:TIGR00630 161 RKLLEKLRKQgFARVRVDGEVYPLEDPPKLEKNKKHTIDVVIDRLTVKNENRSRLAESVETALRLGDGLLEVEFDDdeev 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  245 --KEKKMFSQLFSCPYGDFEMPKIETKLFSFNSPYGMCEVCKGIGVSLKSDPDLLIPDKTKSILQGAIIPFQNtvETSNL 322
Cdd:TIGR00630 241 aeSKEELFSEKFACPECGFSLPELEPRLFSFNSPYGACPECSGLGIKQEFDPELIIPDPLLSLNGGAIVPFKK--STTSY 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  323 DWQEFKALLDYYEISAAKPIEKMTKSELDIIYYGSKEDINYTNVSVSGNKYTRFNK-IEGILTKMERRFLETTSEQLRTW 401
Cdd:TIGR00630 319 YRQMFASLAEHLGFDLDTPWKDLPEEAQKAILYGSGEEVIVVKYRNGGGETFRYHKpFEGVIPELERRYLETESESMREY 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  402 YLKFMSEIQCSKCKGDRLNDYALAVQIEGLNISDFSKLSIEEGLSKILSLEISSFEKEVSTLIVNEIVNRLTFLSDVGLE 481
Cdd:TIGR00630 399 LEKFMSERPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFNQLTLTPEEKKIAEEVLKEIRERLGFLIDVGLD 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  482 YLTLNRTAETLSGGEAQRIRLATQIGSNLTGVLYVLDEPSIGLHQKDNEKLIKTLKHMVEIGNTLIVVEHDDETILEADY 561
Cdd:TIGR00630 479 YLSLSRAAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADY 558
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  562 ILDIGPKAGNEGGQIVAQGSVEDIKKSKESITGKYLSGELKIEIPTFRRSGSGEIIRVIGAKENNLKNIDVKFPIGKFIA 641
Cdd:TIGR00630 559 VIDIGPGAGEHGGEVVASGTPEEILANPDSLTGQYLSGRKKIEVPAERRPGNGKFLTLKGARENNLKNITVSIPLGLFTC 638
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  642 VTGVSGSGKSTLVNEVLIKGIE-FVKGSQVHPGKHKEIKGLHNIDKIIQISQSPIGRTPRSNPATYTTVFDDIRDLFANT 720
Cdd:TIGR00630 639 ITGVSGSGKSTLINDTLYPALAnRLNGAKTVPGRYTSIEGLEHLDKVIHIDQSPIGRTPRSNPATYTGVFDEIRELFAET 718
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  721 EDARASGFLKGRFSFNVNGGRCDKCSGDGYLKIEMHFLPDVYVVCDHCDGKRYNPETLEIKYKFKNISDVLDMTVSEAFD 800
Cdd:TIGR00630 719 PEAKVRGYTPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEAYE 798
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  801 FFANRAKIREKLETLMDVGLGYIKLGQPATTLSGGEAQRVKLATHLLKKSTGKTLYVLDEPTTGLHSYDVSNLLEVLKRI 880
Cdd:TIGR00630 799 FFEAVPSISRKLQTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKRSTGRTLYILDEPTTGLHFDDIKKLLEVLQRL 878
                         890       900       910       920
                  ....*....|....*....|....*....|....*....|....*..
gi 499583918  881 VNKGDTVIVIEHNLDVIKSVDYIIDLGPGGGTNGGKIVATGTPEQVA 927
Cdd:TIGR00630 879 VDKGNTVVVIEHNLDVIKTADYIIDLGPEGGDGGGTVVASGTPEEVA 925
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
11-926 0e+00

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 599.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918   11 ISIKGAKENNLKNIDVVIPKNKLVVFTGLSGSGKSSLAFNTIYEEGRRRYVDSLGSYARQFLGGTKKPDVHSIDGLSPAI 90
Cdd:PRK00635    6 VRLSGITVRNLKNISIEFCPREIVLLTGVSGSGKSSLAFDTIYAAGRKRYLSTLPSFFATTLDSLPDPSVEKIEGLSPTI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918   91 SIEQKTTHNNPRSTVGTVTEIHDYLRLLYARIGHPFCSNHKIKITSQKLKDILNTVFSYEKDSKILILAPVISGAKGTHQ 170
Cdd:PRK00635   86 AVKQNHFSQHSHATVGSTTELNSHLALLFSLEGQARDPVTLHPLTLYSKEKILSTIAAIPDGTQITLLAPLPAKDILAIR 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  171 vllEKLKKDFLRLKIDGEIYSLDEEINLDKSKKHDIEIVVDRLILNEENRSRIADGIEIALEYSKGLVNVEiLGKEKKMF 250
Cdd:PRK00635  166 ---ECLRQGFTKVRIDGEISPIYKFLTSGIPEDVPVDIVVDTLIKNESNTARLKVSLFTALDIGHGECSLH-FDNQKRTF 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  251 SQLFSCPYGDFEMPKIETKLFSFNSPYGMCEVCKGIGVSLKSDpDLLIPDKTKSILQGAIiPFQNTVETSnLDWQEFKAL 330
Cdd:PRK00635  242 STQATIPETQQTYTPLTPQLFSPHSLEDRCPQCQGSGIFISID-DPSLIQQNLSIEENCC-PFAGNCSTY-LYHTIYQSL 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  331 LDYYEISAAKPIEKMTKSELDIIYYGSKEDINYTNV--SVSGNKYTRFNKIEGILTKM--ERRFLETTSEQLRtwylKFM 406
Cdd:PRK00635  319 ADSLGFSLSTPWKDLSPEIQNIFLYGKEGLVLPVRLfdGTLGKKTLTHKVWRGVLNEIgeKVRYSNKPSRYLP----KGT 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  407 SEIQCSKCKGDRLNDYALAVQIEGLNISDFSKLSIEEGLSKILSLEISSfekevstLIVNEIV----NRLTFLSDVGLEY 482
Cdd:PRK00635  395 SATSCPRCQGTGLGDYANAATWHGKTFAEFQQMSLQELFIFLSQLPSKS-------LSIEEVLqglkSRLSILIDLGLPY 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  483 LTLNRTAETLSGGEAQRIRLATQIGSNLTGVLYVLDEPSIGLHQKDNEKLIKTLKHMVEIGNTLIVVEHDDETILEADYI 562
Cdd:PRK00635  468 LTPERALATLSGGEQERTALAKHLGAELIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMISLADRI 547
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  563 LDIGPKAGNEGGQIVAQGSVEDIKKSKESITGKYLSGELKIEIPTfRRSGSGEIIRVIGAKENNLKNIDVKFPIGKFIAV 642
Cdd:PRK00635  548 IDIGPGAGIFGGEVLFNGSPREFLAKSDSLTAKYLRQELTIPIPE-KRTNSLGTLTLSKATKHNLKDLTISLPLGRLTVV 626
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  643 TGVSGSGKSTLVNEVLIKGIE-FVKGSqvhPGKHKEIKGlHNIDKIIQISQSPIGRTPRSNPATYTTVFDDIRDLFANTE 721
Cdd:PRK00635  627 TGVSGSGKSSLINDTLVPAVEeFIEQG---FCSNLSIQW-GAISRLVHITRDLPGRSQRSIPLTYIKAFDDLRELFAEQP 702
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  722 DARASGFLKGRFSFNVNGGRCDKCSGDGYLKIEMHFLPdvyVVCDHCDGKRYNPETLEIKYKFKNISDVLDMTVSEAFDF 801
Cdd:PRK00635  703 RSKRLGLTKSHFSFNTPLGACAECQGLGSITTTDNRTS---IPCPSCLGKRFLPQVLEVRYKGKNIADILEMTAYEAEKF 779
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  802 FANRAKIREKLETLMDVGLGYIKLGQPATTLSGGEAQRVKLATHLLKKSTGKTLYVLDEPTTGLHSYDVSNLLEVLKRIV 881
Cdd:PRK00635  780 FLDEPSIHEKIHALCSLGLDYLPLGRPLSSLSGGEIQRLKLAYELLAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLT 859
                         890       900       910       920
                  ....*....|....*....|....*....|....*....|....*
gi 499583918  882 NKGDTVIVIEHNLDVIKSVDYIIDLGPGGGTNGGKIVATGTPEQV 926
Cdd:PRK00635  860 HQGHTVVIIEHNMHVVKVADYVLELGPEGGNLGGYLLASCSPEEL 904
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
617-923 1.45e-141

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: 422.02  E-value: 1.45e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 617 IRVIGAKENNLKNIDVKFPIGKFIAVTGVSGSGKSTLVNEVLIKGIE-FVKGSQVHPGKHKEIKGLHNIDKIIQISQSPI 695
Cdd:cd03271    1 LTLKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPALArRLHLKKEQPGNHDRIEGLEHIDKVIVIDQSPI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 696 GRTPRSNPATYTTVFDDIRDLFantedarasgflkgrfsfnvnggrcdkcsgdgylkiemhflpdvyvvCDHCDGKRYNP 775
Cdd:cd03271   81 GRTPRSNPATYTGVFDEIRELF-----------------------------------------------CEVCKGKRYNR 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 776 ETLEIKYKFKNISDVLDMTVSEAFDFFANRAKIREKLETLMDVGLGYIKLGQPATTLSGGEAQRVKLATHLLKKSTGKTL 855
Cdd:cd03271  114 ETLEVRYKGKSIADVLDMTVEEALEFFENIPKIARKLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRSTGKTL 193
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499583918 856 YVLDEPTTGLHSYDVSNLLEVLKRIVNKGDTVIVIEHNLDVIKSVDYIIDLGPGGGTNGGKIVATGTP 923
Cdd:cd03271  194 YILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLGPEGGDGGGQVVASGTP 261
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
11-941 8.68e-115

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 387.65  E-value: 8.68e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918   11 ISIKGAKENNLKNIDVVIPKNKLVVFTGLSGSGKSSLAFNTIYEEGRRRYVDSLGSYARQ-FLGGTKKPDVHSIDGLSPA 89
Cdd:PRK00635  941 ITIKNAYQHNLKHIDLSLPRNALTAVTGPSASGKHSLVFDILYAAGNIAYAELFPPYIRQaLIKKTPLPSVDKVTGLSPV 1020
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918   90 ISIEQKTTHNNPRSTVGTVTEIHDYLRLLYARIGHPFC--SNHKI-KITSQKLKDILntvFSYEKDSKILILAPvISGAK 166
Cdd:PRK00635 1021 IAIEKTSASKNSNHSVASALEISNGLEKLFARLGHPYSplSGDALrKITPQTIAEEL---LTHYTKGYVTITSP-IPKEE 1096
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  167 GTHQVLLEKLKKDFLRLKIDGEIYSLDEEI--NLDkskkhDIEIVVDRLILNEENRSRIADGIEIALEYSKGL-VNVEIL 243
Cdd:PRK00635 1097 DLFIYLQEKLKEGFLKLYANEQFYDLDEPLptSLE-----NPAIVIQHTKISEKNLSSLLSSLTLAFSLSSSIcLHIEYA 1171
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  244 GK-EKKMFSQLFSCPYGDfEMPKIETKLFSFNSPYGMCEVCKGIGVSLKSDpdlLIPDKTKsILQGAIIPFqNTVETSNL 322
Cdd:PRK00635 1172 GTsLSLTYRLGWQDSSGN-LYPNITTPLLSRDHEEGLCPLCHGKGFILKCS---LLPHKEK-IAHYTPLSL-FTLFFPNQ 1245
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  323 DWQEFKALLDYYEISAAKPIEKMTKSELDIIYYGSKEdinytnvsvsgnkytrFNKIEGILtkMERRFLETTSEQLRtwy 402
Cdd:PRK00635 1246 DPKPVYPLLKELGIPSIALFQELDTLSFESLCLGTQQ----------------HPGLNALL--MEAMLMESEEPLPP--- 1304
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  403 lKFMSEIQCSKCKGDRLNDYALAVQIEGLNISDfsklsIEEGLSKILSLEISSFEKEVSTLIVNEIVNRLTFLSDVGLEY 482
Cdd:PRK00635 1305 -PLISKTPCNQCQGLGVYTYAHCVRIHNTSLSD-----IYQEDVTFLKKFLLTIHDDEEPSIIQDLLNRLTFIDKVGLSY 1378
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  483 LTLNRTAETLSGGEAQRIRLATQIGSNLTGVLYVLDEPSIGLHQKDNEKLIKTLKHMVEIGNTLIVVEHDDETILEADYI 562
Cdd:PRK00635 1379 ITLGQEQDTLSDGEHYRLHLAKKISSNLTDIIYLLEDPLSGLHPQDAPTLLQLIKELVTNNNTVIATDRSGSLAEHADHL 1458
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  563 LDIGPKAGNEGGQIVAQGSVEDIKKSKESITGKYLSGELKIEIPTfrrsgsgeiirvigakeNNLKNIDVKFPIGKFIAV 642
Cdd:PRK00635 1459 IHLGPGSGPQGGYLLSTSALKQSQPDLHNTRSSEETPTLSVSLSI-----------------HTIQNLNVSAPLHSLVAI 1521
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  643 TGVSGSGKSTLVNEvlikgiEFVKGSQvhpgkhKEI-KGLHNIDKIIQISQSPIGRTPRSNPATYTTVFDDIRDLFANTE 721
Cdd:PRK00635 1522 SGVSGSGKTSLLLE------GFYKQAC------ALIeKGPSVFSEIIFLDSHPQISSQRSDISTYFDIAPSLRNFYASLT 1589
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  722 DARASGFLKGRFSFNVNGGRCDKCSGDGYLKIEMHFLPDVYVVCDHCDGKRYNPETLEIKYKFKNISDVLDMTVSEAFDF 801
Cdd:PRK00635 1590 QAKALNISASMFSTNTKQGQCSDCWGLGYQWIDRAFYALEKRPCPTCSGFRIQPLAQEVVYEGKHFGQLLQTPIEEVAET 1669
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  802 FANRAKIREKLETLMDVGLGYIKLGQPATTLSGGEAQRVKLATHLLKKSTGKTLYVLDEPTTGLHSYDVSNLLEVLKRIV 881
Cdd:PRK00635 1670 FPFLKKIQKPLQALIDNGLGYLPLGQNLSSLSLSEKIAIKIAKFLYLPPKHPTLFLLDEIATSLDNQQKSALLVQLRTLV 1749
                         890       900       910       920       930       940
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  882 NKGDTVIVIEHNLDVIKSVDYIIDLGPGGGTNGGKIVATGTPEQVAEIKESFTGQYLKRM 941
Cdd:PRK00635 1750 SLGHSVIYIDHDPALLKQADYLIEMGPGSGKTGGKILFSGPPKDISASKDSLLKTYMCNL 1809
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
11-123 2.90e-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: 2.90e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  11 ISIKGAKENNLKNIDVVIPKNKLVVFTGLSGSGKSSLAFNTIYEEGRRRYVDSLGSYARQFLGGTKKPDVHSIDGLSPAI 90
Cdd:cd03270    1 IIVRGAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLSPAI 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 499583918  91 SIEQKTTHNNPRSTVGTVTEIHDYLRLLYARIG 123
Cdd:cd03270   81 AIDQKTTSRNPRSTVGTVTEIYDYLRLLFARVG 113
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
468-580 5.52e-64

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: 215.20  E-value: 5.52e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 468 IVNRLTFLSDVGLEYLTLNRTAETLSGGEAQRIRLATQIGSNLTGVLYVLDEPSIGLHQKDNEKLIKTLKHMVEIGNTLI 547
Cdd:cd03270  114 IRERLGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVL 193
                         90       100       110
                 ....*....|....*....|....*....|...
gi 499583918 548 VVEHDDETILEADYILDIGPKAGNEGGQIVAQG 580
Cdd:cd03270  194 VVEHDEDTIRAADHVIDIGPGAGVHGGEIVAQG 226
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
762-938 6.54e-47

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: 181.75  E-value: 6.54e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  762 YVVCDHCDGKRYNPETLEIKYKFKNISDVLDMTVSEAFDFFAN------RAK--------IREKLETLMDVGLGYIKLGQ 827
Cdd:TIGR00630 405 ERPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFNQltltpeEKKiaeevlkeIRERLGFLIDVGLDYLSLSR 484
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  828 PATTLSGGEAQRVKLATHLLKKSTGkTLYVLDEPTTGLHSYDVSNLLEVLKRIVNKGDTVIVIEHNLDVIKSVDYIIDLG 907
Cdd:TIGR00630 485 AAGTLSGGEAQRIRLATQIGSGLTG-VLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVIDIG 563
                         170       180       190
                  ....*....|....*....|....*....|.
gi 499583918  908 PGGGTNGGKIVATGTPEQVAEIKESFTGQYL 938
Cdd:TIGR00630 564 PGAGEHGGEVVASGTPEEILANPDSLTGQYL 594
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
402-581 3.19e-46

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: 166.64  E-value: 3.19e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 402 YLKFMSEIQ---CSKCKGDRLNDYALAVQIEGLNISDFSKLSIEEGLSkilsleisSFEKevstliVNEIVNRLTFLSDV 478
Cdd:cd03271   91 YTGVFDEIRelfCEVCKGKRYNRETLEVRYKGKSIADVLDMTVEEALE--------FFEN------IPKIARKLQTLCDV 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 479 GLEYLTLNRTAETLSGGEAQRIRLATQIGSNLTG-VLYVLDEPSIGLHQKDNEKLIKTLKHMVEIGNTLIVVEHDDETIL 557
Cdd:cd03271  157 GLGYIKLGQPATTLSGGEAQRIKLAKELSKRSTGkTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIK 236
                        170       180
                 ....*....|....*....|....
gi 499583918 558 EADYILDIGPKAGNEGGQIVAQGS 581
Cdd:cd03271  237 CADWIIDLGPEGGDGGGQVVASGT 260
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
617-921 1.68e-45

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


Pssm-ID: 213237 [Multi-domain]  Cd Length: 226  Bit Score: 163.20  E-value: 1.68e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 617 IRVIGAKENNLKNIDVKFPIGKFIAVTGVSGSGKSTLVNEVL--------IKGIEFVKGSQVHPGKHKEIKGLHNIDKII 688
Cdd:cd03270    1 IIVRGAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIyaegqrryVESLSAYARQFLGQMDKPDVDSIEGLSPAI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 689 QISQSPIGRTPRSNPATYTTVFDDIRDLFAntedarasgflkgrfsfnvnggrcdkcsgdgylkiemhflpdvyvvcdhc 768
Cdd:cd03270   81 AIDQKTTSRNPRSTVGTVTEIYDYLRLLFA-------------------------------------------------- 110
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 769 dgkrynpetleikykfknisdvldmtvseafdffanRAKIREKLETLMDVGLGYIKLGQPATTLSGGEAQRVKLATHLLK 848
Cdd:cd03270  111 ------------------------------------RVGIRERLGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIGS 154
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499583918 849 KSTGkTLYVLDEPTTGLHSYDVSNLLEVLKRIVNKGDTVIVIEHNLDVIKSVDYIIDLGPGGGTNGGKIVATG 921
Cdd:cd03270  155 GLTG-VLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDIGPGAGVHGGEIVAQG 226
UvrA_inter pfam17760
UvrA interaction domain; This domain found in UvrA proteins interacts with the UvrB protein.
137-244 1.26e-42

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


Pssm-ID: 436020 [Multi-domain]  Cd Length: 109  Bit Score: 150.71  E-value: 1.26e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  137 QKLKDILNTVFSYEKDSKILILAPVISGAKGTHQVLLEKLKKD-FLRLKIDGEIYSLDEEINLDKSKKHDIEIVVDRLIL 215
Cdd:pfam17760   1 QTVDQIVDRILALPEGTKIQILAPVVRGRKGEHKELLDDLRKQgFVRVRVDGEIYDLDDEPKLDKNKKHTIEVVVDRLVV 80
                          90       100
                  ....*....|....*....|....*....
gi 499583918  216 NEENRSRIADGIEIALEYSKGLVNVEILG 244
Cdd:pfam17760  81 KEDNRSRLADSVETALKLGKGLVIVLVLD 109
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
9-585 4.32e-42

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: 166.73  E-value: 4.32e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918    9 NFISIKGAKENNLKNIDVVIPKNKLVVFTGLSGSGKSSLAFNTIYEegrrryvdslgSYARQFLGGTKKPDVH-SIDG-- 85
Cdd:TIGR00630 612 KFLTLKGARENNLKNITVSIPLGLFTCITGVSGSGKSTLINDTLYP-----------ALANRLNGAKTVPGRYtSIEGle 680
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918   86 -LSPAISIEQKTTHNNPRSTVGTVTEIHDYLRLLYARIghpfcsnhkikitsqklkdilntvfsyeKDSKililapvisg 164
Cdd:TIGR00630 681 hLDKVIHIDQSPIGRTPRSNPATYTGVFDEIRELFAET----------------------------PEAK---------- 722
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  165 akgthqvlleklkkdflrlkidgeiysldeeinldkskkhdieivvdrlilneenrsriadgieiALEYSKGlvnveilg 244
Cdd:TIGR00630 723 -----------------------------------------------------------------VRGYTPG-------- 729
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  245 kekkmfsqlfscpygdfempkietkLFSFNSPYGMCEVCKGIGVslksdpdllipdktksilqgaiipfqntvetsnldw 324
Cdd:TIGR00630 730 -------------------------RFSFNVKGGRCEACQGDGV------------------------------------ 748
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  325 qefkalldyyeisaakpiekmtkseldiiyygskedinytnvsvsgnkytrfnkiegilTKMERRFLETTSeqlrtwylk 404
Cdd:TIGR00630 749 -----------------------------------------------------------IKIEMHFLPDVY--------- 760
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  405 fmseIQCSKCKGDRLNDYALAVQIEGLNISDFSKLSIEEGLskilsleiSSFEKEVStlivneIVNRLTFLSDVGLEYLT 484
Cdd:TIGR00630 761 ----VPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEAY--------EFFEAVPS------ISRKLQTLCDVGLGYIR 822
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  485 LNRTAETLSGGEAQRIRLATQIGSNLTG-VLYVLDEPSIGLHQKDNEKLIKTLKHMVEIGNTLIVVEHDDETILEADYIL 563
Cdd:TIGR00630 823 LGQPATTLSGGEAQRIKLAKELSKRSTGrTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKTADYII 902
                         570       580
                  ....*....|....*....|..
gi 499583918  564 DIGPKAGNEGGQIVAQGSVEDI 585
Cdd:TIGR00630 903 DLGPEGGDGGGTVVASGTPEEV 924
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
469-580 2.90e-40

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


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 146.31  E-value: 2.90e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 469 VNRLTFLSDVGLEYLTLNRTAETLSGGEAQRIRLATQIGSNLTGVLYVLDEPSIGLHQKDNEKLIKTLKHMVEIGNTLIV 548
Cdd:cd03238   65 IDQLQFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVIL 144
                         90       100       110
                 ....*....|....*....|....*....|..
gi 499583918 549 VEHDDETILEADYILDIGPKAGNEGGQIVAQG 580
Cdd:cd03238  145 IEHNLDVLSSADWIIDFGPGSGKSGGKVVFSG 176
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
617-921 9.66e-37

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: 136.30  E-value: 9.66e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 617 IRVIGAKENNLKNIDVKFPIGKFIAVTGVSGSGKSTLVNEVLIKgiefvkgsqvhPGKHKEIKGLhnidkiiqisqspig 696
Cdd:cd03238    1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYA-----------SGKARLISFL--------------- 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 697 rtprSNPATYTTVFDDirdlfantedarasgflkgrfsfnvnggrcdkcsgdgylkiemhflpdvyvvcdhcdgkrynpe 776
Cdd:cd03238   55 ----PKFSRNKLIFID---------------------------------------------------------------- 66
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 777 tleikykfknisdvldmtvseafdffanrakireKLETLMDVGLGYIKLGQPATTLSGGEAQRVKLATHLLKKSTGkTLY 856
Cdd:cd03238   67 ----------------------------------QLQFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPG-TLF 111
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499583918 857 VLDEPTTGLHSYDVSNLLEVLKRIVNKGDTVIVIEHNLDVIKSVDYIIDLGPGGGTNGGKIVATG 921
Cdd:cd03238  112 ILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDFGPGSGKSGGKVVFSG 176
UvrA_DNA-bind pfam17755
UvrA DNA-binding domain;
293-404 8.19e-34

