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Conserved domains on  [gi|835833681|ref|WP_047673967|]
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excinuclease ABC subunit UvrA [Lactiplantibacillus plantarum]

Protein Classification

excinuclease ABC subunit UvrA( domain architecture ID 1000295)

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 super family cl33793
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
9-831 0e+00

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


The actual alignment was detected with superfamily member COG0178:

Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 855.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681   9 HIQVRGAHVNNLKNIDIDIPLNEFVAITGRSGSGKSSLAMGVLYAEGARRYLNALSTFTRRRINQVGKASVDSVQYLPSA 88
Cdd:COG0178    5 KIRIRGAREHNLKNIDVDIPRNKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLSPA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  89 LALRQRPQVPGVRSTVGTMSEslnI---LRLAFSRLSSAVCPN----------------------GHRM----------- 132
Cdd:COG0178   85 ISIEQKTTSRNPRSTVGTVTE---IydyLRLLFARVGTPHCPIcgrpvekqtvdqivdrilalpeGTRLqilapvvrgrk 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 133 -----------------------------PPTLD---------------VAEN----------------DGYVT------ 146
Cdd:COG0178  162 gehkelleelrkqgfvrvrvdgevydldeEPELDknkkhtievvvdrlvVKEDirsrladsvetalklgDGLVIvevvde 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 147 -----------CPTCGAKFRAPGAEDFAFNSG-GACPTCGGLGQVRQIDPALIIADENQTIEEGAVASWHLPGRNFMP-- 212
Cdd:COG0178  242 geellfsekfaCPDCGISFEELEPRLFSFNSPyGACPTCDGLGRVLEFDPDLVIPDPSLSLAEGAIAPWSGPSSSYYFql 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 213 --IVAREIGIPIDIPYKDLSEADKTRVLHGPKQTVAINIPSAKGKifHMDNAVYENAFAAVEDSMATTKNERAITRLNRF 290
Cdd:COG0178  322 leALAKHYGFDLDTPWKDLPEEQRDLILYGSDEKIKFRYKNRGRR--RTYEKPFEGVIPFLERRYRETYSEHVREELSRY 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 291 YKFDTCPDCHGSRFNPQLFNYELNGQNIATVSDMTVAALHDFAATIVpwLPTKMHHLGQSLVDELLLSLQPMEELGLDYL 370
Cdd:COG0178  400 MSETPCPACKGARLKPEALAVKIGGKNIAELTALSIDEALEFFENLE--LTEREAEIAERILKEIRSRLGFLVDVGLDYL 477
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 371 TLSRPGATLSTGELQRIQLGRTLRSTTTGVLYVLDEPSVGLHPANVAGLIKAFRGLVAQGNSVVVVDHDTSIISAADDVI 450
Cdd:COG0178  478 TLDRSAGTLSGGEAQRIRLATQIGSGLVGVLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDTIRAADYII 557
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 451 EIGPGAGKHGGTVVGQGTVAAIKQDKESLIAPFLTGT---ATLRERPVltddalWKKGALAIEVAHHFNIQDITARIPKN 527
Cdd:COG0178  558 DIGPGAGEHGGEVVAQGTPEEILKNPDSLTGQYLSGRkriPVPKKRRK------GNGKFLTIKGARENNLKNVDVEIPLG 631
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 528 RFTTVTGMSGAGKTTLVLDSLIPAL---IATAKKRPLP-THVKAFDngHIRHVVTVDSVPVGKNVRSTVATYTNILDHLR 603
Cdd:COG0178  632 VLTCVTGVSGSGKSTLVNDILYPALarkLNGAKEKPGPhDSIEGLE--HIDKVIDIDQSPIGRTPRSNPATYTGVFDPIR 709
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 604 QLFAATPAAQANGWTASQFSYNVAAGACPTCGGTGQISLDVQYLPDITEVCPQCHGKRYNKQTLTVKWHGYSIADILDLA 683
Cdd:COG0178  710 ELFAQTPEAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMT 789
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 684 VDEALPIFKAQSAIANTLQILHDMGLGYLLLGESTPALSGGEAQRLKLTSRIGKRQTG-TLFVFDEPSVGLHPLDIQQLV 762
Cdd:COG0178  790 VEEALEFFENIPKIARKLQTLQDVGLGYIKLGQPATTLSGGEAQRVKLASELSKRSTGkTLYILDEPTTGLHFHDIRKLL 869
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 835833681 763 KVFDQLIQQGATVIAIEHDLDVIANADYVIDMGPAGGINGGNIVATGTPLAVSQNPTSVTGQYLKTHLA 831
Cdd:COG0178  870 EVLHRLVDKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVAEGTPEEVAKVKASYTGRYLKEYLE 938
 