UvrA DNA-binding domain;


Pssm-ID: 465484 [Multi-domain]  Cd Length: 110  Bit Score: 125.66  E-value: 8.19e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  293 DPDLLIPDKTKSILQGAIIPFQNTveTSNLDWQEFKALLDYYEISAAKPIEKMTKSELDIIYYGSKEDINYTNVSVSGNK 372
Cdd:pfam17755   1 DPDLVIPDPSLSLAEGAIAPWGKK--RSSYYFQLLEALAKHYGFDLDTPFKDLPEEQQDIILYGSGEEIIVFYYSRGGRT 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 499583918  373 YTRFNKIEGILTKMERRFLETTSEQLRTWYLK 404
Cdd:pfam17755  79 RTYTKPFEGVIPNLERRYRETDSESVREELEK 110
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
762-942 2.63e-23

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 107.22  E-value: 2.63e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  762 YVVCDHCDGKRYNPETLEIKYKFKNISDVLDMTVSEAFDFFAN----RAKIRE-------KLETLMDVGLGYIKLGQPAT 830
Cdd:PRK00635  396 ATSCPRCQGTGLGDYANAATWHGKTFAEFQQMSLQELFIFLSQlpskSLSIEEvlqglksRLSILIDLGLPYLTPERALA 475
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  831 TLSGGEAQRVKLATHLLKKSTGKTlYVLDEPTTGLHSYDVSNLLEVLKRIVNKGDTVIVIEHNLDVIKSVDYIIDLGPGG 910
Cdd:PRK00635  476 TLSGGEQERTALAKHLGAELIGIT-YILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMISLADRIIDIGPGA 554
                         170       180       190
                  ....*....|....*....|....*....|..
gi 499583918  911 GTNGGKIVATGTPEQVAEIKESFTGQYLKRML 942
Cdd:PRK00635  555 GIFGGEVLFNGSPREFLAKSDSLTAKYLRQEL 586
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
475-926 4.11e-22

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: 101.13  E-value: 4.11e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 475 LSDVGLEYLtLNRTAETLSGGEAQRIRLATQIGSNltGVLYVLDEPSIGL---HQKDNEKLIKTLKHmvEIGNTLIVVEH 551
Cdd:COG1123  127 LEAVGLERR-LDRYPHQLSGGQRQRVAIAMALALD--PDLLIADEPTTALdvtTQAEILDLLRELQR--ERGTTVLLITH 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 552 DDETILE-ADYILDIgpkagnEGGQIVAQGSVEDIKKSKESItGKYLSGELKIEIPTFRRSGSGEIIRV--------IGA 622
Cdd:COG1123  202 DLGVVAEiADRVVVM------DDGRIVEDGPPEEILAAPQAL-AAVPRLGAARGRAAPAAAAAEPLLEVrnlskrypVRG 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 623 KENN--LKNIDVKFPIGKFIAVTGVSGSGKSTLVNevLIKGIE-------FVKGSQVHPGKHKEIKGLHnidKIIQ-ISQ 692
Cdd:COG1123  275 KGGVraVDDVSLTLRRGETLGLVGESGSGKSTLAR--LLLGLLrptsgsiLFDGKDLTKLSRRSLRELR---RRVQmVFQ 349
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 693 SPIGrtprS-NPATytTVFDDIrdlfanTEDARASGFLkgrfsfnvnggrcdkcsgdgylkiemhflpdvyvvcdhcdgk 771
Cdd:COG1123  350 DPYS----SlNPRM--TVGDII------AEPLRLHGLL------------------------------------------ 375
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 772 rynpetleikykfknisdvldmtvseafdffaNRAKIREKLETLMD-VGLGYIKLGQPATTLSGGEAQRVKLATHLlkkS 850
Cdd:COG1123  376 --------------------------------SRAERRERVAELLErVGLPPDLADRYPHELSGGQRQRVAIARAL---A 420
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 851 TGKTLYVLDEPTTGLhsyDVSN---LLEVLKRIVNK-GDTVIVIEHNLDVIKSV-DYIIDLgpgggtNGGKIVATGTPEQ 925
Cdd:COG1123  421 LEPKLLILDEPTSAL---DVSVqaqILNLLRDLQRElGLTYLFISHDLAVVRYIaDRVAVM------YDGRIVEDGPTEE 491

                 .
gi 499583918 926 V 926
Cdd:COG1123  492 V 492
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
11-119 1.82e-16

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: 80.35  E-value: 1.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  11 ISIKGAKENNLKNIDVVIPKNKLVVFTGLSGSGKSSLAFNTIYEegrrryvdslGSYARQFLGGTKKPDVHSIDGL---S 87
Cdd:cd03271    1 LTLKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYP----------ALARRLHLKKEQPGNHDRIEGLehiD 70
                         90       100       110
                 ....*....|....*....|....*....|..
gi 499583918  88 PAISIEQKTTHNNPRSTVGTVTEIHDYLRLLY 119
Cdd:cd03271   71 KVIVIDQSPIGRTPRSNPATYTGVFDEIRELF 102
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
11-72 4.67e-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: 76.98  E-value: 4.67e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499583918  11 ISIKGAKENNLKNIDVVIPKNKLVVFTGLSGSGKSSLAFNTIYEEGRRRYVDSLGSYARQFL 72
Cdd:cd03238    1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKARLISFLPKFSRNKL 62
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
621-904 8.94e-16

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: 77.12  E-value: 8.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 621 GAKENNLKNIDVKFPIGKFIAVTGVSGSGKSTLVNevLIKGIEFVKGSQVH-PGKHKEIKGLHNIDKII----Qisqspi 695
Cdd:cd03225   11 DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLR--LLNGLLGPTSGEVLvDGKDLTKLSLKELRRKVglvfQ------ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 696 grtprsNPAT---YTTVFDDIrdlfantedarASGflkgrfsfnvnggrcdkcsgdgylkiemhflpdvyvvcdhcdgkr 772
Cdd:cd03225   83 ------NPDDqffGPTVEEEV-----------AFG--------------------------------------------- 100
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 773 ynPETLEIKykfknisdvldmtvseafdffanRAKIREKLETLMDVGLGYIKLGQPATTLSGGEAQRVKLATHLlkkSTG 852
Cdd:cd03225  101 --LENLGLP-----------------------EEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVL---AMD 152
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 499583918 853 KTLYVLDEPTTGLHSYDVSNLLEVLKRIVNKGDTVIVIEHNLDVIKSV-DYII 904
Cdd:cd03225  153 PDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELaDRVI 205
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
801-927 3.89e-15

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: 75.94  E-value: 3.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 801 FFANRAKIREKLETLMD-VGLGYiKLGQPATTLSGGEAQRVKLATHLlkkSTGKTLYVLDEPTTGLHSYDVSNLLEVLKR 879
Cdd:cd03219  113 ARREEREARERAEELLErVGLAD-LADRPAGELSYGQQRRLEIARAL---ATDPKLLLLDEPAAGLNPEETEELAELIRE 188
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 499583918 880 IVNKGDTVIVIEHNLDVIKSV-DYIIDLgpgggtNGGKIVATGTPEQVA 927
Cdd:cd03219  189 LRERGITVLLVEHDMDVVMSLaDRVTVL------DQGRVIAEGTPDEVR 231
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
832-906 7.93e-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: 72.66  E-value: 7.93e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499583918 832 LSGGEAQRVKLATHLLKKSTgktLYVLDEPTTGLHSYDVSNLLEVLKRIVNKGDTVIVIEHNLDVI-KSVDYIIDL 906
Cdd:cd00267   81 LSGGQRQRVALARALLLNPD---LLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAeLAADRVIVL 153
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
627-928 1.67e-14

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


Pssm-ID: 444012 [Multi-domain]  Cd Length: 563  Bit Score: 77.49  E-value: 1.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 627 LKNIDVKFPIGKFIAVTGVSGSGKSTLVN-----------EVLIKGIEfvkgsqvhpgkhkeikgLHNID------KIIQ 689
Cdd:COG4988  353 LDGLSLTIPPGERVALVGPSGAGKSTLLNlllgflppysgSILINGVD-----------------LSDLDpaswrrQIAW 415
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 690 ISQSPigrtprsnpatytTVFDD-IRD--LFANTEdarASgflkgrfsfnvnggrcdkcsgdgylkiemhflpdvyvvcd 766
Cdd:COG4988  416 VPQNP-------------YLFAGtIREnlRLGRPD---AS---------------------------------------- 439
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 767 hcdgkrynPETLEikykfknisdvldmtvsEAfdffANRAKIREKLETLMDvGLGYIkLGQPATTLSGGEAQRVKLATHL 846
Cdd:COG4988  440 --------DEELE-----------------AA----LEAAGLDEFVAALPD-GLDTP-LGEGGRGLSGGQAQRLALARAL 488
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 847 LKKStgkTLYVLDEPTTGLhsyDVSN---LLEVLKRIvNKGDTVIVIEHNLDVIKSVDYIIDLgpgggtNGGKIVATGTP 923
Cdd:COG4988  489 LRDA---PLLLLDEPTAHL---DAETeaeILQALRRL-AKGRTVILITHRLALLAQADRILVL------DDGRIVEQGTH 555

                 ....*
gi 499583918 924 EQVAE 928
Cdd:COG4988  556 EELLA 560
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
832-906 4.63e-14

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: 70.85  E-value: 4.63e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499583918 832 LSGGEAQRVKLATHL-LKKSTGKTLYVLDEPTTGLHSYDVSNLLEVLKRIVNKGDTVIVIEHNLDVIKSVDYIIDL 906
Cdd:cd03227   78 LSGGEKELSALALILaLASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHI 153
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
792-928 6.00e-14

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 72.40  E-value: 6.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 792 DMTVSEAFDFFA-----NRAKIREKLETLMD-VGLGyIKLGQPATTLSGGEAQRVKLATHLLKKSTgktLYVLDEPTTGL 865
Cdd:COG1131   87 DLTVRENLRFFArlyglPRKEARERIDELLElFGLT-DAADRKVGTLSGGMKQRLGLALALLHDPE---LLILDEPTSGL 162
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499583918 866 hsyDVS---NLLEVLKRIVNKGDTVIVIEHNLDVIKSV-DY--IIDlgpgggtnGGKIVATGTPEQVAE 928
Cdd:COG1131  163 ---DPEarrELWELLRELAAEGKTVLLSTHYLEEAERLcDRvaIID--------KGRIVADGTPDELKA 220
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
805-926 1.21e-13

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: 71.21  E-value: 1.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 805 RAKIREK-LETLMDVGL-GYikLGQPATTLSGGEAQRVKLATHLlkkSTGKTLYVLDEPTTGLHSYDVSNLLEVLKRIVN 882
Cdd:COG1122  108 REEIRERvEEALELVGLeHL--ADRPPHELSGGQKQRVAIAGVL---AMEPEVLVLDEPTAGLDPRGRRELLELLKRLNK 182
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 499583918 883 KGDTVIVIEHNLD-VIKSVDYIIDLgpgggtNGGKIVATGTPEQV 926
Cdd:COG1122  183 EGKTVIIVTHDLDlVAELADRVIVL------DDGRIVADGTPREV 221
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
478-567 4.61e-13

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


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 67.77  E-value: 4.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 478 VGLEYLTLNRTAETLSGGEAQRIRLATQIGSNLT--GVLYVLDEPSIGLHQKDNEKLIKTLKHMVEIGNTLIVVEHDDET 555
Cdd:cd03227   64 VAAVSAELIFTRLQLSGGEKELSALALILALASLkpRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPEL 143
                         90
                 ....*....|..
gi 499583918 556 ILEADYILDIGP 567
Cdd:cd03227  144 AELADKLIHIKK 155
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
788-906 5.57e-13

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 69.07  E-value: 5.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 788 SDVLDMTVSEAFDF---FANRAKIREKLETLMD-VGLGYIKLGQPATTLSGGEAQRVKLATHLLkksTGKTLYVLDEPTT 863
Cdd:COG4619   83 PALWGGTVRDNLPFpfqLRERKFDRERALELLErLGLPPDILDKPVERLSGGERQRLALIRALL---LQPDVLLLDEPTS 159
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 499583918 864 GLhsyDVSN---LLEVLKRIVNKGD-TVIVIEHNLDVIKSV-DYIIDL 906
Cdd:COG4619  160 AL---DPENtrrVEELLREYLAEEGrAVLWVSHDPEQIERVaDRVLTL 204
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
803-940 1.02e-12

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 68.96  E-value: 1.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 803 ANRAKIREKLETlmdVGLGYIKlGQPATTLSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGLhsyDVSN---LLEVLKR 879
Cdd:COG1121  115 ADREAVDEALER---VGLEDLA-DRPIGELSGGQQQRVLLARALAQDP---DLLLLDEPFAGV---DAATeeaLYELLRE 184
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499583918 880 IVNKGDTVIVIEHNLD-VIKSVDYIIDLgpgggtnGGKIVATGTPEQVaeikesFTGQYLKR 940
Cdd:COG1121  185 LRREGKTILVVTHDLGaVREYFDRVLLL-------NRGLVAHGPPEEV------LTPENLSR 233
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
475-585 2.17e-12

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


Pssm-ID: 440739 [Multi-domain]  Cd Length: 230  Bit Score: 67.74  E-value: 2.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 475 LSDVGLEYLtLNRTAETLSGGEAQRIRLAtqigsnltGVL------YVLDEPSIGLHQKDNEKLIKTLKHMVEIGNTLIV 548
Cdd:COG1122  119 LELVGLEHL-ADRPPHELSGGQKQRVAIA--------GVLamepevLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVII 189
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 499583918 549 VEHDDETILE-ADYILDIgpkagnEGGQIVAQGSVEDI 585
Cdd:COG1122  190 VTHDLDLVAElADRVIVL------DDGRIVADGTPREV 221
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
805-904 4.08e-12

ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 66.40  E-value: 4.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 805 RAKIREKLETlmdVGLGYIKLgQPATTLSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGLhsyDVSN---LLEVLKRIV 881
Cdd:cd03235  110 KAKVDEALER---VGLSELAD-RQIGELSGGQQQRVLLARALVQDP---DLLLLDEPFAGV---DPKTqedIYELLRELR 179
                         90       100
                 ....*....|....*....|....
gi 499583918 882 NKGDTVIVIEHNLD-VIKSVDYII 904
Cdd:cd03235  180 REGMTILVVTHDLGlVLEYFDRVL 203
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
465-563 1.44e-11

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: 64.80  E-value: 1.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 465 VNEIVNRLtfLSDVGLEYLtLNRTAETLSGGEAQRIRLATQIGSNLTgvLYVLDEPSIGLHQKDNEKLIKTLKHMVEIGN 544
Cdd:cd03225  111 IEERVEEA--LELVGLEGL-RDRSPFTLSGGQKQRVAIAGVLAMDPD--ILLLDEPTAGLDPAGRRELLELLKKLKAEGK 185
                         90       100
                 ....*....|....*....|
gi 499583918 545 TLIVVEHDDETILE-ADYIL 563
Cdd:cd03225  186 TIIIVTHDLDLLLElADRVI 205
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
492-565 2.03e-11

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: 63.03  E-value: 2.03e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499583918 492 LSGGEAQRIRLATQIGSNLTgvLYVLDEPSIGLHQKDNEKLIKTLKHMVEIGNTLIVVEHDDETILEA-DYILDI 565
Cdd:cd00267   81 LSGGQRQRVALARALLLNPD--LLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAaDRVIVL 153
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
597-933 4.28e-11

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: 66.78  E-value: 4.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 597 LSGELKIEIPTFRRSGSGEIIrvigakennLKNIDVKFPIGKFIAVTGVSGSGKSTLVN-----------EVLIKGIEfv 665
Cdd:COG2274  470 LKGDIELENVSFRYPGDSPPV---------LDNISLTIKPGERVAIVGRSGSGKSTLLKlllglyeptsgRILIDGID-- 538
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 666 kgsqvhpgkhkeikgLHNIDKII---QISqspigrtprsnpatytTVFDDIRdLFANT-EDarasgflkgrfsfNVNGGR 741
Cdd:COG2274  539 ---------------LRQIDPASlrrQIG----------------VVLQDVF-LFSGTiRE-------------NITLGD 573
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 742 cdkcsgdgylkiemhflPDVyvvcdhcdgkrynpeTLEikykfkNISDVLDMtvSEAFDFFANRAKireKLETLmdvglg 821
Cdd:COG2274  574 -----------------PDA---------------TDE------EIIEAARL--AGLHDFIEALPM---GYDTV------ 604
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 822 yikLGQPATTLSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGLhsyDVSN---LLEVLKRIVnKGDTVIVIEHNLDVIK 898
Cdd:COG2274  605 ---VGEGGSNLSGGQRQRLAIARALLRNP---RILILDEATSAL---DAETeaiILENLRRLL-KGRTVIIIAHRLSTIR 674
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 499583918 899 SVDYIIDLgpgggtNGGKIVATGTPEQVAEIKESF 933
Cdd:COG2274  675 LADRIIVL------DKGRIVEDGTHEELLARKGLY 703
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
805-926 5.87e-11

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: 63.91  E-value: 5.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 805 RAKIREKLETlmdVGLGYIKlGQPATTLSGGEAQRVKLA------THLLkkstgktlyVLDEPTTGLhsyDVSN---LLE 875
Cdd:COG1120  115 REAVEEALER---TGLEHLA-DRPVDELSGGERQRVLIAralaqePPLL---------LLDEPTSHL---DLAHqleVLE 178
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 499583918 876 VLKRIV-NKGDTVIVIEHNLD-VIKSVDYIIDLgpgggtNGGKIVATGTPEQV 926
Cdd:COG1120  179 LLRRLArERGRTVVMVLHDLNlAARYADRLVLL------KDGRIVAQGPPEEV 225
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
806-900 6.33e-11

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: 62.66  E-value: 6.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 806 AKIREKLETLmdvGLGYIKLGQPaTTLSGGEAQRVKLATHLLkksTGKTLYVLDEPTTGLHSYDVSNLLEVLKRIVNKGD 885
Cdd:cd03226  105 EQAETVLKDL---DLYALKERHP-LSLSGGQKQRLAIAAALL---SGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGK 177
                         90
                 ....*....|....*
gi 499583918 886 TVIVIEHNLDVIKSV 900
Cdd:cd03226  178 AVIVITHDYEFLAKV 192
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
607-933 7.40e-11

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


Pssm-ID: 444011 [Multi-domain]  Cd Length: 569  Bit Score: 65.94  E-value: 7.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 607 TFRRSGSGEIIrvigakennLKNIDVKFPIGKFIAVTGVSGSGKSTLVNeVLIKGIEFVKGSqvhpgkhkeikglhnidk 686
Cdd:COG4987  340 SFRYPGAGRPV---------LDGLSLTLPPGERVAIVGPSGSGKSTLLA-LLLRFLDPQSGS------------------ 391
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 687 iIQISQSPIGRTPRSNPATYTTV-------FDD-IRD--LFANtedarasgflkgrfsfnvnggrcdkcsgdgylkiemh 756
Cdd:COG4987  392 -ITLGGVDLRDLDEDDLRRRIAVvpqrphlFDTtLREnlRLAR------------------------------------- 433
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 757 flPDVyvvcdhcdgkryNPETLEikykfknisDVLDmtvseafdffanRAKIREKLETLMDvGLGYIkLGQPATTLSGGE 836
Cdd:COG4987  434 --PDA------------TDEELW---------AALE------------RVGLGDWLAALPD-GLDTW-LGEGGRRLSGGE 476
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 837 AQRVKLATHLLKKStgkTLYVLDEPTTGLhsyDVSNLLEVLKRIVN--KGDTVIVIEHNLDVIKSVDYIIDLgpgggtNG 914
Cdd:COG4987  477 RRRLALARALLRDA---PILLLDEPTEGL---DAATEQALLADLLEalAGRTVLLITHRLAGLERMDRILVL------ED 544
                        330
                 ....*....|....*....
gi 499583918 915 GKIVATGTPEQVAEIKESF 933
Cdd:COG4987  545 GRIVEQGTHEELLAQNGRY 563
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
803-925 8.36e-11

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: 63.02  E-value: 8.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 803 ANRAKIREKLETLMDvglGY-IKLGQPATTLSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGLHSYDVSNLLEVLKRiV 881
Cdd:cd03253  111 AKAAQIHDKIMRFPD---GYdTIVGERGLKLSGGEKQRVAIARAILKNP---PILLLDEATSALDTHTEREIQAALRD-V 183
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 499583918 882 NKGDTVIVIEHNLDVIKSVDYIIDLgpgggtNGGKIVATGTPEQ 925
Cdd:cd03253  184 SKGRTTIVIAHRLSTIVNADKIIVL------KDGRIVERGTHEE 221
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
775-905 1.30e-10

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 65.19  E-value: 1.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 775 PETLEIKYKFKNISDVLDMTVsEAFDFFANRAKI-----------REKLETLMDvglgyiklgQPATTLSGGEAQRVKLA 843
Cdd:COG1245  398 DEDLKISYKPQYISPDYDGTV-EEFLRSANTDDFgssyykteiikPLGLEKLLD---------KNVKDLSGGELQRVAIA 467
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499583918 844 THLLKKStgkTLYVLDEPTTGLhsyDVSNLLEV---LKRIV-NKGDTVIVIEHNLDVIksvDYIID 905
Cdd:COG1245  468 ACLSRDA---DLYLLDEPSAHL---DVEQRLAVakaIRRFAeNRGKTAMVVDHDIYLI---DYISD 524
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
805-895 1.49e-10

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.


Pssm-ID: 213181 [Multi-domain]  Cd Length: 180  Bit Score: 61.30  E-value: 1.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 805 RAKIREKLETLMD-VGLGYIKlGQPATTLSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGLhsyDVSNLLEVLKRIVN- 882
Cdd:cd03214   71 LARKIAYVPQALElLGLAHLA-DRPFNELSGGERQRVLLARALAQEP---PILLLDEPTSHL---DIAHQIELLELLRRl 143
                         90
                 ....*....|....*.
gi 499583918 883 ---KGDTVIVIEHNLD 895
Cdd:cd03214  144 areRGKTVVMVLHDLN 159
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
805-926 2.65e-10

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 63.77  E-value: 2.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 805 RAKIREK-LETLMDVGLGYIkLGQPATTLSGGEAQRVKLATHLlkkSTGKTLYVLDEPTTGLhsyDVSNLLEVLKRI--- 880
Cdd:COG1123  116 RAEARARvLELLEAVGLERR-LDRYPHQLSGGQRQRVAIAMAL---ALDPDLLIADEPTTAL---DVTTQAEILDLLrel 188
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 499583918 881 -VNKGDTVIVIEHNLDVI-KSVDYIIDLgpgggtNGGKIVATGTPEQV 926
Cdd:COG1123  189 qRERGTTVLLITHDLGVVaEIADRVVVM------DDGRIVEDGPPEEI 230
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
777-905 3.56e-10

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 63.67  E-value: 3.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 777 TLEIKYKFKNISDVLDMTVSeafDFFANRAKI------------REKLETLMDvglgyiklgQPATTLSGGEAQRVKLAT 844
Cdd:PRK13409 399 ELKISYKPQYIKPDYDGTVE---DLLRSITDDlgssyykseiikPLQLERLLD---------KNVKDLSGGELQRVAIAA 466
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499583918 845 HLLKKStgkTLYVLDEPTTGLhsyDVSNLLEV---LKRIV-NKGDTVIVIEHNLDVIksvDYIID 905
Cdd:PRK13409 467 CLSRDA---DLYLLDEPSAHL---DVEQRLAVakaIRRIAeEREATALVVDHDIYMI---DYISD 522
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
444-580 4.36e-10

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.


Pssm-ID: 213181 [Multi-domain]  Cd Length: 180  Bit Score: 59.76  E-value: 4.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 444 GLSKILSLEISSFEKEVSTLIVNEIVNRLTF----LSDVGLEYLtLNRTAETLSGGEAQRIRLATQIGSNlTGVLyVLDE 519
Cdd:cd03214   47 GLLKPSSGEILLDGKDLASLSPKELARKIAYvpqaLELLGLAHL-ADRPFNELSGGERQRVLLARALAQE-PPIL-LLDE 123
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499583918 520 PSIGL---HQKDNEKLIKTLKHmvEIGNTLIVVEHD-DETILEADYILDIgpkagnEGGQIVAQG 580
Cdd:cd03214  124 PTSHLdiaHQIELLELLRRLAR--ERGKTVVMVLHDlNLAARYADRVILL------KDGRIVAQG 180
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
787-906 5.20e-10

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 63.26  E-value: 5.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 787 ISDVLDMTVSEAFDFFANRAKIREKLETLmdvGLGYIkLGQPATTLSGGEAQRVKLATHLLKKSTgktLYVLDEPTtglh 866
Cdd:COG1245  172 IPKVFKGTVRELLEKVDERGKLDELAEKL---GLENI-LDRDISELSGGELQRVAIAAALLRDAD---FYFFDEPS---- 240
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 499583918 867 SY-DVS---NLLEVLKRIVNKGDTVIVIEHNLDVIksvDYIIDL 906
Cdd:COG1245  241 SYlDIYqrlNVARLIRELAEEGKYVLVVEHDLAIL---DYLADY 281
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
824-928 5.23e-10

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


Pssm-ID: 213191 [Multi-domain]  Cd Length: 222  Bit Score: 60.53  E-value: 5.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 824 KLGQPATTLSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGLHSYDVSNLLEVLKRIVNKGDTVIVIEHNLDVIKSV-D- 901
Cdd:cd03224  125 RRKQLAGTLSGGEQQMLAIARALMSRP---KLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIaDr 201
                         90       100
                 ....*....|....*....|....*...
gi 499583918 902 -YIIDlgpgggtnGGKIVATGTPEQVAE 928
Cdd:cd03224  202 aYVLE--------RGRVVLEGTAAELLA 221
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
832-906 2.82e-09

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: 57.23  E-value: 2.82e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499583918 832 LSGGEAQRVKLATHLLKKstgKTLYVLDEPTTGLhsyDVSN---LLEVLKRIVNKGDTVIVIEHNLDVIKSVDYIIDL 906
Cdd:cd03246   97 LSGGQRQRLGLARALYGN---PRILVLDEPNSHL---DVEGeraLNQAIAALKAAGATRIVIAHRPETLASADRILVL 168
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
492-584 3.75e-09

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: 60.54  E-value: 3.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 492 LSGGEAQRIRLATQIGSNltGVLYVLDEPSIGLHQkDNEKLIK-TLKHMVEiGNTLIVVEHDDETILEADYILDIgpkag 570
Cdd:COG4988  474 LSGGQAQRLALARALLRD--APLLLLDEPTAHLDA-ETEAEILqALRRLAK-GRTVILITHRLALLAQADRILVL----- 544
                         90
                 ....*....|....
gi 499583918 571 nEGGQIVAQGSVED 584
Cdd:COG4988  545 -DDGRIVEQGTHEE 557
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
792-937 4.60e-09

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


Pssm-ID: 213228 [Multi-domain]  Cd Length: 235  Bit Score: 57.90  E-value: 4.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 792 DMTVSE--AFDFFAN--------RAKIREKLETlmdVGLGYIKLGQPATtLSGGEAQRVKLATHLlkkSTGKTLYVLDEP 861
Cdd:cd03261   91 SLTVFEnvAFPLREHtrlseeeiREIVLEKLEA---VGLRGAEDLYPAE-LSGGMKKRVALARAL---ALDPELLLYDEP 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 862 TTGLH---SYDVSNLLEVLKRivNKGDTVIVIEHNLDVIKSV-DYIIDLGPGggtnggKIVATGTPEQVAEIKESFTGQY 937
Cdd:cd03261  164 TAGLDpiaSGVIDDLIRSLKK--ELGLTSIMVTHDLDTAFAIaDRIAVLYDG------KIVAEGTPEELRASDDPLVRQF 235
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
627-906 4.93e-09

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


Pssm-ID: 213222 [Multi-domain]  Cd Length: 218  Bit Score: 57.50  E-value: 4.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 627 LKNIDVKFPIGKFIAVTGVSGSGKSTLVNevLIKGIEFVKGSQVhpgkhkEIKGlhnidkiiqisqspigrtprsnpaty 706
Cdd:cd03255   20 LKGVSLSIEKGEFVAIVGPSGSGKSTLLN--ILGGLDRPTSGEV------RVDG-------------------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 707 ttvfddiRDLFANTEDARAS------GFLkgrF-SFNVnggrcdkcsgdgylkiemhfLPDVYVvcdhcdgkrynpetLE 779
Cdd:cd03255   66 -------TDISKLSEKELAAfrrrhiGFV---FqSFNL--------------------LPDLTA--------------LE 101
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 780 ikykfkNISdvLDMTVSEAFdffanRAKIREKLETLMD-VGLGYiKLGQPATTLSGGEAQRVKLATHLLKKStgkTLYVL 858
Cdd:cd03255  102 ------NVE--LPLLLAGVP-----KKERRERAEELLErVGLGD-RLNHYPSELSGGQQQRVAIARALANDP---KIILA 164
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 499583918 859 DEPTTGL---HSYDVSNLLEVLKRivNKGDTVIVIEHNLDVIKSVDYIIDL 906
Cdd:cd03255  165 DEPTGNLdseTGKEVMELLRELNK--EAGTTIVVVTHDPELAEYADRIIEL 213
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
803-906 5.13e-09

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


Pssm-ID: 274323 [Multi-domain]  Cd Length: 529  Bit Score: 59.99  E-value: 5.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  803 ANRAKIREKL------ETLMDVGLGY-IKLGQPATTLSGGEAQRVKLATHLLKkstGKTLYVLDEPTTGLhsyDVSNLLE 875
Cdd:TIGR02857 423 ASDAEIREALeragldEFVAALPQGLdTPIGEGGAGLSGGQAQRLALARAFLR---DAPLLLLDEPTAHL---DAETEAE 496
                          90       100       110
                  ....*....|....*....|....*....|...
gi 499583918  876 VLKRI--VNKGDTVIVIEHNLDVIKSVDYIIDL 906
Cdd:TIGR02857 497 VLEALraLAQGRTVLLVTHRLALAALADRIVVL 529
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
832-906 6.15e-09

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


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 56.24  E-value: 6.15e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499583918 832 LSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGLhsyDVSN---LLEVLKRIvNKGDTVIVIEHNLDVIKSVDYIIDL 906
Cdd:cd03228   97 LSGGQRQRIAIARALLRDP---PILILDEATSAL---DPETealILEALRAL-AKGKTVIVIAHRLSTIRDADRIIVL 167
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
627-906 9.57e-09

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 56.98  E-value: 9.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 627 LKNIDVKFPIGKFIAVTGVSGSGKSTLVNevLIKGIEfvkgsqvhpgkhkeikglhnidkiiqisqspigrTPRSnpATY 706
Cdd:COG1136   24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLN--ILGGLD----------------------------------RPTS--GEV 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 707 TtvFDDiRDLFANTEDARAS------GFLkgrF-SFNVnggrcdkcsgdgylkiemhfLPDVYVVcdhcdgkrynpETLE 779
Cdd:COG1136   66 L--IDG-QDISSLSERELARlrrrhiGFV---FqFFNL--------------------LPELTAL-----------ENVA 108
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 780 IKYKFKNISdvldmtvseafdffanRAKIREKLETLMD-VGLGYiKLGQPATTLSGGEAQRVKLATHLLKKSTgktlyVL 858
Cdd:COG1136  109 LPLLLAGVS----------------RKERRERARELLErVGLGD-RLDHRPSQLSGGQQQRVAIARALVNRPK-----LI 166
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 499583918 859 --DEPTTGLHSYDVSNLLEVLKRIV-NKGDTVIVIEHNLDVIKSVDYIIDL 906
Cdd:COG1136  167 laDEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDPELAARADRVIRL 217
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
475-563 1.04e-08

ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 56.39  E-value: 1.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 475 LSDVGLEYLtLNRTAETLSGGEAQRIRLATQIGSNltGVLYVLDEPSIGLHQKDNEKLIKTLKHMVEIGNTLIVVEHDDE 554
Cdd:cd03235  117 LERVGLSEL-ADRQIGELSGGQQQRVLLARALVQD--PDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLG 193
                         90
                 ....*....|
gi 499583918 555 TILE-ADYIL 563
Cdd:cd03235  194 LVLEyFDRVL 203
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
773-905 1.76e-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: 56.26  E-value: 1.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 773 YNPETLEIKYKfkniSDVLDMTVSEAFDFFANRAKIRE-----KLETLMDvglgyiklgQPATTLSGGEAQRVKLATHLL 847
Cdd:cd03237   65 YKPQYIKADYE----GTVRDLLSSITKDFYTHPYFKTEiakplQIEQILD---------REVPELSGGELQRVAIAACLS 131
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 499583918 848 KKStgkTLYVLDEPTTGLHSYDVSNLLEVLKR-IVNKGDTVIVIEHnlDVIKsVDYIID 905
Cdd:cd03237  132 KDA---DIYLLDEPSAYLDVEQRLMASKVIRRfAENNEKTAFVVEH--DIIM-IDYLAD 184
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
793-928 1.89e-08

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 58.13  E-value: 1.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  793 MTVSEAFDFFA-----NRAKIREKL----ETLMDVGLG---YIKLGQPATT--LSGGEAQRVKLATHLLkksTGKTLYVL 858
Cdd:TIGR00955 114 LTVREHLMFQAhlrmpRRVTKKEKRervdEVLQALGLRkcaNTRIGVPGRVkgLSGGERKRLAFASELL---TDPPLLFC 190
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499583918  859 DEPTTGLHSYDVSNLLEVLKRIVNKGDTVIVIEH--NLDVIKSVDYIIDLgpgggtNGGKIVATGTPEQVAE 928
Cdd:TIGR00955 191 DEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHqpSSELFELFDKIILM------AEGRVAYLGSPDQAVP 256
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
436-588 1.91e-08

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: 55.97  E-value: 1.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 436 FSKLSIEEGLSKILsLEISSFEKEVSTLIVNEivnrltFLSDVGLEYLTLNRTAEtLSGGEAQRIRLATQIGSNLTGVLY 515
Cdd:cd03261   89 FDSLTVFENVAFPL-REHTRLSEEEIREIVLE------KLEAVGLRGAEDLYPAE-LSGGMKKRVALARALALDPELLLY 160
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499583918 516 vlDEPSIGL-----HQKDNekLIKTLKHmvEIGNTLIVVEHDDETILE-ADYILDIGpkagneGGQIVAQGSVEDIKKS 588
Cdd:cd03261  161 --DEPTAGLdpiasGVIDD--LIRSLKK--ELGLTSIMVTHDLDTAFAiADRIAVLY------DGKIVAEGTPEELRAS 227
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
824-894 2.28e-08

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 56.00  E-value: 2.28e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499583918 824 KLGQPATTLSGGEAQRVKLATHLLK-----KSTGKtLYVLDEPTTGLhsyDV---SNLLEVLKRIVNKGDTVIVIEHNL 894
Cdd:COG4138  119 KLSRPLTQLSGGEWQRVRLAAVLLQvwptiNPEGQ-LLLLDEPMNSL---DVaqqAALDRLLRELCQQGITVVMSSHDL 193
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
827-926 3.07e-08

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 55.79  E-value: 3.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 827 QPATTLSGGEAQRVKLAThLLKKSTgkTLYVLDEPTTGLhsyDVSN---LLEVLKRIVNKGDTVIVIEHNLD-VIKSVDY 902
Cdd:PRK11231 134 RRLTDLSGGQRQRAFLAM-VLAQDT--PVVLLDEPTTYL---DINHqveLMRLMRELNTQGKTVVTVLHDLNqASRYCDH 207
                         90       100
                 ....*....|....*....|....
gi 499583918 903 IIDLgpgggtNGGKIVATGTPEQV 926
Cdd:PRK11231 208 LVVL------ANGHVMAQGTPEEV 225
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
791-946 3.55e-08

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


Pssm-ID: 440741 [Multi-domain]  Cd Length: 248  Bit Score: 55.58  E-value: 3.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 791 LDMTVSEAF---DFFANRAKIREKLEtlmDVGLGYIKLGQPATTLSGGEAQRVKLATHLLkksTGKTLYVLDEPTTGLhs 867
Cdd:COG1124   98 VDRILAEPLrihGLPDREERIAELLE---QVGLPPSFLDRYPHQLSGGQRQRVAIARALI---LEPELLLLDEPTSAL-- 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 868 yDVS------NLLEVLKRivNKGDTVIVIEHNLDVIKSV-DYIIDLgpgggtNGGKIVATGTpeqVAEIKESFTGQYLKR 940
Cdd:COG1124  170 -DVSvqaeilNLLKDLRE--ERGLTYLFVSHDLAVVAHLcDRVAVM------QNGRIVEELT---VADLLAGPKHPYTRE 237

                 ....*.
gi 499583918 941 MLKNAI 946
Cdd:COG1124  238 LLAASL 243
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
787-906 3.91e-08

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 57.13  E-value: 3.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 787 ISDVLDMTVSEAFDFFANRAKIREKLETLmdvGLGYIkLGQPATTLSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGLh 866
Cdd:PRK13409 172 IPKVFKGKVRELLKKVDERGKLDEVVERL---GLENI-LDRDISELSGGELQRVAIAAALLRDA---DFYFFDEPTSYL- 243
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 499583918 867 syDVSNLLEVLKRI--VNKGDTVIVIEHNLDVIksvDYIIDL 906
Cdd:PRK13409 244 --DIRQRLNVARLIreLAEGKYVLVVEHDLAVL---DYLADN 280
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
465-588 4.41e-08

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 56.78  E-value: 4.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 465 VNEIVNRLTflsdVGLEYLTLNRTAeTLSGGEAQRIRLATQIGSNltGVLYVLDEPSIGLHQKDNEKLIKTLKHMVEiGN 544
Cdd:PRK11174 464 VSEFLPLLP----QGLDTPIGDQAA-GLSVGQAQRLALARALLQP--CQLLLLDEPTASLDAHSEQLVMQALNAASR-RQ 535
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 499583918 545 TLIVVEHDDETILEADYILDIgpkagnEGGQIVAQGSVEDIKKS 588
Cdd:PRK11174 536 TTLMVTHQLEDLAQWDQIWVM------QDGQIVQQGDYAELSQA 573
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
786-928 6.35e-08

ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.


Pssm-ID: 213185 [Multi-domain]  Cd Length: 232  Bit Score: 54.47  E-value: 6.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 786 NISDVLDMtvseafdFFANRAKIREKLETLM-DVGLGYIKLgQPATTLSGGEAQRVKLATHLlkkSTGKTLYVLDEPTTG 864
Cdd:cd03218   95 NILAVLEI-------RGLSKKEREEKLEELLeEFHITHLRK-SKASSLSGGERRRVEIARAL---ATNPKFLLLDEPFAG 163
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499583918 865 LHSYDVSNLLEVLKRIVNKGDTVIVIEHNL-DVIKSVD--YIIdlgpgggtNGGKIVATGTPEQVAE 928
Cdd:cd03218  164 VDPIAVQDIQKIIKILKDRGIGVLITDHNVrETLSITDraYII--------YEGKVLAEGTPEEIAA 222
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
793-900 6.98e-08

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 56.19  E-value: 6.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 793 MTVSE--------AFDFFANRAKIREKLETLMD-VGLGyIKLGQPATTLSGGEAQRVKLAthllkkstgKTLY------V 857
Cdd:COG3845   95 LTVAEnivlglepTKGGRLDRKAARARIRELSErYGLD-VDPDAKVEDLSVGEQQRVEIL---------KALYrgarilI 164
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 499583918 858 LDEPTTGLHSYDVSNLLEVLKRIVNKGDTVIVIEHNLDVIKSV 900
Cdd:COG3845  165 LDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAI 207
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
627-928 9.00e-08

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: 54.11  E-value: 9.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 627 LKNIDVKFPIGKFIAVTGVSGSGKSTL---VNEVLI--KGIEFVKGSQVHPGKHKEIkglhnidkiiqisqspigRTPRS 701
Cdd:cd03256   17 LKDVSLSINPGEFVALIGPSGAGKSTLlrcLNGLVEptSGSVLIDGTDINKLKGKAL------------------RQLRR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 702 NPATyttVFDDIRdlfantedarasgfLKGRFSF--NVNGGRCDKCSgdgylkiemhflpdvyvvcdhcdgkrynpetle 779
Cdd:cd03256   79 QIGM---IFQQFN--------------LIERLSVleNVLSGRLGRRS--------------------------------- 108
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 780 ikykfknisdvldmTVSEAFDFFAnRAKIREKLETLMDVGLGYiKLGQPATTLSGGEAQRVKLATHLLKKStgkTLYVLD 859
Cdd:cd03256  109 --------------TWRSLFGLFP-KEEKQRALAALERVGLLD-KAYQRADQLSGGQQQRVAIARALMQQP---KLILAD 169
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499583918 860 EPTTGLHSYDVSNLLEVLKRI-VNKGDTVIVIEHNLDVIKS-VDYIIDLgpgggtNGGKIVATGTPEQVAE 928
Cdd:cd03256  170 EPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREyADRIVGL------KDGRIVFDGPPAELTD 234
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
474-567 1.21e-07

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 53.28  E-value: 1.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 474 FLSDVGLEYLTLNRTAETLSGGEAQRIRLATQIgSNLTGVLyVLDEPSIGLHQKDNEKLIKTLKHMV-EIGNTLIVVEHD 552
Cdd:COG4619  113 LLERLGLPPDILDKPVERLSGGERQRLALIRAL-LLQPDVL-LLDEPTSALDPENTRRVEELLREYLaEEGRAVLWVSHD 190
                         90
                 ....*....|....*.
gi 499583918 553 DETILE-ADYILDIGP 567
Cdd:COG4619  191 PEQIERvADRVLTLEA 206
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
465-585 1.22e-07

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 53.78  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 465 VNEIVNRLTfLSDvgleylTLNRTAETLSGGEAQRIRLAT---QI--GSNLTGVLYVLDEPSIGLHQKDNEKLIKTLKHM 539
Cdd:PRK03695 107 LNEVAEALG-LDD------KLGRSVNQLSGGEWQRVRLAAvvlQVwpDINPAGQLLLLDEPMNSLDVAQQAALDRLLSEL 179
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 499583918 540 VEIGNTLIVVEHD-DETILEADYILDIgpkagnEGGQIVAQGSVEDI 585
Cdd:PRK03695 180 CQQGIAVVMSSHDlNHTLRHADRVWLL------KQGKLLASGRRDEV 220
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
466-609 1.45e-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: 53.52  E-value: 1.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 466 NEIVNRLtflsdvGLEYLtLNRTAETLSGGEAQRIRLATQIGSNLTgvLYVLDEPSIGLHQKDNEKLIKTLKHMVEIGNT 545
Cdd:cd03236  121 DELVDQL------ELRHV-LDRNIDQLSGGELQRVAIAAALARDAD--FYFFDEPSSYLDIKQRLNAARLIRELAEDDNY 191
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499583918 546 LIVVEHdDETILeaDYILDIGPKAGNEGGqivAQGSVEDIKKSKESITgKYLSGELKIEIPTFR 609
Cdd:cd03236  192 VLVVEH-DLAVL--DYLSDYIHCLYGEPG---AYGVVTLPKSVREGIN-EFLDGYLPTENMRFR 248
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
803-902 1.56e-07

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 53.13  E-value: 1.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 803 ANRAKIREKLETLMD-VGLGYiKLGQPATTLSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGLHSYDVSNLLEVLKRIV 881
Cdd:COG2884  109 KSRKEIRRRVREVLDlVGLSD-KAKALPHELSGGEQQRVAIARALVNRP---ELLLADEPTGNLDPETSWEIMELLEEIN 184
                         90       100
                 ....*....|....*....|.
gi 499583918 882 NKGDTVIVIEHNLDVIKSVDY 902
Cdd:COG2884  185 RRGTTVLIATHDLELVDRMPK 205
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
805-927 1.90e-07

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 54.85  E-value: 1.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 805 RAKIREKLETLMDvGLGYIkLGQPATTLSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGLHSYDVSNLLEVLKRIVNkG 884
Cdd:PRK11174 461 NAWVSEFLPLLPQ-GLDTP-IGDQAAGLSVGQAQRLALARALLQPC---QLLLLDEPTASLDAHSEQLVMQALNAASR-R 534
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 499583918 885 DTVIVIEHNLDVIKSVDYIIDLgpgggtNGGKIVATGTPEQVA 927
Cdd:PRK11174 535 QTTLMVTHQLEDLAQWDQIWVM------QDGQIVQQGDYAELS 571
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
832-904 1.94e-07

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: 52.01  E-value: 1.94e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499583918 832 LSGGEAQRVKLATHLLKKSTgktLYVLDEPTTGLHSYDVSNLLEVLKRIVNKGDTVIVIEHNLDVIKSV-DYII 904
Cdd:cd03230   96 LSGGMKQRLALAQALLHDPE---LLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLcDRVA 166
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
805-894 2.07e-07

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: 54.67  E-value: 2.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  805 RAKIREKLETLMDvGLGyIKLGQPATTLSGGEAQRVKLATHLLkksTGKTLYVLDEPTTGLHSYDVSNLLEVLkRIVNKG 884
Cdd:TIGR02868 447 RVGLADWLRALPD-GLD-TVLGEGGARLSGGERQRLALARALL---ADAPILLLDEPTEHLDAETADELLEDL-LAALSG 520
                          90
                  ....*....|
gi 499583918  885 DTVIVIEHNL 894
Cdd:TIGR02868 521 RTVVLITHHL 530
cbiO PRK13644
energy-coupling factor transporter ATPase;
807-926 2.09e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 53.45  E-value: 2.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 807 KIREKLE-TLMDVGLGYIKLGQPaTTLSGGEAQRVKLATHLlkkSTGKTLYVLDEPTTGLHSYDVSNLLEVLKRIVNKGD 885
Cdd:PRK13644 112 EIRKRVDrALAEIGLEKYRHRSP-KTLSGGQGQCVALAGIL---TMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGK 187
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 499583918 886 TVIVIEHNLDVIKSVDYIIDLgpgggtNGGKIVATGTPEQV 926
Cdd:PRK13644 188 TIVYITHNLEELHDADRIIVM------DRGKIVLEGEPENV 222
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
485-586 2.22e-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: 52.82  E-value: 2.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 485 LNRTAETLSGGEAQriRLAtqIGSNLTG--VLYVLDEPSIGLHQKDNEKLIKTLKHMVEIGNTLIVVEHDDETILE-AD- 560
Cdd:cd03224  126 RKQLAGTLSGGEQQ--MLA--IARALMSrpKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEiADr 201
                         90       100
                 ....*....|....*....|....*..
gi 499583918 561 -YILdigpkagnEGGQIVAQGSVEDIK 586
Cdd:cd03224  202 aYVL--------ERGRVVLEGTAAELL 220
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
832-892 2.42e-07

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


Pssm-ID: 213180 [Multi-domain]  Cd Length: 194  Bit Score: 52.17  E-value: 2.42e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499583918 832 LSGGEAQRVKLATHLLkksTGKTLYVLDEPTTGLHSYDVSNLLEVLKRIVNKGDTVIVIEH 892
Cdd:cd03213  112 LSGGERKRVSIALELV---SNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIH 169
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
792-892 2.93e-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: 52.10  E-value: 2.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 792 DMTVSEAFDFFA---NRAKIREKLETLMD-VGLGYIkLGQPATTLSGGEAQRVKLATHLLKKSTgktLYVLDEPTTGLhs 867
Cdd:COG4133   89 ELTVRENLRFWAalyGLRADREAIDEALEaVGLAGL-ADLPVRQLSAGQKRRVALARLLLSPAP---LWLLDEPFTAL-- 162
                         90       100
                 ....*....|....*....|....*...
gi 499583918 868 yDVSN---LLEVLKRIVNKGDTVIVIEH 892
Cdd:COG4133  163 -DAAGvalLAELIAAHLARGGAVLLTTH 189
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
809-905 2.97e-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: 52.75  E-value: 2.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 809 REKLETLMDV-GLGYIkLGQPATTLSGGEAQRVKLATHLLKKSTgktLYVLDEPTTGLHSYDVSNLLEVLKRIVNKGDTV 887
Cdd:cd03236  117 RGKLDELVDQlELRHV-LDRNIDQLSGGELQRVAIAAALARDAD---FYFFDEPSSYLDIKQRLNAARLIRELAEDDNYV 192
                         90
                 ....*....|....*...
gi 499583918 888 IVIEHNLDVIksvDYIID 905
Cdd:cd03236  193 LVVEHDLAVL---DYLSD 207
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
478-594 3.01e-07

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 52.87  E-value: 3.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 478 VGLEYLTlNRTAETLSGGEAQRIRLATQIGSNLTGVLyvLDEPSIGL---HQKDNEKLIKTLKHmvEIGNTLIVVEHD-D 553
Cdd:PRK10575 135 VGLKPLA-HRLVDSLSGGERQRAWIAMLVAQDSRCLL--LDEPTSALdiaHQVDVLALVHRLSQ--ERGLTVIAVLHDiN 209
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 499583918 554 ETILEADYILDIgpkagnEGGQIVAQGSVEDIKKSK--ESITG 594
Cdd:PRK10575 210 MAARYCDYLVAL------RGGEMIAQGTPAELMRGEtlEQIYG 246
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
832-905 3.17e-07

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


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 51.42  E-value: 3.17e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499583918 832 LSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGLHSYDVSNLLEVLKRIVNKGD-TVIVIEHNLDVIksvDYIID 905
Cdd:cd03222   72 LSGGELQRVAIAAALLRNA---TFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVL---DYLSD 140
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
827-900 3.17e-07

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 53.09  E-value: 3.17e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499583918 827 QPATTLSGGEAQRVKLATHLLKKSTgktLYVLDEPTTGLHSYDVSNLLEVLKRIVNKGDTVIVIEHNLDVIKSV 900
Cdd:PRK13638 132 QPIQCLSHGQKKRVAIAGALVLQAR---YLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEI 202
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
806-904 3.45e-07

ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.