Name Accession Description Interval E-value
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
9-831 0e+00

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


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 855.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681   9 HIQVRGAHVNNLKNIDIDIPLNEFVAITGRSGSGKSSLAMGVLYAEGARRYLNALSTFTRRRINQVGKASVDSVQYLPSA 88
Cdd:COG0178    5 KIRIRGAREHNLKNIDVDIPRNKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLSPA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  89 LALRQRPQVPGVRSTVGTMSEslnI---LRLAFSRLSSAVCPN----------------------GHRM----------- 132
Cdd:COG0178   85 ISIEQKTTSRNPRSTVGTVTE---IydyLRLLFARVGTPHCPIcgrpvekqtvdqivdrilalpeGTRLqilapvvrgrk 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 133 -----------------------------PPTLD---------------VAEN----------------DGYVT------ 146
Cdd:COG0178  162 gehkelleelrkqgfvrvrvdgevydldeEPELDknkkhtievvvdrlvVKEDirsrladsvetalklgDGLVIvevvde 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 147 -----------CPTCGAKFRAPGAEDFAFNSG-GACPTCGGLGQVRQIDPALIIADENQTIEEGAVASWHLPGRNFMP-- 212
Cdd:COG0178  242 geellfsekfaCPDCGISFEELEPRLFSFNSPyGACPTCDGLGRVLEFDPDLVIPDPSLSLAEGAIAPWSGPSSSYYFql 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 213 --IVAREIGIPIDIPYKDLSEADKTRVLHGPKQTVAINIPSAKGKifHMDNAVYENAFAAVEDSMATTKNERAITRLNRF 290
Cdd:COG0178  322 leALAKHYGFDLDTPWKDLPEEQRDLILYGSDEKIKFRYKNRGRR--RTYEKPFEGVIPFLERRYRETYSEHVREELSRY 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 291 YKFDTCPDCHGSRFNPQLFNYELNGQNIATVSDMTVAALHDFAATIVpwLPTKMHHLGQSLVDELLLSLQPMEELGLDYL 370
Cdd:COG0178  400 MSETPCPACKGARLKPEALAVKIGGKNIAELTALSIDEALEFFENLE--LTEREAEIAERILKEIRSRLGFLVDVGLDYL 477
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 371 TLSRPGATLSTGELQRIQLGRTLRSTTTGVLYVLDEPSVGLHPANVAGLIKAFRGLVAQGNSVVVVDHDTSIISAADDVI 450
Cdd:COG0178  478 TLDRSAGTLSGGEAQRIRLATQIGSGLVGVLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDTIRAADYII 557
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 451 EIGPGAGKHGGTVVGQGTVAAIKQDKESLIAPFLTGT---ATLRERPVltddalWKKGALAIEVAHHFNIQDITARIPKN 527
Cdd:COG0178  558 DIGPGAGEHGGEVVAQGTPEEILKNPDSLTGQYLSGRkriPVPKKRRK------GNGKFLTIKGARENNLKNVDVEIPLG 631
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 528 RFTTVTGMSGAGKTTLVLDSLIPAL---IATAKKRPLP-THVKAFDngHIRHVVTVDSVPVGKNVRSTVATYTNILDHLR 603
Cdd:COG0178  632 VLTCVTGVSGSGKSTLVNDILYPALarkLNGAKEKPGPhDSIEGLE--HIDKVIDIDQSPIGRTPRSNPATYTGVFDPIR 709
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 604 QLFAATPAAQANGWTASQFSYNVAAGACPTCGGTGQISLDVQYLPDITEVCPQCHGKRYNKQTLTVKWHGYSIADILDLA 683
Cdd:COG0178  710 ELFAQTPEAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMT 789
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 684 VDEALPIFKAQSAIANTLQILHDMGLGYLLLGESTPALSGGEAQRLKLTSRIGKRQTG-TLFVFDEPSVGLHPLDIQQLV 762
Cdd:COG0178  790 VEEALEFFENIPKIARKLQTLQDVGLGYIKLGQPATTLSGGEAQRVKLASELSKRSTGkTLYILDEPTTGLHFHDIRKLL 869
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 835833681 763 KVFDQLIQQGATVIAIEHDLDVIANADYVIDMGPAGGINGGNIVATGTPLAVSQNPTSVTGQYLKTHLA 831
Cdd:COG0178  870 EVLHRLVDKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVAEGTPEEVAKVKASYTGRYLKEYLE 938
uvrA PRK00349
excinuclease ABC subunit UvrA;
9-831 0e+00