Pssm-ID: 213224 [Multi-domain]  Cd Length: 228  Bit Score: 52.12  E-value: 3.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 806 AKIREKLETLMDVGLGYIKLGQPATTLSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGLhsyDVS---NLLEVLKRIVN 882
Cdd:cd03257  120 ARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNP---KLLIADEPTSAL---DVSvqaQILDLLKKLQE 193
                         90       100
                 ....*....|....*....|....
gi 499583918 883 K-GDTVIVIEHNLDVIKSV-DYII 904
Cdd:cd03257  194 ElGLTLLFITHDLGVVAKIaDRVA 217
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
827-926 3.84e-07

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 53.69  E-value: 3.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 827 QPATTLSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGLHSYDVSNLLEVLKRIVNKGDTVIVIEHNLDV-IKSVDYIID 905
Cdd:PRK09536 135 RPVTSLSGGERQRVLLARALAQAT---PVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLaARYCDELVL 211
                         90       100
                 ....*....|....*....|.
gi 499583918 906 LgpgggtNGGKIVATGTPEQV 926
Cdd:PRK09536 212 L------ADGRVRAAGPPADV 226
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
792-939 4.10e-07

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 52.80  E-value: 4.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 792 DMTVSEAFDFFA-----NRAKIREKLETLMD-VGLGYiKLGQPATTLSGGEAQRVKLATHLLKKSTgktLYVLDEPTTGL 865
Cdd:COG4152   85 KMKVGEQLVYLArlkglSKAEAKRRADEWLErLGLGD-RANKKVEELSKGNQQKVQLIAALLHDPE---LLILDEPFSGL 160
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499583918 866 HSYDVSNLLEVLKRIVNKGDTVIVIEHNLDVIKSV-DYIIDLgpgggtNGGKIVATGTpeqVAEIKESFTGQYLK 939
Cdd:COG4152  161 DPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELcDRIVII------NKGRKVLSGS---VDEIRRQFGRNTLR 226
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
806-906 5.01e-07

ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.


Pssm-ID: 213219 [Multi-domain]  Cd Length: 237  Bit Score: 51.72  E-value: 5.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 806 AKIREKLETLMDVGLGYIK-LGQPATTLSGGEAQRVKLATHLLkksTGKTLYVLDEPTTGLHSYDVSNLLEVLKRIVnKG 884
Cdd:cd03252  112 AKLAGAHDFISELPEGYDTiVGEQGAGLSGGQRQRIAIARALI---HNPRILIFDEATSALDYESEHAIMRNMHDIC-AG 187
                         90       100
                 ....*....|....*....|..
gi 499583918 885 DTVIVIEHNLDVIKSVDYIIDL 906
Cdd:cd03252  188 RTVIIIAHRLSTVKNADRIIVM 209
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
832-900 5.38e-07

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: 50.50  E-value: 5.38e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499583918 832 LSGGEAQRVKLAthllkkstgKTLY------VLDEPTTGLHSYDVSNLLEVLKRIVNKGDTVIVIEHNLDVIKSV 900
Cdd:cd03216   83 LSVGERQMVEIA---------RALArnarllILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEI 148
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
452-580 5.47e-07

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: 50.77  E-value: 5.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 452 EISSFEKEVSTLIvnEIVNRLTFLSDVGLeyltLNRTAETLSGGEAQRIRLATQIGSNLTGVLyvLDEPSIGLHQKDNEK 531
Cdd:cd03247   65 PVSDLEKALSSLI--SVLNQRPYLFDTTL----RNNLGRRFSGGERQRLALARILLQDAPIVL--LDEPTVGLDPITERQ 136
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 499583918 532 LIKTLKHMVEiGNTLIVVEHDDETILEADYILDIgpkagnEGGQIVAQG 580
Cdd:cd03247  137 LLSLIFEVLK-DKTLIWITHHLTGIEHMDKILFL------ENGKIIMQG 178
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
824-894 5.49e-07

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 51.86  E-value: 5.49e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499583918 824 KLGQPATTLSGGEAQRVKLATHLLK-----KSTGKTLyVLDEPTTGLHSYDVSNLLEVLKRIVNKGDTVIVIEHNL 894
Cdd:PRK03695 119 KLGRSVNQLSGGEWQRVRLAAVVLQvwpdiNPAGQLL-LLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDL 193
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
805-900 7.59e-07

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


Pssm-ID: 213225 [Multi-domain]  Cd Length: 233  Bit Score: 51.04  E-value: 7.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 805 RAKIREKLETLMD-VGLGYIKLGQPATtLSGGEAQRVKLATHLlkkSTGKTLYVLDEPTTGLHSYDVSNLLEVLKRIvNK 883
Cdd:cd03258  114 KAEIEERVLELLElVGLEDKADAYPAQ-LSGGQKQRVGIARAL---ANNPKVLLCDEATSALDPETTQSILALLRDI-NR 188
                         90
                 ....*....|....*....
gi 499583918 884 --GDTVIVIEHNLDVIKSV 900
Cdd:cd03258  189 elGLTIVLITHEMEVVKRI 207
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
793-892 7.94e-07

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: 51.12  E-value: 7.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 793 MTVSEAFDFFAN-------RAKIREKL---ETLMDVGLGYIKlGQPATTLSGGEAQRVKLATHLLKKStgKTLyVLDEPT 862
Cdd:cd03234   96 LTVRETLTYTAIlrlprksSDAIRKKRvedVLLRDLALTRIG-GNLVKGISGGERRRVSIAVQLLWDP--KVL-ILDEPT 171
                         90       100       110
                 ....*....|....*....|....*....|
gi 499583918 863 TGLHSYDVSNLLEVLKRIVNKGDTVIVIEH 892
Cdd:cd03234  172 SGLDSFTALNLVSTLSQLARRNRIVILTIH 201
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
466-564 8.68e-07

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: 51.25  E-value: 8.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 466 NEIVNRLtflsdvGLEYLtLNRTAETLSGGEAQRIRLATQIGSNLTgvLYVLDEPSIGLhqkDNEKLI---KTLKHMVEI 542
Cdd:cd03237   97 TEIAKPL------QIEQI-LDREVPELSGGELQRVAIAACLSKDAD--IYLLDEPSAYL---DVEQRLmasKVIRRFAEN 164
                         90       100
                 ....*....|....*....|...
gi 499583918 543 GN-TLIVVEHDdetILEADYILD 564
Cdd:cd03237  165 NEkTAFVVEHD---IIMIDYLAD 184
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
775-895 9.25e-07

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


Pssm-ID: 213264 [Multi-domain]  Cd Length: 214  Bit Score: 50.76  E-value: 9.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 775 PETLEIKYKFKNISDVLDMTVSEAFDF---FANRAKIREKLETLMD-VGLGYIkLGQPATTLSGGEAQRVKLATHLLKKS 850
Cdd:cd03297   72 PQQRKIGLVFQQYALFPHLNVRENLAFglkRKRNREDRISVDELLDlLGLDHL-LNRYPAQLSGGEKQRVALARALAAQP 150
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 499583918 851 tgkTLYVLDEPTTGLHSYDVSNLLEVLKRIV-NKGDTVIVIEHNLD 895
Cdd:cd03297  151 ---ELLLLDEPFSALDRALRLQLLPELKQIKkNLNIPVIFVTHDLS 193
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
492-565 1.01e-06

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


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 49.88  E-value: 1.01e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499583918 492 LSGGEAQRIRLATQIGSNLTgvLYVLDEPSIGLHQKDNEKLIKTLKHMVEIGN-TLIVVEHDdetILEADYILDI 565
Cdd:cd03222   72 LSGGELQRVAIAAALLRNAT--FYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHD---LAVLDYLSDR 141
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
805-906 1.02e-06

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 52.80  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 805 RAKIREKLETLMD-VGLGYIKLGQPATtLSGGEAQRVKLATHLLkksTGKTLYVLDEPTTGLHSYDVSNLLEVLKRIVNK 883
Cdd:PRK10535 118 RKQRLLRAQELLQrLGLEDRVEYQPSQ-LSGGQQQRVSIARALM---NGGQVILADEPTGALDSHSGEEVMAILHQLRDR 193
                         90       100
                 ....*....|....*....|...
gi 499583918 884 GDTVIVIEHNLDVIKSVDYIIDL 906
Cdd:PRK10535 194 GHTVIIVTHDPQVAAQAERVIEI 216
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
433-564 1.04e-06

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 52.48  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 433 ISDFSKLSIEEGLSKILSLEI-SSFEKEvstlivnEIVNRLtflsdvGLEYLtLNRTAETLSGGEAQRIRLATQIGSNLT 511
Cdd:COG1245  410 ISPDYDGTVEEFLRSANTDDFgSSYYKT-------EIIKPL------GLEKL-LDKNVKDLSGGELQRVAIAACLSRDAD 475
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499583918 512 gvLYVLDEPSIGLHQKDNEKLIKTLKHMVEI-GNTLIVVEHDdetILEADYILD 564
Cdd:COG1245  476 --LYLLDEPSAHLDVEQRLAVAKAIRRFAENrGKTAMVVDHD---IYLIDYISD 524
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
478-590 1.07e-06

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: 50.90  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 478 VGLEYLtLNRTAETLSGGEAQRIRLATQIGSNlTGVLyVLDEPSIGLHQKDNEKLIKTLKHMVEIGNTLIVVEHDDETIL 557
Cdd:cd03219  131 VGLADL-ADRPAGELSYGQQRRLEIARALATD-PKLL-LLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVM 207
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 499583918 558 E-ADYI--LDigpkagneGGQIVAQGSVEDIKKSKE 590
Cdd:cd03219  208 SlADRVtvLD--------QGRVIAEGTPDEVRNNPR 235
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
830-926 1.08e-06

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 50.93  E-value: 1.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 830 TTLSGGEAQRVKLA---THLLKKSTGKTLYVLDEPTTGLHSYDVSNLLEVLKRIVNK-GDTVIVIEH--NLDVIKSvDYI 903
Cdd:PRK13548 133 PQLSGGEQQRVQLArvlAQLWEPDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVVLHdlNLAARYA-DRI 211
                         90       100
                 ....*....|....*....|...
gi 499583918 904 IDLgpgggtNGGKIVATGTPEQV 926
Cdd:PRK13548 212 VLL------HQGRLVADGTPAEV 228
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
790-926 1.13e-06

ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];


Pssm-ID: 440736 [Multi-domain]  Cd Length: 250  Bit Score: 50.85  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 790 VLDMTVSEAFDFF--------ANRAKIREKLETLmdvGLGYIKlGQPATTLSGGEAQRVKLATHLLKKstgKTLYVLDEP 861
Cdd:COG1119   97 VLDVVLSGFFDSIglyreptdEQRERARELLELL---GLAHLA-DRPFGTLSQGEQRRVLIARALVKD---PELLILDEP 169
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 862 TTGLhsyDVSN---LLEVLKRIVNKGDTVIV-IEHNL-DVIKSVDYIIDLgpgggtNGGKIVATGTPEQV 926
Cdd:COG1119  170 TAGL---DLGArelLLALLDKLAAEGAPTLVlVTHHVeEIPPGITHVLLL------KDGRVVAAGPKEEV 230
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
627-906 1.19e-06

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


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 50.16  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 627 LKNIDVKFPIGKFIAVTGVSGSGKSTLVNeVLIKGIEFVKGSQVHPGkhkeikglhnidKIIQISQSPIGRTprsnpaty 706
Cdd:cd03250   21 LKDINLEVPKGELVAIVGPVGSGKSSLLS-ALLGELEKLSGSVSVPG------------SIAYVSQEPWIQN-------- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 707 TTVFDDIrdLFantedarasgflkgrfsfnvnggrcdkcsgdgylkiemhflpdvyvvcdhcdGKRYNPEtleiKYKfkn 786
Cdd:cd03250   80 GTIRENI--LF----------------------------------------------------GKPFDEE----RYE--- 98
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 787 isDVLDmtvseafdffanRAKIREKLETLMDVGLGYIklGQPATTLSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGLH 866
Cdd:cd03250   99 --KVIK------------ACALEPDLEILPDGDLTEI--GEKGINLSGGQKQRISLARAVYSDA---DIYLLDDPLSAVD 159
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 499583918 867 SyDVSNLL--EVLKRIVNKGDTVIVIEHNLDVIKSVDYIIDL 906
Cdd:cd03250  160 A-HVGRHIfeNCILGLLLNNKTRILVTHQLQLLPHADQIVVL 200
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
832-904 1.22e-06

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


Pssm-ID: 213214 [Multi-domain]  Cd Length: 178  Bit Score: 49.62  E-value: 1.22e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499583918 832 LSGGEAQRVKLATHLLKKSTgktLYVLDEPTTGLHSYDVSNLLEVLKRiVNKGDTVIVIEHNLDVIKSVDYII 904
Cdd:cd03247   99 FSGGERQRLALARILLQDAP---IVLLDEPTVGLDPITERQLLSLIFE-VLKDKTLIWITHHLTGIEHMDKIL 167
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
477-600 1.54e-06

ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213266 [Multi-domain]  Cd Length: 235  Bit Score: 50.41  E-value: 1.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 477 DVGLEYLtLNRTAETLSGGEAQRIRLATQIGSNLTgvLYVLDEPSIGLHQKDNEKLIKTLKHMV-EIGNTLIVVEHDDET 555
Cdd:cd03299  116 MLGIDHL-LNRKPETLSGGEQQRVAIARALVVNPK--ILLLDEPFSALDVRTKEKLREELKKIRkEFGVTVLHVTHDFEE 192
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 499583918 556 ILE-ADYILDIgpkagnEGGQIVAQGSVEDI-KKSKESITGKYLSGE 600
Cdd:cd03299  193 AWAlADKVAIM------LNGKLIQVGKPEEVfKKPKNEFVAEFLGFN 233
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
815-926 1.79e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 51.00  E-value: 1.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 815 LMDVGLGYIKLGQPATTLSGGEAQRVKLATHLLKKSTgktLYVLDEPTTGLHSYDVSNLLEVLKRIVNKGDTVIVIEHNL 894
Cdd:PRK13631 160 LNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPE---ILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTM 236
                         90       100       110
                 ....*....|....*....|....*....|...
gi 499583918 895 D-VIKSVDYIIDLgpgggtNGGKIVATGTPEQV 926
Cdd:PRK13631 237 EhVLEVADEVIVM------DKGKILKTGTPYEI 263
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
433-564 1.96e-06

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 51.73  E-value: 1.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 433 ISDFSKLSIEEGLSKILSLEISSFEKevstlivNEIVNRLtflsdvGLEYLtLNRTAETLSGGEAQRIRLATQIGSNLTg 512
Cdd:PRK13409 409 IKPDYDGTVEDLLRSITDDLGSSYYK-------SEIIKPL------QLERL-LDKNVKDLSGGELQRVAIAACLSRDAD- 473
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 499583918 513 vLYVLDEPSIGLhqkDNEKLI---KTLKHMVE-IGNTLIVVEHDdetILEADYILD 564
Cdd:PRK13409 474 -LYLLDEPSAHL---DVEQRLavaKAIRRIAEeREATALVVDHD---IYMIDYISD 522
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
793-906 2.05e-06

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


Pssm-ID: 213198 [Multi-domain]  Cd Length: 201  Bit Score: 49.41  E-value: 2.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 793 MTVSEAFDFFANRAKIREKLETLMDVGLGYIKlGQPATTLSGGEAQRVKLATHLLkksTGKTLYVLDEPTTGLHSYDVSN 872
Cdd:cd03231   88 LSVLENLRFWHADHSDEQVEEALARVGLNGFE-DRPVAQLSAGQQRRVALARLLL---SGRPLWILDEPTTALDKAGVAR 163
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 499583918 873 LLEVLKRIVNKGDTVIVIEH-NLDVIKSVDYIIDL 906
Cdd:cd03231  164 FAEAMAGHCARGGMVVLTTHqDLGLSEAGARELDL 198
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
627-863 2.10e-06

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


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 48.41  E-value: 2.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  627 LKNIDVKFPIGKFIAVTGVSGSGKSTLVNevLIKGIEfvkgsqvhpgkhKEIKGlhnidkIIQISQSPIGRTPRSnpaty 706
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLK--LIAGLL------------SPTEG------TILLDGQDLTDDERK----- 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  707 ttvfddirdlfantedarasgFLKGRFsfnvnggrcdkcsgdGYLKIEMHFLPDVYVvcdhcdgkrynpetleikykFKN 786
Cdd:pfam00005  56 ---------------------SLRKEI---------------GYVFQDPQLFPRLTV--------------------REN 79
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499583918  787 ISDVLDMtvsEAFDFFANRAKIREKLETLMDVGLGYIKLGQPATTLSGGEAQRVKLATHLLKKStgkTLYVLDEPTT 863
Cdd:pfam00005  80 LRLGLLL---KGLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKP---KLLLLDEPTA 150
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
486-585 2.18e-06

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 50.01  E-value: 2.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 486 NRTAETLSGGEAQRIRLATQIGSNLTGVLyvLDEPSIGL---HQKDnekLIKTLKHMVEIGNTLIVVEHD-DETILEADY 561
Cdd:PRK11231 133 DRRLTDLSGGQRQRAFLAMVLAQDTPVVL--LDEPTTYLdinHQVE---LMRLMRELNTQGKTVVTVLHDlNQASRYCDH 207
                         90       100
                 ....*....|....*....|....
gi 499583918 562 ILDIgpkagnEGGQIVAQGSVEDI 585
Cdd:PRK11231 208 LVVL------ANGHVMAQGTPEEV 225
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
492-565 2.26e-06

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


Pssm-ID: 274323 [Multi-domain]  Cd Length: 529  Bit Score: 51.52  E-value: 2.26e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499583918  492 LSGGEAQRIRLAtQIGSNLTGVLyVLDEPSIGLHQKDNEKLIKTLKHMVEiGNTLIVVEHDDETILEADYILDI 565
Cdd:TIGR02857 459 LSGGQAQRLALA-RAFLRDAPLL-LLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAALADRIVVL 529
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
491-589 2.64e-06

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: 51.37  E-value: 2.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 491 TLSGGEAQRIRLATqigsnltgVLY------VLDEPSIGLhqkDNE---KLIKTLKHMVEiGNTLIVVEHDDETILEADY 561
Cdd:COG2274  611 NLSGGQRQRLAIAR--------ALLrnprilILDEATSAL---DAEteaIILENLRRLLK-GRTVIIIAHRLSTIRLADR 678
                         90       100
                 ....*....|....*....|....*...
gi 499583918 562 ILDIgpkagnEGGQIVAQGSVEDIKKSK 589
Cdd:COG2274  679 IIVL------DKGRIVEDGTHEELLARK 700
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
832-941 3.16e-06

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 50.01  E-value: 3.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 832 LSGGEAQRVKLATHLLKKSTgktLYVLDEPTTGLHSYDVSNLLEVLKRIVNKGD-TVIVIEHNLDVIKSVDYIIDLGPGg 910
Cdd:PRK13635 141 LSGGQKQRVAIAGVLALQPD---IIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQADRVIVMNKG- 216
                         90       100       110
                 ....*....|....*....|....*....|.
gi 499583918 911 gtnggKIVATGTPEQVAEIkesftGQYLKRM 941
Cdd:PRK13635 217 -----EILEEGTPEEIFKS-----GHMLQEI 237
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
825-925 3.31e-06

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 50.93  E-value: 3.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 825 LGQPATTLSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGLhsyDVSN---LLEVLKRIVnKGDTVIVIEHNLDVIKSVD 901
Cdd:COG1132  470 VGERGVNLSGGQRQRIAIARALLKDP---PILILDEATSAL---DTETealIQEALERLM-KGRTTIVIAHRLSTIRNAD 542
                         90       100
                 ....*....|....*....|....
gi 499583918 902 YIIDLgpgggtNGGKIVATGTPEQ 925
Cdd:COG1132  543 RILVL------DDGRIVEQGTHEE 560
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
805-938 3.66e-06

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: 49.21  E-value: 3.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 805 RAKIREKLETlmdVGL-GYIKLgQPATtLSGGEAQRVKLAthllkkstgKTL-----YVL-DEPTTGLhsyD---VSNLL 874
Cdd:COG1127  119 RELVLEKLEL---VGLpGAADK-MPSE-LSGGMRKRVALA---------RALaldpeILLyDEPTAGL---DpitSAVID 181
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499583918 875 EVLKRIVNK-GDTVIVIEHNLDVIKSV-DYIIDLgpgggtNGGKIVATGTPEQVAEIKESFTGQYL 938
Cdd:COG1127  182 ELIRELRDElGLTSVVVTHDLDSAFAIaDRVAVL------ADGKIIAEGTPEELLASDDPWVRQFL 241
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
826-935 3.94e-06

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 49.60  E-value: 3.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 826 GQPATTLSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGL---HSYDVSNLLEVLKRivNKGDTVIVIEHNLD-VIKSVD 901
Cdd:PRK10253 138 DQSVDTLSGGQRQRAWIAMVLAQET---AIMLLDEPTTWLdisHQIDLLELLSELNR--EKGYTLAAVLHDLNqACRYAS 212
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 499583918 902 YIIDLgpgggtNGGKIVATGTPEQV--AEIKESFTG 935
Cdd:PRK10253 213 HLIAL------REGKIVAQGAPKEIvtAELIERIYG 242
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
803-925 4.03e-06