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 747.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681   9 HIQVRGAHVNNLKNIDIDIPLNEFVAITGRSGSGKSSLAMGVLYAEGARRYLNALSTFTRRRINQVGKASVDSVQYLPSA 88
Cdd:PRK00349   5 KIIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLSPA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  89 LALRQR-----PqvpgvRSTVGTMSESLNILRLAFSRLSSAVCPNGHR---------M---------------------- 132
Cdd:PRK00349  85 ISIDQKttshnP-----RSTVGTVTEIYDYLRLLYARVGKPHCPNCGRpieaqtvsqMvdrvlelpegtrlqilapvvrg 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 133 -------------------------------PPTLD---------------VAEN----------------DGYVT---- 146
Cdd:PRK00349 160 rkgehkkllenlrkqgfvrvrvdgevydldePPKLDknkkhtievvvdrlvVKEDirqrladsietalklsDGLVVvevm 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 147 ---------------CPTCGAKF-----RApgaedFAFNSG-GACPTCGGLGQVRQIDPALIIADENQTIEEGAVASWHL 205
Cdd:PRK00349 240 ddpeaeellfsekfaCPVCGFSIpelepRL-----FSFNSPyGACPTCDGLGVKLEFDPDLVVPDPELSLAEGAIAPWSR 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 206 PGRNFMP----IVAREIGIPIDIPYKDLSEADKTRVLHG-PKQTVAINIPSAKGKIFHMdNAVYENAFAAVEDSMATTKN 280
Cdd:PRK00349 315 SSSSYYFqmlkSLAEHYGFDLDTPWKDLPEEVQDIILYGsGDEEIEFRYKNDRGRTRER-KHPFEGVIPNLERRYRETES 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 281 ERAITRLNRFYKFDTCPDCHGSRFNPQLFNYELNGQNIATVSDMTVAALHDFAATIVpwLPTKMHHLGQSLVDELLLSLQ 360
Cdd:PRK00349 394 EYVREELEKYMSERPCPSCKGKRLKPEALAVKVGGKNIGEVSELSIGEALEFFENLK--LSEQEAKIAEPILKEIRERLK 471
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 361 PMEELGLDYLTLSRPGATLSTGELQRI----QLGRTLrsttTGVLYVLDEPSVGLHPANVAGLIKAFRGLVAQGNSVVVV 436
Cdd:PRK00349 472 FLVDVGLDYLTLSRSAGTLSGGEAQRIrlatQIGSGL----TGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVV 547
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 437 DHDTSIISAADDVIEIGPGAGKHGGTVVGQGTVAAIKQDKESLIAPFLTGT---ATLRERPVLtddalwKKGALAIEVAH 513
Cdd:PRK00349 548 EHDEDTIRAADYIVDIGPGAGVHGGEVVASGTPEEIMKNPNSLTGQYLSGKkkiEVPKERRKG------NGKFLKLKGAR 621
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 514 HFNIQDITARIPKNRFTTVTGMSGAGKTTLVLDSLIPAL---IATAKKRPLP-THVKAFDngHIRHVVTVDSVPVGKNVR 589
Cdd:PRK00349 622 ENNLKNVDVEIPLGKFTCVTGVSGSGKSTLINETLYKALarkLNGAKKVPGKhKEIEGLE--HLDKVIDIDQSPIGRTPR 699
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 590 STVATYTNILDHLRQLFAATPAAQANGWTASQFSYNVAAGACPTCGGTGQISLDVQYLPDITEVCPQCHGKRYNKQTLTV 669
Cdd:PRK00349 700 SNPATYTGVFDPIRELFAGTPEAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEV 779
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 670 KWHGYSIADILDLAVDEALPIFKAQSAIANTLQILHDMGLGYLLLGESTPALSGGEAQRLKLTSRIGKRQTG-TLFVFDE 748
Cdd:PRK00349 780 KYKGKNIADVLDMTVEEALEFFEAIPKIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELSKRSTGkTLYILDE 859
                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 749 PSVGLHPLDIQQLVKVFDQLIQQGATVIAIEHDLDVIANADYVIDMGPAGGINGGNIVATGTPLAVSQNPTSVTGQYLKT 828
Cdd:PRK00349 860 PTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVATGTPEEVAKVEASYTGRYLKP 939