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


Pssm-ID: 213218 [Multi-domain]  Cd Length: 234  Bit Score: 49.15  E-value: 4.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 803 ANRAKIREKLET------LMDVGLGY-IKLGQPATTLSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGLHS---YDVSN 872
Cdd:cd03251  103 ATREEVEEAARAanahefIMELPEGYdTVIGERGVKLSGGQRQRIAIARALLKDP---PILILDEATSALDTeseRLVQA 179
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 499583918 873 LLEVLKrivnKGDTVIVIEHNLDVIKSVDYIIDLgpgggtNGGKIVATGTPEQ 925
Cdd:cd03251  180 ALERLM----KNRTTFVIAHRLSTIENADRIVVL------EDGKIVERGTHEE 222
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
627-925 4.38e-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: 49.08  E-value: 4.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 627 LKNIDVKFPIGKFIAVTGVSGSGKSTLVN-----------EVLIKGiefvkgsqvhpgkhKEIKGLhNI----DKIIQIS 691
Cdd:cd03249   19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSllerfydptsgEILLDG--------------VDIRDL-NLrwlrSQIGLVS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 692 QSPIgrtprsnpatyttvfddirdLFANTedarasgflkgrFSFNVNGGRcdkcsgdgylkiemhflpdvyvvcdhcdgk 771
Cdd:cd03249   84 QEPV--------------------LFDGT------------IAENIRYGK------------------------------ 101
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 772 ryNPETLEikykfknisdvldmTVSEAfdffANRAKIREKLETLMDvglGY-IKLGQPATTLSGGEAQRVKLATHLLKKS 850
Cdd:cd03249  102 --PDATDE--------------EVEEA----AKKANIHDFIMSLPD---GYdTLVGERGSQLSGGQKQRIAIARALLRNP 158
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499583918 851 TgktLYVLDEPTTGLhsyDVSNLLEVLKRIVN--KGDTVIVIEHNLDVIKSVDYIIDLgpgggtNGGKIVATGTPEQ 925
Cdd:cd03249  159 K---ILLLDEATSAL---DAESEKLVQEALDRamKGRTTIVIAHRLSTIRNADLIAVL------QNGQVVEQGTHDE 223
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
830-926 5.18e-06

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 48.96  E-value: 5.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 830 TTLSGGEAQRVKLATHLL-----KKSTGKTLYvLDEPTTGLhsyDVS---NLLEVLKRIVNKGDTVIVIEH--NL----- 894
Cdd:COG4559  132 QTLSGGEQQRVQLARVLAqlwepVDGGPRWLF-LDEPTSAL---DLAhqhAVLRLARQLARRGGGVVAVLHdlNLaaqya 207
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 499583918 895 D---VIKSvdyiidlgpgggtngGKIVATGTPEQV 926
Cdd:COG4559  208 DrilLLHQ---------------GRLVAQGTPEEV 227
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
832-898 5.58e-06

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 50.09  E-value: 5.58e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499583918 832 LSGGEAQRVKLATHLLkksTGKTLYVLDEPTTGLhsyDVS------NLLEVLKRIVNKGdtVIVIEHNLDVIK 898
Cdd:PRK15134 157 LSGGERQRVMIAMALL---TRPELLIADEPTTAL---DVSvqaqilQLLRELQQELNMG--LLFITHNLSIVR 221
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
813-926 5.63e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 48.92  E-value: 5.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 813 ETLMDVGL-GYIKlgQPATTLSGGEAQRVKLATHLLKKSTgktLYVLDEPTTGLHSYDVSNLLEVLKRIVNKGDTVIVIE 891
Cdd:PRK13639 120 EALKAVGMeGFEN--KPPHHLSGGQKKRVAIAGILAMKPE---IIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIST 194
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 499583918 892 HNLD-VIKSVD--YIIdlgpgggtNGGKIVATGTPEQV 926
Cdd:PRK13639 195 HDVDlVPVYADkvYVM--------SDGKIIKEGTPKEV 224
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
804-900 5.75e-06

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 49.31  E-value: 5.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 804 NRAKIREKLETLMD-VGLG-----YiklgqPATtLSGGEAQRV----KLATH---LLkkstgktlyvLDEPTTGLHSYDV 870
Cdd:COG1135  113 PKAEIRKRVAELLElVGLSdkadaY-----PSQ-LSGGQKQRVgiarALANNpkvLL----------CDEATSALDPETT 176
                         90       100       110
                 ....*....|....*....|....*....|..
gi 499583918 871 SNLLEVLKRIvNK--GDTVIVIEHNLDVIKSV 900
Cdd:COG1135  177 RSILDLLKDI-NRelGLTIVLITHEMDVVRRI 207
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
805-926 5.87e-06

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: 48.97  E-value: 5.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  805 RAKIREKL-ETLMDVGL-GYIKlgQPATTLSGGEAQRVKLATHL-LKKStgktLYVLDEPTTGLHSYDVSNLLEVLKRIV 881
Cdd:TIGR04520 110 REEMRKRVdEALKLVGMeDFRD--REPHLLSGGQKQRVAIAGVLaMRPD----IIILDEATSMLDPKGRKEVLETIRKLN 183
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 499583918  882 N-KGDTVIVIEHNLDVIKSVDYIIDLgpgggtNGGKIVATGTPEQV 926
Cdd:TIGR04520 184 KeEGITVISITHDMEEAVLADRVIVM------NKGKIVAEGTPREI 223
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
832-904 6.69e-06

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: 49.82  E-value: 6.69e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499583918 832 LSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGLHSYDVSNLLEVLKRiVNKGDTVIVIEHNLDVIKSVDYII 904
Cdd:COG5265  495 LSGGEKQRVAIARTLLKNP---PILIFDEATSALDSRTERAIQAALRE-VARGRTTLVIAHRLSTIVDADEIL 563
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
492-576 6.93e-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: 47.21  E-value: 6.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 492 LSGGEAQRIRLATqigsnltgVLY------VLDEPSIGLHQKDNEKLIKTLKHMVEIGNTLIVVEHDDETILEADYILDI 565
Cdd:cd03246   97 LSGGQRQRLGLAR--------ALYgnprilVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVL 168
                         90
                 ....*....|.
gi 499583918 566 gpkagnEGGQI 576
Cdd:cd03246  169 ------EDGRV 173
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
793-900 6.96e-06

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: 48.13  E-value: 6.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 793 MTVSEAFDFFA-----NRAKIREKLETLMDV-GLGYIkLGQPATTLSGGEAQRVKLATHLLKKSTgktLYVLDEPTTGLH 866
Cdd:cd03266   93 LTARENLEYFAglyglKGDELTARLEELADRlGMEEL-LDRRVGGFSTGMRQKVAIARALVHDPP---VLLLDEPTTGLD 168
                         90       100       110
                 ....*....|....*....|....*....|....
gi 499583918 867 SYDVSNLLEVLKRIVNKGDTVIVIEHNLDVIKSV 900
Cdd:cd03266  169 VMATRALREFIRQLRALGKCILFSTHIMQEVERL 202
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
804-943 8.25e-06

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 48.43  E-value: 8.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 804 NRAKIREKLETLMD-VGLGYIKLGQPATTLSGGEAQRVKLATHLlkkSTGKTLYVLDEPTTGLHSYDVSNLLEVLKRIVN 882
Cdd:PRK10619 124 SKQEARERAVKYLAkVGIDERAQGKYPVHLSGGQQQRVSIARAL---AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAE 200
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499583918 883 KGDTVIVIEHNLDVIKSV-DYIIDLgpgggtNGGKIVATGTPEQV-AEIKESFTGQYLKRMLK 943
Cdd:PRK10619 201 EGKTMVVVTHEMGFARHVsSHVIFL------HQGKIEEEGAPEQLfGNPQSPRLQQFLKGSLK 257
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
825-927 8.88e-06

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 48.19  E-value: 8.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 825 LGQPATTLSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGLhsyDVS------NLLEVLKRIVNKGdtVIVIEHNLD-VI 897
Cdd:PRK09544 114 IDAPMQKLSGGETQRVLLARALLNRP---QLLVLDEPTQGV---DVNgqvalyDLIDQLRRELDCA--VLMVSHDLHlVM 185
                         90       100       110
                 ....*....|....*....|....*....|
gi 499583918 898 KSVDYIIDLgpgggtnGGKIVATGTPEQVA 927
Cdd:PRK09544 186 AKTDEVLCL-------NHHICCSGTPEVVS 208
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
828-906 1.02e-05

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


Pssm-ID: 443809 [Multi-domain]  Cd Length: 229  Bit Score: 47.81  E-value: 1.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 828 PATTLSGGEAQRVKLATHLLKKstgKTLYVLDEPTTGLhsyDVSN------LLEVLKRivnKGDTVIVIEHNLDVIKSV- 900
Cdd:COG4778  149 PPATFSGGEQQRVNIARGFIAD---PPLLLLDEPTASL---DAANravvveLIEEAKA---RGTAIIGIFHDEEVREAVa 219

                 ....*.
gi 499583918 901 DYIIDL 906
Cdd:COG4778  220 DRVVDV 225
cbiO PRK13644
energy-coupling factor transporter ATPase;
426-585 1.03e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 48.44  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 426 VQIEGLNISDFSKLsieEGLSKILSL---------------EISSFEKEVSTLIVNEIVNRLTF-LSDVGLEYLTlNRTA 489
Cdd:PRK13644  59 VLVSGIDTGDFSKL---QGIRKLVGIvfqnpetqfvgrtveEDLAFGPENLCLPPIEIRKRVDRaLAEIGLEKYR-HRSP 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 490 ETLSGGEAQRIRLAtqigsnltGVL------YVLDEPSIGLHQKDNEKLIKTLKHMVEIGNTLIVVEHDDETILEADYIL 563
Cdd:PRK13644 135 KTLSGGQGQCVALA--------GILtmepecLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRII 206
                        170       180
                 ....*....|....*....|..
gi 499583918 564 DIgpkagnEGGQIVAQGSVEDI 585
Cdd:PRK13644 207 VM------DRGKIVLEGEPENV 222
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
802-903 1.14e-05

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 48.86  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 802 FANRAKIREKLETLMD-VGLGyIKLGQPATTLSGGEAQRVKLATHLLKKStgKTLyVLDEPTTGLHSYDVSNLLEVLKRI 880
Cdd:COG1129  111 LIDWRAMRRRARELLArLGLD-IDPDTPVGDLSVAQQQLVEIARALSRDA--RVL-ILDEPTASLTEREVERLFRIIRRL 186
                         90       100
                 ....*....|....*....|....
gi 499583918 881 VNKGDTVIVIEHNLDVIKSV-DYI 903
Cdd:COG1129  187 KAQGVAIIYISHRLDEVFEIaDRV 210
cbiO PRK13640
energy-coupling factor transporter ATPase;
794-926 1.17e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 48.26  E-value: 1.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 794 TVSEAFDF-FANRAKIREKLET-----LMDVG-LGYIKlGQPATtLSGGEAQRVKLATHLlkkSTGKTLYVLDEPTTGLH 866
Cdd:PRK13640 101 TVGDDVAFgLENRAVPRPEMIKivrdvLADVGmLDYID-SEPAN-LSGGQKQRVAIAGIL---AVEPKIIILDESTSMLD 175
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499583918 867 SYDVSNLLEVLKRIVNKGD-TVIVIEHNLDVIKSVDYIIDLgpgggtNGGKIVATGTPEQV 926
Cdd:PRK13640 176 PAGKEQILKLIRKLKKKNNlTVISITHDIDEANMADQVLVL------DDGKLLAQGSPVEI 230
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
774-926 1.30e-05

ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213266 [Multi-domain]  Cd Length: 235  Bit Score: 47.72  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 774 NPETLEIKYKFKNISDVLDMTVSEAFDF-----FANRAKIREK-LETLMDVGLGYIkLGQPATTLSGGEAQRVKLATHLL 847
Cdd:cd03299   67 PPEKRDISYVPQNYALFPHMTVYKNIAYglkkrKVDKKEIERKvLEIAEMLGIDHL-LNRKPETLSGGEQQRVAIARALV 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 848 KKStgkTLYVLDEPTTGLHSYDVSNLLEVLKRIVNK-GDTVIVIEHNLDVIKSV-DYIIDLgpgggtNGGKIVATGTPEQ 925
Cdd:cd03299  146 VNP---KILLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALaDKVAIM------LNGKLIQVGKPEE 216

                 .
gi 499583918 926 V 926
Cdd:cd03299  217 V 217
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
832-895 1.40e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 48.16  E-value: 1.40e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499583918 832 LSGGEAQRVKLATHLlkkSTGKTLYVLDEPTTGLHSYDVSNLLEVLKRIVNKGDTVIVIEHNLD 895
Cdd:PRK13651 166 LSGGQKRRVALAGIL---AMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLD 226
cbiO PRK13645
energy-coupling factor transporter ATPase;
803-934 1.45e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 48.08  E-value: 1.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 803 ANRAKIREKLETLMD-VGLGYIKLGQPATTLSGGEAQRVKLAThlLKKSTGKTLyVLDEPTTGLH---SYDVSNLLEVLK 878
Cdd:PRK13645 121 ENKQEAYKKVPELLKlVQLPEDYVKRSPFELSGGQKRRVALAG--IIAMDGNTL-VLDEPTGGLDpkgEEDFINLFERLN 197
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 499583918 879 RivNKGDTVIVIEHNLD-VIKSVDYIIDLgpgggtNGGKIVATGTPEQVAEIKESFT 934
Cdd:PRK13645 198 K--EYKKRIIMVTHNMDqVLRIADEVIVM------HEGKVISIGSPFEIFSNQELLT 246
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
478-585 1.51e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 47.88  E-value: 1.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 478 VGLEYLtLNRTAETLSGGEAQRIRLATQIGsnLTGVLYVLDEPSIGLHQKDNEKLIKTLKHMVE-IGNTLIVVEHDDETI 556
Cdd:PRK13652 125 LGLEEL-RDRVPHHLSGGEKKRVAIAGVIA--MEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtYGMTVIFSTHQLDLV 201
                         90       100       110
                 ....*....|....*....|....*....|
gi 499583918 557 LE-ADYILDIgpkagnEGGQIVAQGSVEDI 585
Cdd:PRK13652 202 PEmADYIYVM------DKGRIVAYGTVEEI 225
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
807-896 1.52e-05

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 47.61  E-value: 1.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 807 KIREK-LETLMDVGLGYIKLGQPATTLSGGEAQRVKLATHLLkksTGKTLYVLDEPTTGLhsyDVS---NLLEVLKRIVN 882
Cdd:PRK11701 126 DIRATaGDWLERVEIDAARIDDLPTTFSGGMQQRLQIARNLV---THPRLVFMDEPTGGL---DVSvqaRLLDLLRGLVR 199
                         90
                 ....*....|....*
gi 499583918 883 K-GDTVIVIEHNLDV 896
Cdd:PRK11701 200 ElGLAVVIVTHDLAV 214
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
489-928 1.61e-05

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: 48.65  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  489 AETLSGGEAQRIRLATQIGSNltGVLYVLDEPSIGLHQKDNEKLIKTLKHMV-EIGNTLIVVEHDDETILE-ADYILDIg 566
Cdd:TIGR03269 166 ARDLSGGEKQRVVLARQLAKE--PFLFLADEPTGTLDPQTAKLVHNALEEAVkASGISMVLTSHWPEVIEDlSDKAIWL- 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  567 pkagnEGGQIVAQG-----------SVEDIKKSKESITGKylsgelkieiptfrrsgsgEIIRVIGAKENN-------LK 628
Cdd:TIGR03269 243 -----ENGEIKEEGtpdevvavfmeGVSEVEKECEVEVGE-------------------PIIKVRNVSKRYisvdrgvVK 298
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  629 NID-VKFPI--GKFIAVTGVSGSGKSTLvnevlikgiefvkgsqvhpgkhkeikglhniDKIIqisqspIGRTPRSNPAT 705
Cdd:TIGR03269 299 AVDnVSLEVkeGEIFGIVGTSGAGKTTL-------------------------------SKII------AGVLEPTSGEV 341
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  706 YTTVFDDIRDLFANTEDARasgflkgrfsfnvngGRCDKCSGdgylkiemhFLPDVYVVCDHcdgkrynpetleikykfk 785
Cdd:TIGR03269 342 NVRVGDEWVDMTKPGPDGR---------------GRAKRYIG---------ILHQEYDLYPH------------------ 379
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  786 niSDVLD-MTVSEAFDFFANRAKiREKLETLMDVGLGYIK----LGQPATTLSGGEAQRVKLATHLLKKStgkTLYVLDE 860
Cdd:TIGR03269 380 --RTVLDnLTEAIGLELPDELAR-MKAVITLKMVGFDEEKaeeiLDKYPDELSEGERHRVALAQVLIKEP---RIVILDE 453
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499583918  861 PTTGLhsyDVSNLLEVLKRIVNK----GDTVIVIEHNLDVIKSVdyiidLGPGGGTNGGKIVATGTPEQVAE 928
Cdd:TIGR03269 454 PTGTM---DPITKVDVTHSILKAreemEQTFIIVSHDMDFVLDV-----CDRAALMRDGKIVKIGDPEEIVE 517
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
832-926 1.88e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 47.49  E-value: 1.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 832 LSGGEAQRVKLATHLlkkSTGKTLYVLDEPTTGLHSYDVSNLLEVLKRIVNK-GDTVIVIEHNLDVIKSV-DYIIDLgpg 909
Cdd:PRK13652 138 LSGGEKKRVAIAGVI---AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMaDYIYVM--- 211
                         90
                 ....*....|....*..
gi 499583918 910 ggtNGGKIVATGTPEQV 926
Cdd:PRK13652 212 ---DKGRIVAYGTVEEI 225
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
803-900 1.96e-05

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


Pssm-ID: 440213 [Multi-domain]  Cd Length: 320  Bit Score: 47.74  E-value: 1.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 803 ANRAKIREKLETLMD-VGLGyiklgQPATT-------LSGGEAQRVKLATHLlkkSTGKTLYVLDEPTTGLhsyDVS--- 871
Cdd:COG0444  119 LSKAEARERAIELLErVGLP-----DPERRldrypheLSGGMRQRVMIARAL---ALEPKLLIADEPTTAL---DVTiqa 187
                         90       100       110
                 ....*....|....*....|....*....|..
gi 499583918 872 ---NLLEVLKRivNKGDTVIVIEHNLDVIKSV 900
Cdd:COG0444  188 qilNLLKDLQR--ELGLAILFITHDLGVVAEI 217
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
832-897 2.04e-05

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


Pssm-ID: 213196 [Multi-domain]  Cd Length: 178  Bit Score: 46.03  E-value: 2.04e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499583918 832 LSGGEAQRVKLATHLLKKstgKTLYVLDEPTTGLHSYDVSNLLEVLKRIV-NKGDTVIVIEHNLDVI 897
Cdd:cd03229  101 LSGGQQQRVALARALAMD---PDVLLLDEPTSALDPITRREVRALLKSLQaQLGITVVLVTHDLDEA 164
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
627-934 2.44e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 47.05  E-value: 2.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 627 LKNIDVKFPIGKFIAVTGVSGSGKSTLVNevLIKGIEFVKGSQvhpgkhkeikglhnidkiIQISQSPIgrtprsNPATY 706
Cdd:PRK13648  25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAK--LMIGIEKVKSGE------------------IFYNNQAI------TDDNF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 707 TTVFDDIRDLFANTEDArasgFLKGRFSFNVNGGrcdkcsgdgylkIEMHFLPdvyvvcdHCDGKRYNPETLEikykfkn 786
Cdd:PRK13648  79 EKLRKHIGIVFQNPDNQ----FVGSIVKYDVAFG------------LENHAVP-------YDEMHRRVSEALK------- 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 787 isDVlDMTvseafdffaNRAKirekletlmdvglgyiklGQPaTTLSGGEAQRVKLATHLlkkSTGKTLYVLDEPTTGLH 866
Cdd:PRK13648 129 --QV-DML---------ERAD------------------YEP-NALSGGQKQRVAIAGVL---ALNPSVIILDEATSMLD 174
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499583918 867 SYDVSNLLEVLKRI-VNKGDTVIVIEHNLDVIKSVDYIIDLgpgggtNGGKIVATGTPEQVAEIKESFT 934
Cdd:PRK13648 175 PDARQNLLDLVRKVkSEHNITIISITHDLSEAMEADHVIVM------NKGTVYKEGTPTEIFDHAEELT 237
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
793-893 2.52e-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: 2.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 793 MTVSEAF---DFFANRAKIREKLETLMDV-GLGYIKLGQPATTLSGGEAQRVKLATHLLKKSTgktLYVLDEPTTGLHSY 868
Cdd:PRK11614  95 MTVEENLamgGFFAERDQFQERIKWVYELfPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPR---LLLLDEPSLGLAPI 171
                         90       100
                 ....*....|....*....|....*
gi 499583918 869 DVSNLLEVLKRIVNKGDTVIVIEHN 893
Cdd:PRK11614 172 IIQQIFDTIEQLREQGMTIFLVEQN 196
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
474-634 2.83e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 47.15  E-value: 2.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 474 FLSDVGLEYLTLNRTAETLSGGEAQRIRLAtqigsnltGVL------YVLDEPSIGLHQKDNEKLIKTLKHMVEIGNTLI 547
Cdd:PRK13631 159 YLNKMGLDDSYLERSPFGLSGGQKRRVAIA--------GILaiqpeiLIFDEPTAGLDPKGEHEMMQLILDAKANNKTVF 230
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 548 VVEHDDETILE-ADYILDIgpkagnEGGQIVAQGSVEDIKKSKESITgkylsgELKIEIPtfrrsgsgEIIRVIgakeNN 626
Cdd:PRK13631 231 VITHTMEHVLEvADEVIVM------DKGKILKTGTPYEIFTDQHIIN------STSIQVP--------RVIQVI----ND 286

                 ....*...
gi 499583918 627 LKNIDVKF 634
Cdd:PRK13631 287 LIKKDPKY 294
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
475-598 3.36e-05

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: 46.62  E-value: 3.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 475 LSDVGLEYLtLNRTAETLSGGEAQRIRLATQIGSN---LtgvlyVLDEPSIGLHQKDNEKLIKTLKHMVEIGN-TLIVVE 550
Cdd:COG1119  127 LELLGLAHL-ADRPFGTLSQGEQRRVLIARALVKDpelL-----ILDEPTAGLDLGARELLLALLDKLAAEGApTLVLVT 200
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 499583918 551 HDDETILEA-DYILDIgpkagnEGGQIVAQGSVEDIkkskesITGKYLS 598
Cdd:COG1119  201 HHVEEIPPGiTHVLLL------KDGRVVAAGPKEEV------LTSENLS 237
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
799-895 3.52e-05

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 46.54  E-value: 3.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 799 FDFFAnRAKIREKLETLMDVGLGYIKlGQPATTLSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGLHSYDVSNLLEVLK 878
Cdd:PRK09984 122 FSWFT-REQKQRALQALTRVGMVHFA-HQRVSTLSGGQQQRVAIARALMQQA---KVILADEPIASLDPESARIVMDTLR 196
                         90
                 ....*....|....*...
gi 499583918 879 RI-VNKGDTVIVIEHNLD 895
Cdd:PRK09984 197 DInQNDGITVVVTLHQVD 214
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
793-893 3.66e-05

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 45.64  E-value: 3.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 793 MTVSEAFDFFAN--RAKIREKLETLMDVGLGYIkLGQPATTLSGGEAQRVKLATHLLkksTGKTLYVLDEPTTGLHSYDV 870
Cdd:PRK13539  88 LTVAENLEFWAAflGGEELDIAAALEAVGLAPL-AHLPFGYLSAGQKRRVALARLLV---SNRPIWILDEPTAALDAAAV 163
                         90       100
                 ....*....|....*....|...
gi 499583918 871 SNLLEVLKRIVNKGDTVIVIEHN 893
Cdd:PRK13539 164 ALFAELIRAHLAQGGIVIAATHI 186
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
805-926 3.67e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 46.55  E-value: 3.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 805 RAKIREKLETlmdVGLGYIKLGQPATTLSGGEAQRVKLATHLlkkSTGKTLYVLDEPTTGLHSYDVSNLLEVLKRI-VNK 883
Cdd:PRK13634 122 KQKAREMIEL---VGLPEELLARSPFELSGGQMRRVAIAGVL---AMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhKEK 195
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 499583918 884 GDTVIVIEHNL-DVIKSVDYIIDLgpgggtNGGKIVATGTPEQV 926
Cdd:PRK13634 196 GLTTVLVTHSMeDAARYADQIVVM------HKGTVFLQGTPREI 233
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
792-892 3.71e-05

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: 45.81  E-value: 3.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  792 DMTVSEAFDFFAN--RAKIREKLETLMDVGL-GYIKLgqPATTLSGGEAQRVKLATHLLkksTGKTLYVLDEPTTGLHSY 868
Cdd:TIGR01189  87 ELSALENLHFWAAihGGAQRTIEDALAAVGLtGFEDL--PAAQLSAGQQRRLALARLWL---SRRPLWILDEPTTALDKA 161
                          90       100
                  ....*....|....*....|....
gi 499583918  869 DVSNLLEVLKRIVNKGDTVIVIEH 892
Cdd:TIGR01189 162 GVALLAGLLRAHLARGGIVLLTTH 185
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
832-906 3.73e-05

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


Pssm-ID: 213188 [Multi-domain]  Cd Length: 144  Bit Score: 44.75  E-value: 3.73e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499583918 832 LSGGEAQRVKLATHLLKKSTgktLYVLDEPTTGLhsyDVSNLLEVLKRIVNKGDTVIVIEHNLDVIKSV-DYIIDL 906
Cdd:cd03221   71 LSGGEKMRLALAKLLLENPN---LLLLDEPTNHL---DLESIEALEEALKEYPGTVILVSHDRYFLDQVaTKIIEL 140
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
825-903 4.00e-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: 47.44  E-value: 4.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 825 LGQPATTLSGGEAQRVKLAthllkkstgKTLY------VLDEPTTGLHSYDVSNLLEVLKRIVNKGDTVIVIEHNLDVIK 898
Cdd:COG4618  461 IGEGGARLSGGQRQRIGLA---------RALYgdprlvVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLA 531

                 ....*
gi 499583918 899 SVDYI 903
Cdd:COG4618  532 AVDKL 536
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
475-585 4.24e-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: 46.14  E-value: 4.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 475 LSDVGLEYLTL-NRTAETLSGGEAQRIRLATQIGSNLTGVLyvLDEPSIGLHQKDNEKLIKTLKHM-VEIGNTLIVVEHD 552
Cdd:cd03295  118 LALVGLDPAEFaDRYPHELSGGQQQRVGVARALAADPPLLL--MDEPFGALDPITRDQLQEEFKRLqQELGKTIVFVTHD 195
                         90       100       110
                 ....*....|....*....|....*....|....
gi 499583918 553 -DETILEADYIldigpkAGNEGGQIVAQGSVEDI 585
Cdd:cd03295  196 iDEAFRLADRI------AIMKNGEIVQVGTPDEI 223
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
810-904 4.24e-05

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 47.13  E-value: 4.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 810 EKL-ETLMDVGLGYIK---------LGQPATTLSGGEAQRVKLATHLLKKstgKTLYVLDEPTTGLHSYDVSNLLEVLkR 879
Cdd:PRK11160 444 EALiEVLQQVGLEKLLeddkglnawLGEGGRQLSGGEQRRLGIARALLHD---APLLLLDEPTEGLDAETERQILELL-A 519
                         90       100
                 ....*....|....*....|....*
gi 499583918 880 IVNKGDTVIVIEHNLDVIKSVDYII 904
Cdd:PRK11160 520 EHAQNKTVLMITHRLTGLEQFDRIC 544
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
805-895 4.25e-05

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


Pssm-ID: 130252 [Multi-domain]  Cd Length: 230  Bit Score: 45.92  E-value: 4.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  805 RAKIREKLETlmdVGLGYIKLGQPaTTLSGGEAQRVKLATHLlkkSTGKTLYVLDEPTTGLHSYDVSNLLEVLKRIVNK- 883
Cdd:TIGR01184  92 RAIVEEHIAL---VGLTEAADKRP-GQLSGGMKQRVAIARAL---SIRPKVLLLDEPFGALDALTRGNLQEELMQIWEEh 164
                          90
                  ....*....|..
gi 499583918  884 GDTVIVIEHNLD 895
Cdd:TIGR01184 165 RVTVLMVTHDVD 176
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
492-563 4.66e-05

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: 44.68  E-value: 4.66e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499583918 492 LSGGEAQRIRLATQIGSNLTgvLYVLDEPSIGLhqkD--NEKLIKTLKHMVEIGNTLIVVEHDDETILEADYIL 563
Cdd:cd03228   97 LSGGQRQRIAIARALLRDPP--ILILDEATSAL---DpeTEALILEALRALAKGKTVIVIAHRLSTIRDADRII 165
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
803-898 6.93e-05

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 45.19  E-value: 6.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 803 ANRAKIREK-LETLMDVGLGYIKLGQPATtLSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGLHSYDVSNLLEVLKRI- 880
Cdd:PRK11629 117 KKPAEINSRaLEMLAAVGLEHRANHRPSE-LSGGERQRVAIARALVNNP---RLVLADEPTGNLDARNADSIFQLLGELn 192
                         90
                 ....*....|....*...
gi 499583918 881 VNKGDTVIVIEHNLDVIK 898
Cdd:PRK11629 193 RLQGTAFLVVTHDLQLAK 210
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
816-904 7.10e-05

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 46.55  E-value: 7.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 816 MDVGLGYIkLGQPATTLSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGLHSYD---VSNLLEVLKrivnKGDTVIVIEH 892
Cdd:PRK11176 466 MDNGLDTV-IGENGVLLSGGQRQRIAIARALLRDS---PILILDEATSALDTESeraIQAALDELQ----KNRTSLVIAH 537
                         90
                 ....*....|..
gi 499583918 893 NLDVIKSVDYII 904
Cdd:PRK11176 538 RLSTIEKADEIL 549
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
825-930 7.23e-05

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


Pssm-ID: 213221 [Multi-domain]  Cd Length: 229  Bit Score: 45.29  E-value: 7.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 825 LGQPATTLSGGEAQRVKLATHLLKKSTgktLYVLDEPTTGLHSYDVSNLLEVLKRIvNKGDTVIVIEHNLDVIKSVDYII 904
Cdd:cd03254  133 LGENGGNLSQGERQLLAIARAMLRDPK---ILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKNADKIL 208
                         90       100
                 ....*....|....*....|....*.
gi 499583918 905 DLGPGggtnggKIVATGTPEQVAEIK 930
Cdd:cd03254  209 VLDDG------KIIEEGTHDELLAKK 228
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
475-584 7.79e-05

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 45.53  E-value: 7.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 475 LSDVGLEYLTlNRTAETLSGGEAQRIRLA---TQI--GSNLTGVLYvLDEPSIGL---HQKDNEKLIKTLKHmvEIGNTL 546
Cdd:PRK13548 119 LAQVDLAHLA-GRDYPQLSGGEQQRVQLArvlAQLwePDGPPRWLL-LDEPTSALdlaHQHHVLRLARQLAH--ERGLAV 194
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 499583918 547 IVVEHD-DETILEADYILDIgpkagnEGGQIVAQGSVED 584
Cdd:PRK13548 195 IVVLHDlNLAARYADRIVLL------HQGRLVADGTPAE 227
cbiO PRK13640
energy-coupling factor transporter ATPase;
468-610 7.87e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 45.56  E-value: 7.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 468 IVNRLtfLSDVG-LEYLtlNRTAETLSGGEAQRIRLAtqigsnltGVLYV------LDEPSIGLHQKDNEKLIKTLKHMV 540
Cdd:PRK13640 123 IVRDV--LADVGmLDYI--DSEPANLSGGQKQRVAIA--------GILAVepkiiiLDESTSMLDPAGKEQILKLIRKLK 190
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499583918 541 EIGN-TLIVVEHDDETILEADYILDIgpkagnEGGQIVAQGSVEDIKKSKESITgkylsgELKIEIPTFRR 610
Cdd:PRK13640 191 KKNNlTVISITHDIDEANMADQVLVL------DDGKLLAQGSPVEIFSKVEMLK------EIGLDIPFVYK 249
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
808-897 8.19e-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: 44.71  E-value: 8.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 808 IREKLETLMD-VGLGYIKLGQPATtLSGGEAQRVKLATHLLKKSTgktLYVLDEPTTGLHSYDVSNLLEVLKRIVNKGDT 886
Cdd:cd03292  113 IRKRVPAALElVGLSHKHRALPAE-LSGGEQQRVAIARAIVNSPT---ILIADEPTGNLDPDTTWEIMNLLKKINKAGTT 188
                         90
                 ....*....|.
gi 499583918 887 VIVIEHNLDVI 897
Cdd:cd03292  189 VVVATHAKELV 199
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
486-569 8.96e-05

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 45.99  E-value: 8.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 486 NRTAETLSGGEAQRIRLATQIGSNlTGVLyVLDEPSIGL---HQKDNEKLIKTLkhmVEIGNTLIVVEHD--------DE 554
Cdd:PRK09536 134 DRPVTSLSGGERQRVLLARALAQA-TPVL-LLDEPTASLdinHQVRTLELVRRL---VDDGKTAVAAIHDldlaarycDE 208
                         90
                 ....*....|....*.
gi 499583918 555 TILEAD-YILDIGPKA 569
Cdd:PRK09536 209 LVLLADgRVRAAGPPA 224
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
478-606 9.51e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 45.37  E-value: 9.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 478 VGLEYLtLNRTAETLSGGEAQRIRLATQIGSNLTGVLYvlDEPSIGLHQKDNEKLIKTLKHMVEIGN-TLIVVEHDDETI 556
Cdd:PRK13632 130 VGMEDY-LDKEPQNLSGGQKQRVAIASVLALNPEIIIF--DESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEA 206
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 499583918 557 LEADYILDIgpkagnEGGQIVAQGSVEDIKKSKESITgkylsgELKIEIP 606
Cdd:PRK13632 207 ILADKVIVF------SEGKLIAQGKPKEILNNKEILE------KAKIDSP 244
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
790-904 9.64e-05

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


Pssm-ID: 213229 [Multi-domain]  Cd Length: 213  Bit Score: 44.44  E-value: 9.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 790 VLDMTVSEAfdffanRAKIREKLEtlmDVGLGYIKLGQPATtLSGGEAQRVKLATHLLKKstgKTLYVLDEPTTGLHSYD 869
Cdd:cd03262  104 VKGMSKAEA------EERALELLE---KVGLADKADAYPAQ-LSGGQQQRVAIARALAMN---PKVMLFDEPTSALDPEL 170
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 499583918 870 VSNLLEVLKRIVNKGDTVIVIEHNLDVIKSV-DYII 904
Cdd:cd03262  171 VGEVLDVMKDLAEEGMTMVVVTHEMGFAREVaDRVI 206
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
831-926 1.05e-04

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 45.16  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 831 TLSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGL---HSYDVSNLLEVLKRivNKGDTVIVIEHNLDV-IKSVDYIIDL 906
Cdd:PRK10575 147 SLSGGERQRAWIAMLVAQDS---RCLLLDEPTSALdiaHQVDVLALVHRLSQ--ERGLTVIAVLHDINMaARYCDYLVAL 221
                         90       100
                 ....*....|....*....|
gi 499583918 907 gpgggtNGGKIVATGTPEQV 926
Cdd:PRK10575 222 ------RGGEMIAQGTPAEL 235
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
465-580 1.16e-04

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


Pssm-ID: 213264 [Multi-domain]  Cd Length: 214  Bit Score: 44.59  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 465 VNEIVNRLtflsdvGLEYLtLNRTAETLSGGEAQRIRLATQIGSNLTgvLYVLDEPSIGLHQKDNEKLIKTLKHMVEIGN 544
Cdd:cd03297  112 VDELLDLL------GLDHL-LNRYPAQLSGGEKQRVALARALAAQPE--LLLLDEPFSALDRALRLQLLPELKQIKKNLN 182
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 499583918 545 -TLIVVEHD-DETILEADYILDIgpkagnEGGQIVAQG 580
Cdd:cd03297  183 iPVIFVTHDlSEAEYLADRIVVM------EDGRLQYIG 214
PLN03211 PLN03211
ABC transporter G-25; Provisional
832-892 1.16e-04

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 46.03  E-value: 1.16e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499583918 832 LSGGEAQRVKLATHLLkksTGKTLYVLDEPTTGLHSYDVSNLLEVLKRIVNKGDTVIVIEH 892
Cdd:PLN03211 207 ISGGERKRVSIAHEML---INPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
813-900 1.24e-04

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 45.69  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 813 ETLMDVGLGyIKLGQPATTLSGGEAQRVKLATHLLKKSTgktLYVLDEPTTGLHSYDVSNLLEVLKRIVNKGDTVIVIEH 892
Cdd:PRK13549 126 KLLAQLKLD-INPATPVGNLGLGQQQLVEIAKALNKQAR---LLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISH 201

                 ....*...
gi 499583918 893 NLDVIKSV 900
Cdd:PRK13549 202 KLNEVKAI 209
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
492-578 1.28e-04

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 45.87  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 492 LSGGEAQRIRLATQIGSNltGVLYVLDEPSIGLHQKDNEKLIKTLKHMVEIGNTLIVVEHDDETILEADYILDIgpkagn 571
Cdd:PRK10535 145 LSGGQQQRVSIARALMNG--GQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEI------ 216

                 ....*..
gi 499583918 572 EGGQIVA 578
Cdd:PRK10535 217 RDGEIVR 223
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
491-588 1.28e-04

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: 45.89  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 491 TLSGGEAQRIRLATQigsnLTG--VLYVLDEPSIGLhqkDNE---KLIKTLKHMVEIGNTLIVVEHDDETILEADYILDI 565
Cdd:COG4618  467 RLSGGQRQRIGLARA----LYGdpRLVVLDEPNSNL---DDEgeaALAAAIRALKARGATVVVITHRPSLLAAVDKLLVL 539
                         90       100
                 ....*....|....*....|...
gi 499583918 566 gpkagnEGGQIVAQGSVEDIKKS 588
Cdd:COG4618  540 ------RDGRVQAFGPRDEVLAR 556
cbiO PRK13641
energy-coupling factor transporter ATPase;
472-598 1.34e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 44.82  E-value: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 472 LTFLSDVGLEYLTLNRTAETLSGGEAQRIRLAtqigsnltGVL------YVLDEPSIGLHQKDNEKLIKTLKHMVEIGNT 545
Cdd:PRK13641 126 LKWLKKVGLSEDLISKSPFELSGGQMRRVAIA--------GVMayepeiLCLDEPAAGLDPEGRKEMMQLFKDYQKAGHT 197
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499583918 546 LIVVEHDDETILE-ADYILDIgpkagnEGGQIVAQGSVEDIKKSKESITGKYLS 598
Cdd:PRK13641 198 VILVTHNMDDVAEyADDVLVL------EHGKLIKHASPKEIFSDKEWLKKHYLD 245
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
474-558 1.44e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 45.08  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 474 FLSDVGLEYLTLNRTAETLSGGEAQRIRLAtqigsnltGVL------YVLDEPSIGLHQKDNEKLIKTLKHMVEIGNTLI 547
Cdd:PRK13651 148 YIELVGLDESYLQRSPFELSGGQKRRVALA--------GILamepdfLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTII 219
                         90
                 ....*....|.
gi 499583918 548 VVEHDDETILE 558
Cdd:PRK13651 220 LVTHDLDNVLE 230
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
492-599 1.63e-04

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 44.37  E-value: 1.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 492 LSGGEAQRIRLATQIGsnLTGVLYVLDEPSIGlhqKDN------EKLIKTLKHmvEIGNTLIVVEHDDETILE-ADYILD 564
Cdd:PRK11831 144 LSGGMARRAALARAIA--LEPDLIMFDEPFVG---QDPitmgvlVKLISELNS--ALGVTCVVVSHDVPEVLSiADHAYI 216
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 499583918 565 IGPKagneggQIVAQGSVEDIKKSKESITGKYLSG 599
Cdd:PRK11831 217 VADK------KIVAHGSAQALQANPDPRVRQFLDG 245
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
478-580 1.64e-04

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


Pssm-ID: 213226 [Multi-domain]  Cd Length: 213  Bit Score: 44.05  E-value: 1.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 478 VGLEYLtLNRTAETLSGGEAQRI---R-LATQIGsnltgvLYVLDEPSIGLHQKDNEKLIKTLKHM-VEIGNTLIVVEHD 552
Cdd:cd03259  118 VGLEGL-LNRYPHELSGGQQQRValaRaLAREPS------LLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHD 190
                         90       100
                 ....*....|....*....|....*....
gi 499583918 553 DETILE-ADYILDIgpkagnEGGQIVAQG 580
Cdd:cd03259  191 QEEALAlADRIAVM------NEGRIVQVG 213
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
472-552 1.68e-04

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 44.04  E-value: 1.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 472 LTFLSDVGLEYLTLNRTAEtLSGGEAQRIRLATQIGSNLTGVLyvLDEPSIGLHQKDNEKLIKTLKHM-VEIGNTLIVVE 550
Cdd:PRK11629 127 LEMLAAVGLEHRANHRPSE-LSGGERQRVAIARALVNNPRLVL--ADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVT 203

                 ..
gi 499583918 551 HD 552
Cdd:PRK11629 204 HD 205
cbiO PRK13643
energy-coupling factor transporter ATPase;
810-926 1.75e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 44.72  E-value: 1.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 810 EKLETlmdVGLGYIKLGQPATTLSGGEAQRVKLATHLlkkSTGKTLYVLDEPTTGLHSYDVSNLLEVLKRIVNKGDTVIV 889
Cdd:PRK13643 126 EKLEM---VGLADEFWEKSPFELSGGQMRRVAIAGIL---AMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVL 199
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 499583918 890 IEHNL-DVIKSVDYIIDLgpgggtNGGKIVATGTPEQV 926
Cdd:PRK13643 200 VTHLMdDVADYADYVYLL------EKGHIISCGTPSDV 231
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
627-663 1.77e-04

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 44.28  E-value: 1.77e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 499583918 627 LKNIDVKFPIGKFIAVTGVSGSGKSTLVNevLIKGIE 663
Cdd:PRK11247  28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLR--LLAGLE 62
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
475-565 1.86e-04

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


Pssm-ID: 213222 [Multi-domain]  Cd Length: 218  Bit Score: 43.63  E-value: 1.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 475 LSDVGLEYLtLNRTAETLSGGEAQRIRLATQIGSNLTGVLyvLDEPSIGLHQKDNEKLIKTLKHMV-EIGNTLIVVEHDD 553
Cdd:cd03255  125 LERVGLGDR-LNHYPSELSGGQQQRVAIARALANDPKIIL--ADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDP 201
                         90
                 ....*....|..
gi 499583918 554 ETILEADYILDI 565
Cdd:cd03255  202 ELAEYADRIIEL 213
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
478-598 2.08e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 44.24  E-value: 2.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 478 VGLEYLTLNRTAETLSGGEAQRIRLAtqigsnltGVL------YVLDEPSIGLH---QKDNEKLIKTLKHmvEIGNTLIV 548
Cdd:PRK13634 132 VGLPEELLARSPFELSGGQMRRVAIA--------GVLamepevLVLDEPTAGLDpkgRKEMMEMFYKLHK--EKGLTTVL 201
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 499583918 549 VEHD-DETILEADYILDIgpkagnEGGQIVAQGSVEDIKKSKESITGKYLS 598
Cdd:PRK13634 202 VTHSmEDAARYADQIVVM------HKGTVFLQGTPREIFADPDELEAIGLD 246
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
21-47 2.48e-04

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


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 43.23  E-value: 2.48e-04
                         10        20
                 ....*....|....*....|....*..
gi 499583918  21 LKNIDVVIPKNKLVVFTGLSGSGKSSL 47
Cdd:cd03250   21 LKDINLEVPKGELVAIVGPVGSGKSSL 47
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
801-897 2.51e-04

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 44.66  E-value: 2.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 801 FFANRAKIREKLEtlmdvglGY-----IKLG---QPATTLSGGEAQRVKLATHLlkkSTGKTLYVLDEPTTGLhsyDVS- 871
Cdd:PRK15439 372 FWIKPARENAVLE-------RYrralnIKFNhaeQAARTLSGGNQQKVLIAKCL---EASPQLLIVDEPTRGV---DVSa 438
                         90       100
                 ....*....|....*....|....*...
gi 499583918 872 --NLLEVLKRIVNKGDTVIVIEHNLDVI 897
Cdd:PRK15439 439 rnDIYQLIRSIAAQNVAVLFISSDLEEI 466
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
805-900 2.64e-04

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 44.41  E-value: 2.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 805 RAKIREKLETLMD-VGLGYIKLGQPATtLSGGEAQRVKLATHLlkkSTGKTLYVLDEPTTGLHSYDVSNLLEVLKRIvNK 883
Cdd:PRK11153 114 KAEIKARVTELLElVGLSDKADRYPAQ-LSGGQKQRVAIARAL---ASNPKVLLCDEATSALDPATTRSILELLKDI-NR 188
                         90
                 ....*....|....*....
gi 499583918 884 --GDTVIVIEHNLDVIKSV 900
Cdd:PRK11153 189 elGLTIVLITHEMDVVKRI 207
cbiO PRK13643
energy-coupling factor transporter ATPase;
475-585 2.87e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 43.95  E-value: 2.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 475 LSDVGLEYLTLNRTAETLSGGEAQRIRLATQIGsnLTGVLYVLDEPSIGLHQKDNEKLIKTLKHMVEIGNTLIVVEH-DD 553
Cdd:PRK13643 128 LEMVGLADEFWEKSPFELSGGQMRRVAIAGILA--MEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHlMD 205
                         90       100       110
                 ....*....|....*....|....*....|..
gi 499583918 554 ETILEADYILDIgpkagnEGGQIVAQGSVEDI 585
Cdd:PRK13643 206 DVADYADYVYLL------EKGHIISCGTPSDV 231
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
485-590 2.88e-04

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 43.85  E-value: 2.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 485 LNRTAETLSGGEAQRIRLAtqigsnltGVL------YVLDEPSIGLHQKDNEKLIKTLKHMVEIGN-TLIVVEHDDETIL 557
Cdd:PRK13635 134 LNREPHRLSGGQKQRVAIA--------GVLalqpdiIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAA 205
                         90       100       110
                 ....*....|....*....|....*....|...
gi 499583918 558 EADYILDIgpkagnEGGQIVAQGSVEDIKKSKE 590
Cdd:PRK13635 206 QADRVIVM------NKGEILEEGTPEEIFKSGH 232
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
806-900 2.93e-04

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: 44.43  E-value: 2.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  806 AKIREKLETLMDVGLGYIKLGQPATTLSGGEAQRVKLATHLLKKSTgktLYVLDEPTTGLHSYDVSNLLEVLKRIVNKGD 885
Cdd:TIGR02633 116 AMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQAR---LLILDEPSSSLTEKETEILLDIIRDLKAHGV 192
                          90
                  ....*....|....*
gi 499583918  886 TVIVIEHNLDVIKSV 900
Cdd:TIGR02633 193 ACVYISHKLNEVKAV 207
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
815-906 2.93e-04

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 43.16  E-value: 2.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 815 LMDVGLGYIKLGQPATTLSGGEAQRVKLATHL--LKKstgktLYVLDEPTTGLHSYDVSNLLEVLKRIV-NKGDTVIVIE 891
Cdd:PRK10247 121 LERFALPDTILTKNIAELSGGEKQRISLIRNLqfMPK-----VLLLDEITSALDESNKHNVNEIIHRYVrEQNIAVLWVT 195
                         90
                 ....*....|....*
gi 499583918 892 HNLDVIKSVDYIIDL 906
Cdd:PRK10247 196 HDKDEINHADKVITL 210
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
653-897 3.54e-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: 43.53  E-value: 3.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  653 LVNEVLIKGIEFVKGSQVHPGKHKEIKGLHNIDKIIQISQSPIGRTPRSNPATYTTVFDDIRDLFANTEDARASGFLKGR 732
Cdd:pfam13304  61 EISEFLEDGVRYRYGLDLEREDVEEKLSSKPTLLEKRLLLREDSEEREPKFPPEAEELRLGLDVEERIELSLSELSDLIS 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  733 FSFNVNGGRCDkcsgdGYLKIEMHFLPDVYVVCDHcDGKRYNPETLEIKYKFKNISDVLDmTVSEAFDFFANRAKIREKL 812
Cdd:pfam13304 141 GLLLLSIISPL-----SFLLLLDEGLLLEDWAVLD-LAADLALFPDLKELLQRLVRGLKL-ADLNLSDLGEGIEKSLLVD 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  813 ETLMDVGLGYIKLGQ----PATTLSGGEAQRVKLATHLLKKSTGKTLYVLDEPTTGLHSYDVSNLLEVLKRIVNKGDTVI 888
Cdd:pfam13304 214 DRLRERGLILLENGGggelPAFELSDGTKRLLALLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLI 293

                  ....*....
gi 499583918  889 VIEHNLDVI 897
Cdd:pfam13304 294 LTTHSPLLL 302
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
792-892 3.54e-04

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 43.64  E-value: 3.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 792 DMTVSEAFDFFA-----NRAKIREKLETLMDVGLGYIKLGQPATTLSGGEAQRVKLATHLLKKSTgktLYVLDEPTTGLH 866
Cdd:PRK13537  94 DFTVRENLLVFGryfglSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPD---VLVLDEPTTGLD 170
                         90       100
                 ....*....|....*....|....*.
gi 499583918 867 SYDVSNLLEVLKRIVNKGDTVIVIEH 892
Cdd:PRK13537 171 PQARHLMWERLRSLLARGKTILLTTH 196
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
789-892 3.72e-04

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 43.67  E-value: 3.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 789 DVLDM--TVSEAFDFFAN--RAKIREkLETLMDVGLGYIKLGQPATT----LSGGEAQRVKLATHLLKKSTgktLYVLDE 860
Cdd:PRK13536 123 DNLDLefTVRENLLVFGRyfGMSTRE-IEAVIPSLLEFARLESKADArvsdLSGGMKRRLTLARALINDPQ---LLILDE 198
                         90       100       110
                 ....*....|....*....|....*....|..
gi 499583918 861 PTTGLHSYDVSNLLEVLKRIVNKGDTVIVIEH 892
Cdd:PRK13536 199 PTTGLDPHARHLIWERLRSLLARGKTILLTTH 230
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
628-906 3.88e-04

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 44.63  E-value: 3.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  628 KNIDVKFPIGKFIAVTGVSGSGKSTLVNevLIKGI-EFVKGSQVHPGKH--KEIKGLHNIDKIIQISQSPI-GRTPRSNP 703
Cdd:PTZ00265  402 KDLNFTLTEGKTYAFVGESGCGKSTILK--LIERLyDPTEGDIIINDSHnlKDINLKWWRSKIGVVSQDPLlFSNSIKNN 479
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  704 ATYTTVfdDIRDLFANTEDARASGFLKGRFSFNVNGGRCdKCSGDgylkiemhfLPDVYVVCDhcdgkryNPETLEIKYK 783
Cdd:PTZ00265  480 IKYSLY--SLKDLEALSNYYNEDGNDSQENKNKRNSCRA-KCAGD---------LNDMSNTTD-------SNELIEMRKN 540
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  784 FKNISDVLDMTVSEAFDFFANRAKIREKLETLmdvglgyikLGQPATTLSGGEAQRVKLATHLLKKStgkTLYVLDEPTT 863
Cdd:PTZ00265  541 YQTIKDSEVVDVSKKVLIHDFVSALPDKYETL---------VGSNASKLSGGQKQRISIARAIIRNP---KILILDEATS 608
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 499583918  864 GLHS---YDVSNLLEVLKRivNKGDTVIVIEHNLDVIKSVDYIIDL 906
Cdd:PTZ00265  609 SLDNkseYLVQKTINNLKG--NENRITIIIAHRLSTIRYANTIFVL 652
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
631-901 3.89e-04

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


Pssm-ID: 213265 [Multi-domain]  Cd Length: 211  Bit Score: 42.87  E-value: 3.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 631 DVKFPIGKFIAVTGVSGSGKSTLVNevLIKGIEFVKGSQVHpgkhkeikgLHNIDkiiqISQSPIGRTPRSnpatytTVF 710
Cdd:cd03298   18 DLTFAQGEITAIVGPSGSGKSTLLN--LIAGFETPQSGRVL---------INGVD----VTAAPPADRPVS------MLF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 711 DDiRDLFANTEDARasgflkgrfsfNVNGGRCDkcsgdgylkiemhflpdvyvvcdhcdGKRYNPETleikykfknisdv 790
Cdd:cd03298   77 QE-NNLFAHLTVEQ-----------NVGLGLSP--------------------------GLKLTAED------------- 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 791 ldmtvSEAFDFFANRAKIREKLETLMDvglgyiklgqpatTLSGGEAQRVKLATHLLKKstgKTLYVLDEPTTGLHSYDV 870
Cdd:cd03298  106 -----RQAIEVALARVGLAGLEKRLPG-------------ELSGGERQRVALARVLVRD---KPVLLLDEPFAALDPALR 164
                        250       260       270
                 ....*....|....*....|....*....|..
gi 499583918 871 SNLLE-VLKRIVNKGDTVIVIEHNLDVIKSVD 901
Cdd:cd03298  165 AEMLDlVLDLHAETKMTVLMVTHQPEDAKRLA 196
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
832-931 4.16e-04

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


Pssm-ID: 213184 [Multi-domain]  Cd Length: 200  Bit Score: 42.51  E-value: 4.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 832 LSGGEAQRVKLATHLLKKSTgktLYVLDEPTTGLhsyDVSNL---LEVLKRIVNKGDTVIVIEHNLDVIKSVD----YII 904
Cdd:cd03217  105 FSGGEKKRNEILQLLLLEPD---LAILDEPDSGL---DIDALrlvAEVINKLREEGKSVLIITHYQRLLDYIKpdrvHVL 178
                         90       100
                 ....*....|....*....|....*..
gi 499583918 905 DlgpgggtnGGKIVATGTPEQVAEIKE 931
Cdd:cd03217  179 Y--------DGRIVKSGDKELALEIEK 197
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
492-585 4.85e-04

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: 42.86  E-value: 4.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 492 LSGGEAQRIRLATQIGSNLTgvLYVLDEPSIGLhQKDNEKLIKTLKHMVEIGNTLIVVEHDDETILEADYILDIgpkagn 571
Cdd:cd03252  139 LSGGQRQRIAIARALIHNPR--ILIFDEATSAL-DYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVM------ 209
                         90
                 ....*....|....
gi 499583918 572 EGGQIVAQGSVEDI 585
Cdd:cd03252  210 EKGRIVEQGSHDEL 223
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
808-926 5.08e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 43.15  E-value: 5.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 808 IREKL-ETLMDVGLGYIKLGQPATtLSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGLhsyDVSNLLEVLKRI--VNK- 883
Cdd:PRK13633 121 IRERVdESLKKVGMYEYRRHAPHL-LSGGQKQRVAIAGILAMRP---ECIIFDEPTAML---DPSGRREVVNTIkeLNKk 193
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 499583918 884 -GDTVIVIEHNLDVIKSVDYIIDLgpgggtNGGKIVATGTPEQV 926
Cdd:PRK13633 194 yGITIILITHYMEEAVEADRIIVM------DSGKVVMEGTPKEI 231
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
792-865 6.30e-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: 42.18  E-value: 6.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 792 DMTVSEAFDFFANRAKIREK------LETLMDVGLGYIKlGQPATTLSGGEAQRVKLATHLLKKSTgktLYVLDEPTTGL 865
Cdd:cd03264   86 NFTVREFLDYIAWLKGIPSKevkarvDEVLELVNLGDRA-KKKIGSLSGGMRRRVGIAQALVGDPS---ILIVDEPTAGL 161
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
825-939 7.26e-04

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 43.48  E-value: 7.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  825 LGQPATTLSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGLHSYDVSNLLEVLKRIVNKGD-TVIVIEHNLDVIKSVDYI 903
Cdd:PTZ00265 1352 VGPYGKSLSGGQKQRIAIARALLREP---KILLLDEATSSLDSNSEKLIEKTIVDIKDKADkTIITIAHRIASIKRSDKI 1428
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 499583918  904 IdLGPGGGTNGGKIVATGTPEQVAEIKESFTGQYLK 939
Cdd:PTZ00265 1429 V-VFNNPDRTGSFVQAHGTHEELLSVQDGVYKKYVK 1463
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
467-585 7.42e-04

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 43.35  E-value: 7.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 467 EIVNRLtfLSDVGLEYLTLNRTAETLSGGEAQRI---R-LATQ---IgsnltgvlyVLDEPSIGL---HQKDNEKLIKTL 536
Cdd:COG1123  382 ERVAEL--LERVGLPPDLADRYPHELSGGQRQRVaiaRaLALEpklL---------ILDEPTSALdvsVQAQILNLLRDL 450
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 499583918 537 KHmvEIGNTLIVVEHDDETILE-ADYILDIgpkagnEGGQIVAQGSVEDI 585
Cdd:COG1123  451 QR--ELGLTYLFISHDLAVVRYiADRVAVM------YDGRIVEDGPTEEV 492
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
833-897 7.63e-04

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 42.79  E-value: 7.63e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499583918 833 SGGEAQRVKLATHLLKKStgkTLYVLDEPTTGLhsyDVS------NLLEVLKRIVNKgdTVIVIEHNLDVI 897
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRP---KLLIADEPTTAL---DVTvqaqimTLLNELKREFNT--AIIMITHDLGVV 225
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
436-601 7.65e-04

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 42.34  E-value: 7.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 436 FSKLSIEEGLSKILSLEISSFEKEVSTlIVNEIVNRLTFLSDVgleYLTLNRTAETLSGGEAQRIRLATQIGsnLTGVLY 515
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGIKEKREIKK-IVEECLRKVGLWKEV---YDRLNSPASQLSGGQQQRLTIARALA--LKPKVL 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 516 VLDEPSIGL---HQKDNEKLIKTLKHMVeignTLIVVEHDDETILE-ADYIldigpkAGNEGGQIVAQGSVEDIKKS-KE 590
Cdd:PRK14246 176 LMDEPTSMIdivNSQAIEKLITELKNEI----AIVIVSHNPQQVARvADYV------AFLYNGELVEWGSSNEIFTSpKN 245
                        170
                 ....*....|.
gi 499583918 591 SITGKYLSGEL 601
Cdd:PRK14246 246 ELTEKYVIGRI 256
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
491-581 7.95e-04

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 43.23  E-value: 7.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 491 TLSGGEAQRIRLA------TQIgsnltgvlYVLDEPSIGLhqkD--NEKLI-KTLKHMVEiGNTLIVVEHDDETILEADY 561
Cdd:COG1132  476 NLSGGQRQRIAIArallkdPPI--------LILDEATSAL---DteTEALIqEALERLMK-GRTTIVIAHRLSTIRNADR 543
                         90       100
                 ....*....|....*....|
gi 499583918 562 ILDIgpkagnEGGQIVAQGS 581
Cdd:COG1132  544 ILVL------DDGRIVEQGT 557
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
490-592 8.17e-04

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 42.30  E-value: 8.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 490 ETLSGGEAQRIRLATQIgsNLTGVLYVLDEPSIGLHQKDNEKLIKTLKHMVEIGNTLIVVEHDDETILE---ADYILdig 566
Cdd:PRK13638 135 QCLSHGQKKRVAIAGAL--VLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEisdAVYVL--- 209
                         90       100
                 ....*....|....*....|....*.
gi 499583918 567 pkagnEGGQIVAQGSVEDIKKSKESI 592
Cdd:PRK13638 210 -----RQGQILTHGAPGEVFACTEAM 230
cbiO PRK13649
energy-coupling factor transporter ATPase;
809-926 8.79e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 42.42  E-value: 8.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 809 REKLETlmdVGLGYIKLGQPATTLSGGEAQRVKLATHLlkkSTGKTLYVLDEPTTGLHSYDVSNLLEVLKRIVNKGDTVI 888
Cdd:PRK13649 126 REKLAL---VGISESLFEKNPFELSGGQMRRVAIAGIL---AMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIV 199
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 499583918 889 VIEHNL-DVIKSVDYIIDLgpgggtNGGKIVATGTPEQV 926
Cdd:PRK13649 200 LVTHLMdDVANYADFVYVL------EKGKLVLSGKPKDI 232
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
807-897 9.31e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 42.14  E-value: 9.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 807 KIREKLETLMD-VGLGYIKlGQPATTLSGGEAQRVKLATHLLKKSTgktLYVLDEPTTGLHSYDVSNLLEVLKRIVNK-G 884
Cdd:PRK13636 117 EVRKRVDNALKrTGIEHLK-DKPTHCLSFGQKKRVAIAGVLVMEPK---VLVLDEPTAGLDPMGVSEIMKLLVEMQKElG 192
                         90
                 ....*....|...
gi 499583918 885 DTVIVIEHNLDVI 897
Cdd:PRK13636 193 LTIIIATHDIDIV 205
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
805-925 9.88e-04

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


Pssm-ID: 213232 [Multi-domain]  Cd Length: 220  Bit Score: 41.59  E-value: 9.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 805 RAKIREKLETLMD-VGLGYIKlGQPATTLSGGEAQRVKLATHLLKkstGKTLYVLDEPTTGLHSYDVSNLLEVLKRIVNK 883
Cdd:cd03265  105 GAERRERIDELLDfVGLLEAA-DRLVKTYSGGMRRRLEIARSLVH---RPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEE 180
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 499583918 884 GD-TVIVIEHNLDVIKSVD---YIIDlgpgggtnGGKIVATGTPEQ 925
Cdd:cd03265  181 FGmTILLTTHYMEEAEQLCdrvAIID--------HGRIIAEGTPEE 218
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
475-567 1.04e-03

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


Pssm-ID: 443308 [Multi-domain]  Cd Length: 206  Bit Score: 41.31  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 475 LSDVGLEYLtLNRTAETLSGGEAQRIRLATQIgsnLTGV-LYVLDEPSIGLHQKDNEKLIKTLKHMVEIGNTLIVVEHDD 553
Cdd:COG4133  116 LEAVGLAGL-ADLPVRQLSAGQKRRVALARLL---LSPApLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQP 191
                         90
                 ....*....|....
gi 499583918 554 ETiLEADYILDIGP 567
Cdd:COG4133  192 LE-LAAARVLDLGD 204
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
825-936 1.12e-03

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 41.80  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 825 LGQpatTLSGGEAQRVKLATHLlkkSTGKTLYVLDEPTTGLHSYDVSNLLEVLKRIVNKGDTVIVIEHN----LDVIKSV 900
Cdd:PRK10895 134 MGQ---SLSGGERRRVEIARAL---AANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNvretLAVCERA 207
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 499583918 901 dYIIDlgpgggtnGGKIVATGTPEQV---AEIKESFTGQ 936
Cdd:PRK10895 208 -YIVS--------QGHLIAHGTPTEIlqdEHVKRVYLGE 237
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
803-900 1.15e-03

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 41.62  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 803 ANRAKIREKLETLMD-VGLGYIKLGQPATtLSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGLHSYDVSNLLEVLKRIV 881
Cdd:PRK09493 108 ASKEEAEKQARELLAkVGLAERAHHYPSE-LSGGQQQRVAIARALAVKP---KLMLFDEPTSALDPELRHEVLKVMQDLA 183
                         90
                 ....*....|....*....
gi 499583918 882 NKGDTVIVIEHNLDVIKSV 900
Cdd:PRK09493 184 EEGMTMVIVTHEIGFAEKV 202
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
793-944 1.27e-03

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 42.69  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918   793 MTVSEAFDFFAN---RAKIREKLET---LMDVGLGYiKLGQPATTLSGGEAQRVKLATHLLKKSTgktLYVLDEPTTGLH 866
Cdd:TIGR01257 1018 LTVAEHILFYAQlkgRSWEEAQLEMeamLEDTGLHH-KRNEEAQDLSGGMQRKLSVAIAFVGDAK---VVVLDEPTSGVD 1093
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918   867 SYDVSNLLEVLKRiVNKGDTVIVIEHNLDvikSVDYIIDlgPGGGTNGGKIVATGTPeqvAEIKESF-TGQYLK--RMLK 943
Cdd:TIGR01257 1094 PYSRRSIWDLLLK-YRSGRTIIMSTHHMD---EADLLGD--RIAIISQGRLYCSGTP---LFLKNCFgTGFYLTlvRKMK 1164

                   .
gi 499583918   944 N 944
Cdd:TIGR01257 1165 N 1165
cbiO PRK13641
energy-coupling factor transporter ATPase;
799-938 1.31e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 41.74  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 799 FDFFANRAKIReKLETLMDVGLGYIKLGQPATTLSGGEAQRVKLATHLLKKSTgktLYVLDEPTTGLHSYDVSNLLEVLK 878
Cdd:PRK13641 114 FGFSEDEAKEK-ALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPE---ILCLDEPAAGLDPEGRKEMMQLFK 189
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 879 RIVNKGDTVIVIEHNLDVIKsvDYIIDLgpgGGTNGGKIVATGTPEQVAEIKESFTGQYL 938
Cdd:PRK13641 190 DYQKAGHTVILVTHNMDDVA--EYADDV---LVLEHGKLIKHASPKEIFSDKEWLKKHYL 244
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
827-892 1.36e-03

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 42.23  E-value: 1.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499583918  827 QPATTLSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGLHSYDVSNLLEVLKRIvnKGdTVIVIEH 892
Cdd:TIGR03719 157 ADVTKLSGGERRRVALCRLLLSKP---DMLLLDEPTNHLDAESVAWLERHLQEY--PG-TVVAVTH 216
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
792-895 1.37e-03

ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213236 [Multi-domain]  Cd Length: 210  Bit Score: 41.11  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 792 DMTVSEAFDFFA-----NRAKIREKLETLMD-VGLGYiKLGQPATTLSGGEAQRVKLATHLLKKSTgktLYVLDEPTTGL 865
Cdd:cd03269   84 KMKVIDQLVYLAqlkglKKEEARRRIDEWLErLELSE-YANKRVEELSKGNQQKVQFIAAVIHDPE---LLILDEPFSGL 159
                         90       100       110
                 ....*....|....*....|....*....|
gi 499583918 866 HSYDVSNLLEVLKRIVNKGDTVIVIEHNLD 895
Cdd:cd03269  160 DPVNVELLKDVIRELARAGKTVILSTHQME 189
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
469-585 1.38e-03

ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213263 [Multi-domain]  Cd Length: 239  Bit Score: 41.56  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 469 VNRLtfLSDVGLEYLTlNRTAETLSGGEAQRIRLATQIGSNlTGVLyVLDEPSIGLHQKDNEKLIKTLKHM-VEIGNTLI 547
Cdd:cd03296  117 VHEL--LKLVQLDWLA-DRYPAQLSGGQRQRVALARALAVE-PKVL-LLDEPFGALDAKVRKELRRWLRRLhDELHVTTV 191
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 499583918 548 VVEHDDETILE-ADYILDIgpkagnEGGQIVAQGSVEDI 585
Cdd:cd03296  192 FVTHDQEEALEvADRVVVM------NKGRIEQVGTPDEV 224
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
475-581 1.47e-03

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 42.12  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 475 LSDVGLEYLT-----LN-------RTaetLSGGEAQRIRLATQIGSNltGVLYVLDEPSIGLhQKDNEKLIKTL--KHMV 540
Cdd:PRK11160 450 LQQVGLEKLLeddkgLNawlgeggRQ---LSGGEQRRLGIARALLHD--APLLLLDEPTEGL-DAETERQILELlaEHAQ 523
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 499583918 541 eiGNTLIVVEHDDETILEADYILDIgpkagnEGGQIVAQGS 581
Cdd:PRK11160 524 --NKTVLMITHRLTGLEQFDRICVM------DNGQIIEQGT 556
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
790-890 1.61e-03

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 41.93  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 790 VLDMTVSE-----AFD-----FFANRAKIREKLETLMDvGLGyIK---LGQPATTLSGGEAQRVKLATHLLkksTGKTLY 856
Cdd:COG1129  342 VLDLSIREnitlaSLDrlsrgGLLDRRRERALAEEYIK-RLR-IKtpsPEQPVGNLSGGNQQKVVLAKWLA---TDPKVL 416
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 499583918 857 VLDEPTTGLhsyDV---SNLLEVLKRIVNKGDTVIVI 890
Cdd:COG1129  417 ILDEPTRGI---DVgakAEIYRLIRELAAEGKAVIVI 450
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
826-904 1.72e-03

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 42.02  E-value: 1.72e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499583918  826 GQPATTLSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGLHSYDVSNLLEVLKRivnKGDTVIVIEHNLDVIKSVDYII 904
Cdd:TIGR00958 612 GEKGSQLSGGQKQRIAIARALVRKP---RVLILDEATSALDAECEQLLQESRSR---ASRTVLLIAHRLSTVERADQIL 684
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
796-904 1.73e-03

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 42.26  E-value: 1.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 796 SEAFDFFANRAKireKLETLmdvglgyikLGQPATTLSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGLhsyDVSNLLE 875
Cdd:PRK13657 448 AQAHDFIERKPD---GYDTV---------VGERGRQLSGGERQRLAIARALLKDP---PILILDEATSAL---DVETEAK 509
                         90       100       110
                 ....*....|....*....|....*....|.
gi 499583918 876 VLKRI--VNKGDTVIVIEHNLDVIKSVDYII 904
Cdd:PRK13657 510 VKAALdeLMKGRTTFIIAHRLSTVRNADRIL 540
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
803-926 1.81e-03

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 41.13  E-value: 1.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 803 ANRAKIREKLET----LMDVGLGYIKlGQPATTLSGGEAQRVKLATHLLkksTGKTLYVLDEPTTGLH---SYDVSNLLE 875
Cdd:PRK11300 122 AFRRAESEALDRaatwLERVGLLEHA-NRQAGNLAYGQQRRLEIARCMV---TQPEILMLDEPAAGLNpkeTKELDELIA 197
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 499583918 876 VLKRivNKGDTVIVIEHNLDVIKSV-DYIIdlgpggGTNGGKIVATGTPEQV 926
Cdd:PRK11300 198 ELRN--EHNVTVLLIEHDMKLVMGIsDRIY------VVNQGTPLANGTPEEI 241
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
485-571 1.96e-03

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: 40.67  E-value: 1.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 485 LNRTAETLSGGE------AQRIRLATQIGSNLtGVLyVLDEPSIGLhQKDN--EKLIKTLKHMVEIGN-TLIVVEHDDET 555
Cdd:cd03240  109 LLDMRGRCSGGEkvlaslIIRLALAETFGSNC-GIL-ALDEPTTNL-DEENieESLAEIIEERKSQKNfQLIVITHDEEL 185
                         90
                 ....*....|....*.
gi 499583918 556 ILEADYILDIGPKAGN 571
Cdd:cd03240  186 VDAADHIYRVEKDGRQ 201
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
475-554 1.97e-03

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: 40.85  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 475 LSDVGLEYlTLNRTAETLSGGEAQRIRLATQIGSNLTgvLYVLDEPSIGLHQKDNEKLIKTLKHMVEIGNTLIVVEHDDE 554
Cdd:cd03292  121 LELVGLSH-KHRALPAELSGGEQQRVAIARAIVNSPT--ILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKE 197
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
458-585 1.97e-03

ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213267 [Multi-domain]  Cd Length: 232  Bit Score: 40.68  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 458 KEVSTLIVNEIVNRLtfLSDVGLEYLtLNRTAETLSGGEAQRIRLATQIgSNLTGVLyVLDEPSIGLHQKDNEKL---IK 534
Cdd:cd03300  100 KKLPKAEIKERVAEA--LDLVQLEGY-ANRKPSQLSGGQQQRVAIARAL-VNEPKVL-LLDEPLGALDLKLRKDMqleLK 174
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 499583918 535 TLKHMVEIgnTLIVVEHDDETILE-ADYILDIgpkagNEgGQIVAQGSVEDI 585
Cdd:cd03300  175 RLQKELGI--TFVFVTHDQEEALTmSDRIAVM-----NK-GKIQQIGTPEEI 218
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
467-593 2.10e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 40.89  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 467 EIVNRLtfLSDVGLeYLTLNRTAETLSGGEAQRIRLATQIGSNlTGVLyVLDEPSIGLHQKDNEKLIKTLKHMVEIGN-T 545
Cdd:PRK13648 121 RRVSEA--LKQVDM-LERADYEPNALSGGQKQRVAIAGVLALN-PSVI-ILDEATSMLDPDARQNLLDLVRKVKSEHNiT 195
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 499583918 546 LIVVEHDDETILEADYILDIGPkagnegGQIVAQGSVEDIKKSKESIT 593
Cdd:PRK13648 196 IISITHDLSEAMEADHVIVMNK------GTVYKEGTPTEIFDHAEELT 237
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
813-904 2.15e-03

ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).


Pssm-ID: 213227 [Multi-domain]  Cd Length: 227  Bit Score: 40.63  E-value: 2.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 813 ETLMDVGL-GYIKLGQPATTLSGGEAQRVKLAthllkkstgKTLYV------LDEPTTGLHSYDVSNLLEVLKRIvNKGD 885
Cdd:cd03260  122 EALRKAALwDEVKDRLHALGLSGGQQQRLCLA---------RALANepevllLDEPTSALDPISTAKIEELIAEL-KKEY 191
                         90       100
                 ....*....|....*....|
gi 499583918 886 TVIVIEHNLDVIKSV-DYII 904
Cdd:cd03260  192 TIVIVTHNMQQAARVaDRTA 211
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
488-552 2.21e-03

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


Pssm-ID: 274331 [Multi-domain]  Cd Length: 530  Bit Score: 41.58  E-value: 2.21e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499583918  488 TAETLSGGEAQRIRLATQIgsnLTGV-LYVLDEPSIGLHQKDNEKLIKTLKHmVEIGNTLIVVEHD 552
Cdd:TIGR02868 468 GGARLSGGERQRLALARAL---LADApILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHH 529
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
627-670 2.26e-03

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


Pssm-ID: 213260 [Multi-domain]  Cd Length: 220  Bit Score: 40.53  E-value: 2.26e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 499583918 627 LKNIDVKFPIGKFIAVTGVSGSGKSTLVNevLIKGIEFVKGSQV 670
Cdd:cd03293   20 LEDISLSVEEGEFVALVGPSGCGKSTLLR--IIAGLERPTSGEV 61
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
790-897 2.31e-03

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 41.55  E-value: 2.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 790 VLDMTVSE-----AFD-------FFANRAKIREKLETLMDvglGY-IK---LGQPATTLSGGEAQRVKLATHLlkkSTGK 853
Cdd:COG3845  348 VPDMSVAEnlilgRYRrppfsrgGFLDRKAIRAFAEELIE---EFdVRtpgPDTPARSLSGGNQQKVILAREL---SRDP 421
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 499583918 854 TLYVLDEPTTGLhsyDVSNLLEVLKRIV---NKGDTVIVIEHNLDVI 897
Cdd:COG3845  422 KLLIAAQPTRGL---DVGAIEFIHQRLLelrDAGAAVLLISEDLDEI 465
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
472-571 2.38e-03

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 40.47  E-value: 2.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 472 LTFLSDVGLEYLTLNRTAETLSGGEAQRIRLATQIgSNLTGVLyVLDEPSIGLHQKDNEKLIKTLKHMVEIGNTLIV-VE 550
Cdd:PRK10247 118 LDDLERFALPDTILTKNIAELSGGEKQRISLIRNL-QFMPKVL-LLDEITSALDESNKHNVNEIIHRYVREQNIAVLwVT 195
                         90       100
                 ....*....|....*....|.
gi 499583918 551 HDDETILEADYILDIGPKAGN 571
Cdd:PRK10247 196 HDKDEINHADKVITLQPHAGE 216
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
489-599 2.45e-03

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 40.63  E-value: 2.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 489 AETLSGGEAQRIRLATQIGSNLTgvLYVLDEPSIGLHQKDNEKLIKTLKHMVEIGNTLIVVEHDDETILE-AD--YILdi 565
Cdd:PRK11614 135 AGTMSGGEQQMLAIGRALMSQPR--LLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKlADrgYVL-- 210
                         90       100       110
                 ....*....|....*....|....*....|....
gi 499583918 566 gpkagnEGGQIVAQGSVEDIkKSKESITGKYLSG 599
Cdd:PRK11614 211 ------ENGHVVLEDTGDAL-LANEAVRSAYLGG 237
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
832-904 2.49e-03

ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.


Pssm-ID: 213212 [Multi-domain]  Cd Length: 220  Bit Score: 40.27  E-value: 2.49e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499583918 832 LSGGEAQRVKLATHLLKKSTgktLYVLDEPTTGLHSYDVSNLLEVLKRIVnKGDTVIVIEHNLDVIKSVDYII 904
Cdd:cd03245  141 LSGGQRQAVALARALLNDPP---ILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPSLLDLVDRII 209
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
790-926 2.56e-03

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 40.36  E-value: 2.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 790 VLDMTVSEAfdffanRAKIREKLETlmdVGLG-----YiklgqPATtLSGGEAQRV----KLATH---LLkkstgktlyv 857
Cdd:COG1126  105 VKKMSKAEA------EERAMELLER---VGLAdkadaY-----PAQ-LSGGQQQRVaiarALAMEpkvML---------- 159
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499583918 858 LDEPTTGLhsyD---VSNLLEVLKRIVNKGDTVIVIEHNLDVIKSV-DYII--DlgpgggtnGGKIVATGTPEQV 926
Cdd:COG1126  160 FDEPTSAL---DpelVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVaDRVVfmD--------GGRIVEEGPPEEF 223
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
14-48 2.69e-03

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


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 40.14  E-value: 2.69e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 499583918  14 KGAKENNLKNIDVVIPKNKLVVFTGLSGSGKSSLA 48
Cdd:cd03225   10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLL 44
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
826-906 2.72e-03

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


Pssm-ID: 213215 [Multi-domain]  Cd Length: 226  Bit Score: 40.53  E-value: 2.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 826 GQPATTLSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGLhsyDVSNLLEVLKRIV--NKGDTVIVIEHNLDVIKSVDYI 903
Cdd:cd03248  145 GEKGSQLSGGQKQRVAIARALIRNP---QVLILDEATSAL---DAESEQQVQQALYdwPERRTVLVIAHRLSTVERADQI 218

                 ...
gi 499583918 904 IDL 906
Cdd:cd03248  219 LVL 221
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
803-895 2.82e-03

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 40.51  E-value: 2.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 803 ANRAKIREKLETlmdVGLGYIKLGQPATtLSGGEAQRVKLATHLLKKstgKTLYVLDEPTTGLhsyDV---SNLLEVLKR 879
Cdd:COG3840  105 EQRAQVEQALER---VGLAGLLDRLPGQ-LSGGQRQRVALARCLVRK---RPILLLDEPFSAL---DPalrQEMLDLVDE 174
                         90
                 ....*....|....*..
gi 499583918 880 IV-NKGDTVIVIEHNLD 895
Cdd:COG3840  175 LCrERGLTVLMVTHDPE 191
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
805-936 2.92e-03

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


Pssm-ID: 213262 [Multi-domain]  Cd Length: 242  Bit Score: 40.36  E-value: 2.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 805 RAKIREK-LETLMDVGLGYIKLGQ--PATtLSGGEAQRVKLATHLlkkSTGKTLYVLDEPTTGLHSYDVSNLLEVLKRIV 881
Cdd:cd03295  107 KEKIRERaDELLALVGLDPAEFADryPHE-LSGGQQQRVGVARAL---AADPPLLLMDEPFGALDPITRDQLQEEFKRLQ 182
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499583918 882 NK-GDTVIVIEHNLD-VIKSVDYIIDLgpgggtNGGKIVATGTPEQV-----AEIKESFTGQ 936
Cdd:cd03295  183 QElGKTIVFVTHDIDeAFRLADRIAIM------KNGEIVQVGTPDEIlrspaNDFVAEFVGA 238
cbiO PRK13637
energy-coupling factor transporter ATPase;
832-926 3.03e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 40.80  E-value: 3.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 832 LSGGEAQRVKLATHLLKKStgKTLyVLDEPTTGLHSYDVSNLLEVLKRIVNKGD-TVIVIEHNL-DVIKSVDYIIDLgpg 909
Cdd:PRK13637 145 LSGGQKRRVAIAGVVAMEP--KIL-ILDEPTAGLDPKGRDEILNKIKELHKEYNmTIILVSHSMeDVAKLADRIIVM--- 218
                         90
                 ....*....|....*..
gi 499583918 910 ggtNGGKIVATGTPEQV 926
Cdd:PRK13637 219 ---NKGKCELQGTPREV 232
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
627-671 3.29e-03

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 40.12  E-value: 3.29e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 499583918 627 LKNIDVKFPIGKFIAVTGVSGSGKSTLVNevLIKGIEFVKGSQVH 671
Cdd:COG3840   15 PLRFDLTIAAGERVAILGPSGAGKSTLLN--LIAGFLPPDSGRIL 57
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
627-653 3.62e-03

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


Pssm-ID: 443338 [Multi-domain]  Cd Length: 233  Bit Score: 40.11  E-value: 3.62e-03
                         10        20
                 ....*....|....*....|....*..
gi 499583918 627 LKNIDVKFPIGKFIAVTGVSGSGKSTL 653
Cdd:COG4181   28 LKGISLEVEAGESVAIVGASGSGKSTL 54
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
824-904 3.73e-03

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 41.47  E-value: 3.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918   824 KLGQPATTLSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGLHSYDVSNLLE--VLKRIVNKGDTVIVIEHNLDVIKSVD 901
Cdd:TIGR00957  753 EIGEKGVNLSGGQKQRVSLARAVYSNA---DIYLFDDPLSAVDAHVGKHIFEhvIGPEGVLKNKTRILVTHGISYLPQVD 829

                   ...
gi 499583918   902 YII 904
Cdd:TIGR00957  830 VII 832
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
21-48 3.79e-03

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


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 39.29  E-value: 3.79e-03
                         10        20
                 ....*....|....*....|....*...
gi 499583918  21 LKNIDVVIPKNKLVVFTGLSGSGKSSLA 48
Cdd:cd03228   18 LKDVSLTIKPGEKVAIVGPSGSGKSTLL 45
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
813-903 3.96e-03

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 40.03  E-value: 3.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 813 ETLMDVGLG---YIKLGQPATTLSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGL---HSYDVSNLLEVLKRIVnkgdT 886
Cdd:PRK14246 132 ECLRKVGLWkevYDRLNSPASQLSGGQQQRLTIARALALKP---KVLLMDEPTSMIdivNSQAIEKLITELKNEI----A 204
                         90
                 ....*....|....*...
gi 499583918 887 VIVIEHN-LDVIKSVDYI 903
Cdd:PRK14246 205 IVIVSHNpQQVARVADYV 222
cbiO PRK13645
energy-coupling factor transporter ATPase;
487-606 4.04e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 40.38  E-value: 4.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 487 RTAETLSGGEAQRIRLATQIGsnLTGVLYVLDEPSIGLHQKDNEKLIKTLKHM-VEIGNTLIVVEHDDETILE-ADYILd 564
Cdd:PRK13645 146 RSPFELSGGQKRRVALAGIIA--MDGNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRiADEVI- 222
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 499583918 565 igpkagneggqIVAQGSVEDIKKSKESITGKYLSGELKIEIP 606
Cdd:PRK13645 223 -----------VMHEGKVISIGSPFEIFSNQELLTKIEIDPP 253
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
21-47 4.09e-03

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


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 38.77  E-value: 4.09e-03
                         10        20
                 ....*....|....*....|....*..
gi 499583918  21 LKNIDVVIPKNKLVVFTGLSGSGKSSL 47
Cdd:cd00267   15 LDNVSLTLKAGEIVALVGPNGSGKSTL 41
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
36-61 4.20e-03

Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; Adenylylsulfate kinase or related kinase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440295 [Multi-domain]  Cd Length: 189  Bit Score: 39.30  E-value: 4.20e-03
                         10        20
                 ....*....|....*....|....*....
gi 499583918  36 FTGLSGSGKSSLAF---NTIYEEGRRRYV 61
Cdd:COG0529   21 FTGLSGSGKSTLANaleRRLFERGRHVYL 49
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
793-894 4.36e-03

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: 39.51  E-value: 4.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 793 MTVSEAFDFFANRAKIREKL--ETLMDVGLGYIKlGQPATTLSGGEAQRVKLATHLLkksTGKTLYVLDEPTTGLHSYDV 870
Cdd:cd03268   87 LTARENLRLLARLLGIRKKRidEVLDVVGLKDSA-KKKVKGFSLGMKQRLGIALALL---GNPDLLILDEPTNGLDPDGI 162
                         90       100
                 ....*....|....*....|....
gi 499583918 871 SNLLEVLKRIVNKGDTVIVIEHNL 894
Cdd:cd03268  163 KELRELILSLRDQGITVLISSHLL 186
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
832-931 4.40e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 39.97  E-value: 4.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 832 LSGGEAQRVKLATHLlkkSTGKTLYVLDEPTTGLHSYDVSNLLEVLKRIVNKGD-TVIVIEHNLDVIKSVDYIIDLgpgg 910
Cdd:PRK13632 143 LSGGQKQRVAIASVL---ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAILADKVIVF---- 215
                         90       100
                 ....*....|....*....|.
gi 499583918 911 gtNGGKIVATGTPEQVAEIKE 931
Cdd:PRK13632 216 --SEGKLIAQGKPKEILNNKE 234
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
485-585 4.44e-03

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


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 40.56  E-value: 4.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  485 LNRTAETLSGGEAQRIRLAtQIGSNLTGVLyVLDEPSIGLHQKDNEKLIKT-LKHMVEIGNTLIVVEHDdetileADYIL 563
Cdd:TIGR03269 421 LDKYPDELSEGERHRVALA-QVLIKEPRIV-ILDEPTGTMDPITKVDVTHSiLKAREEMEQTFIIVSHD------MDFVL 492
                          90       100
                  ....*....|....*....|...
gi 499583918  564 DIGPKAG-NEGGQIVAQGSVEDI 585
Cdd:TIGR03269 493 DVCDRAAlMRDGKIVKIGDPEEI 515
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
491-584 4.45e-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: 39.91  E-value: 4.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 491 TLSGGEAQRIRLATQIGSNLTgvLYVLDEPSIGLhqkDN--EKLI-KTLKHMVEiGNTLIVVEHDDETILEADYILDIgp 567
Cdd:cd03251  138 KLSGGQRQRIAIARALLKDPP--ILILDEATSAL---DTesERLVqAALERLMK-NRTTFVIAHRLSTIENADRIVVL-- 209
                         90
                 ....*....|....*..
gi 499583918 568 kagnEGGQIVAQGSVED 584
Cdd:cd03251  210 ----EDGKIVERGTHEE 222
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
805-895 4.77e-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: 39.43  E-value: 4.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 805 RAKIREKLETLMD-VGLGyIKLGQPATTLSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGLHSYDVSNLLEVLKRIVNK 883
Cdd:cd03259  104 KAEIRARVRELLElVGLE-GLLNRYPHELSGGQQQRVALARALAREP---SLLLLDEPLSALDAKLREELREELKELQRE 179
                         90
                 ....*....|...
gi 499583918 884 -GDTVIVIEHNLD 895
Cdd:cd03259  180 lGITTIYVTHDQE 192
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
806-906 4.88e-03

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 40.43  E-value: 4.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 806 AKIREKLETLmdvGLGYIKLGQPATTLSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGLhsyDVSNLL---EVLKRivN 882
Cdd:COG0488  130 ARAEEILSGL---GFPEEDLDRPVSELSGGWRRRVALARALLSEP---DLLLLDEPTNHL---DLESIEwleEFLKN--Y 198
                         90       100
                 ....*....|....*....|....*..
gi 499583918 883 KGdTVIVIEHN---LDVIksVDYIIDL 906
Cdd:COG0488  199 PG-TVLVVSHDryfLDRV--ATRILEL 222
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
480-586 5.22e-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: 39.28  E-value: 5.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 480 LEYLTL----NRTAETLSGGEAQRIRLATQIgSNLTGVLYvLDEPSIGLHQKDNEKLIKTLKHMV-EIGNTLIVVEHDDE 554
Cdd:cd03265  116 LDFVGLleaaDRLVKTYSGGMRRRLEIARSL-VHRPEVLF-LDEPTIGLDPQTRAHVWEYIEKLKeEFGMTILLTTHYME 193
                         90       100       110
                 ....*....|....*....|....*....|..
gi 499583918 555 tilEADYILDigPKAGNEGGQIVAQGSVEDIK 586
Cdd:cd03265  194 ---EAEQLCD--RVAIIDHGRIIAEGTPEELK 220
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
475-597 5.45e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 39.68  E-value: 5.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 475 LSDVGLEYLTlNRTAETLSGGEAQRIRLATQIGSNLTgvLYVLDEPSIGLHQKDNEKLIKTLKHMVEIGNTLIVVEHD-D 553
Cdd:PRK13639 122 LKAVGMEGFE-NKPPHHLSGGQKKRVAIAGILAMKPE--IIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDvD 198
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 499583918 554 ETILEADYILDIGpkagneGGQIVAQGSVEDIKKSKESITGKYL 597
Cdd:PRK13639 199 LVPVYADKVYVMS------DGKIIKEGTPKEVFSDIETIRKANL 236
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
828-892 5.48e-03

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 40.32  E-value: 5.48e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499583918 828 PATTLSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGLhsyDVSNlLEVLKRIV-NKGDTVIVIEH 892
Cdd:PRK11147 437 PVKALSGGERNRLLLARLFLKPS---NLLILDEPTNDL---DVET-LELLEELLdSYQGTVLLVSH 495
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
492-564 6.81e-03

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


Pssm-ID: 213196 [Multi-domain]  Cd Length: 178  Bit Score: 38.71  E-value: 6.81e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499583918 492 LSGGEAQRIRLATQIGSNlTGVLyVLDEPSIGLHQK---DNEKLIKTLKHMVEIgnTLIVVEHDdetILEADYILD 564
Cdd:cd03229  101 LSGGQQQRVALARALAMD-PDVL-LLDEPTSALDPItrrEVRALLKSLQAQLGI--TVVLVTHD---LDEAARLAD 169
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
640-677 6.92e-03

Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits.


Pssm-ID: 238979 [Multi-domain]  Cd Length: 150  Bit Score: 38.00  E-value: 6.92e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 499583918 640 IAVTGVSGSGKSTlVNEVLIK--GIEFVKGSQVHPGKHKE 677
Cdd:cd02021    2 IVVMGVSGSGKST-VGKALAErlGAPFIDGDDLHPPANIA 40
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
824-904 7.57e-03

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: 38.85  E-value: 7.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 824 KLGQPATTLSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGLHSYDVSNLLE--VLKRIVNKGDTVIVIEHNLDVIKSVD 901
Cdd:cd03290  133 EIGERGINLSGGQRQRICVARALYQNT---NIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPHAD 209

                 ...
gi 499583918 902 YII 904
Cdd:cd03290  210 WII 212
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
492-554 7.80e-03

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 38.99  E-value: 7.80e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499583918 492 LSGGEAQRIRLATQIgSNLTGVLYVlDEPSIGLHQKDNEKLIKTLKHM-VEIGNTLIVVEHDDE 554
Cdd:PRK10584 147 LSGGEQQRVALARAF-NGRPDVLFA-DEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDLQ 208
cbiO PRK13642
energy-coupling factor transporter ATPase;
769-904 8.51e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 39.31  E-value: 8.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 769 DGKRYNPETL-----EIKYKFKNISD-VLDMTVSEAFDF-FANRAKIREKL-----ETLMDVGLGYIKLGQPATtLSGGE 836
Cdd:PRK13642  67 DGELLTAENVwnlrrKIGMVFQNPDNqFVGATVEDDVAFgMENQGIPREEMikrvdEALLAVNMLDFKTREPAR-LSGGQ 145
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499583918 837 AQRVKLATHLLKKStgkTLYVLDEPTTGLHSYDVSNLLEVLKRIVNKGD-TVIVIEHNLDVIKSVDYII 904
Cdd:PRK13642 146 KQRVAVAGIIALRP---EIIILDESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAASSDRIL 211
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
832-904 8.69e-03

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 39.10  E-value: 8.69e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499583918 832 LSGGEAQRVKLATHLLKKSTgktLYVLDEPTTGLHSYDVSNLLEVLKRIVNKGDTVIVIEHNL-DVIKSVDYII 904
Cdd:PRK15056 143 LSGGQKKRVFLARAIAQQGQ---VILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLgSVTEFCDYTV 213
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
823-906 8.89e-03

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


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 39.89  E-value: 8.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918   823 IKLGQPATTLSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGLHSYDVSNLLE--VLKRIVNKgdTVIVIEHNLDVIKSV 900
Cdd:TIGR01271  540 TVLGEGGITLSGGQRARISLARAVYKDA---DLYLLDSPFTHLDVVTEKEIFEscLCKLMSNK--TRILVTSKLEHLKKA 614

                   ....*.
gi 499583918   901 DYIIDL 906
Cdd:TIGR01271  615 DKILLL 620
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
819-927 9.20e-03

molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]


Pssm-ID: 131197 [Multi-domain]  Cd Length: 354  Bit Score: 39.32  E-value: 9.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918  819 GLGYIkLGQPATTLSGGEAQRVKLATHLLkksTGKTLYVLDEPttgLHSYDVSNLLEVLKRIVNKGDT----VIVIEHNL 894
Cdd:TIGR02142 120 GIGHL-LGRLPGRLSGGEKQRVAIGRALL---SSPRLLLMDEP---LAALDDPRKYEILPYLERLHAEfgipILYVSHSL 192
                          90       100       110
                  ....*....|....*....|....*....|....
gi 499583918  895 D-VIKSVDYIIDLgpgggtNGGKIVATGTPEQVA 927
Cdd:TIGR02142 193 QeVLRLADRVVVL------EDGRVAAAGPIAEVW 220
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
805-926 9.35e-03

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 39.67  E-value: 9.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 805 RAKIREKLEtlmDVGLgyiklgqPATTL-------SGGEAQRVKLATHL-LKKStgktLYVLDEPTTGLhsyDVS---NL 873
Cdd:COG4172  402 RARVAEALE---EVGL-------DPAARhryphefSGGQRQRIAIARALiLEPK----LLVLDEPTSAL---DVSvqaQI 464
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 499583918 874 LEVLKRIVNK-GDTVIVIEHNLDVIKSV-DYIIDLgpgggtNGGKIVATGTPEQV 926
Cdd:COG4172  465 LDLLRDLQREhGLAYLFISHDLAVVRALaHRVMVM------KDGKVVEQGPTEQV 513
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
803-902 9.62e-03

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 38.70  E-value: 9.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499583918 803 ANRAKIREKLETLMD-VGLgYIKLGQPATTLSGGEAQRVKLATHLLKKStgkTLYVLDEPTTGLH---SYDVSNLLEVLK 878
Cdd:PRK10908 109 ASGDDIRRRVSAALDkVGL-LDKAKNFPIQLSGGEQQRVGIARAVVNKP---AVLLADEPTGNLDdalSEGILRLFEEFN 184
                         90       100
                 ....*....|....*....|....
gi 499583918 879 RIvnkGDTVIVIEHNLDVIKSVDY 902
Cdd:PRK10908 185 RV---GVTVLMATHDIGLISRRSY 205
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
832-890 9.89e-03

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: 38.18  E-value: 9.89e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499583918 832 LSGGEAQRVKLATHLLkksTGKTLYVLDEPTTGLhsyDVSNLLEVLKRIV---NKGDTVIVI 890
Cdd:cd03215  105 LSGGNQQKVVLARWLA---RDPRVLILDEPTRGV---DVGAKAEIYRLIRelaDAGKAVLLI 160
 
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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