                 ...
gi 835833681 829 HLA 831
Cdd:PRK00349 940 VLE 942
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
10-815 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: 721.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681   10 IQVRGAHVNNLKNIDIDIPLNEFVAITGRSGSGKSSLAMGVLYAEGARRYLNALSTFTRRRINQVGKASVDSVQYLPSAL 89
Cdd:TIGR00630   2 IIVRGAREHNLKNIDVEIPRDKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGVMDKPDVDSIEGLSPAI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681   90 ALRQRPQVPGVRSTVGTMSESLNILRLAFSRLSSAVCPNGHR----------------MPP------------------- 134
Cdd:TIGR00630  82 SIDQKTTSHNPRSTVGTITEIYDYLRLLFARVGTPYCPTCGRpisrqtpsqivdqilaLPEgtrvillapivrgrkgefr 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  135 -TLDVAENDGYV-------------------------------------------------------------------- 145
Cdd:TIGR00630 162 kLLEKLRKQGFArvrvdgevypledppkleknkkhtidvvidrltvknenrsrlaesvetalrlgdgllevefdddeeva 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  146 -----------TCPTCGAKFRAPGAEDFAFNSG-GACPTCGGLGQVRQIDPALIIADENQTIEEGAVASWHLPGRNF--- 210
Cdd:TIGR00630 242 eskeelfsekfACPECGFSLPELEPRLFSFNSPyGACPECSGLGIKQEFDPELIIPDPLLSLNGGAIVPFKKSTTSYyrq 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  211 -MPIVAREIGIPIDIPYKDLSEADKTRVLHGPKQTVAINIPSAKGKIFHMDNAVYENAFAAVEDSMATTKNERAITRLNR 289
Cdd:TIGR00630 322 mFASLAEHLGFDLDTPWKDLPEEAQKAILYGSGEEVIVVKYRNGGGETFRYHKPFEGVIPELERRYLETESESMREYLEK 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  290 FYKFDTCPDCHGSRFNPQLFNYELNGQNIATVSDMTVAALHDFAATIvpWLPTKMHHLGQSLVDELLLSLQPMEELGLDY 369
Cdd:TIGR00630 402 FMSERPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFNQL--TLTPEEKKIAEEVLKEIRERLGFLIDVGLDY 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  370 LTLSRPGATLSTGELQRIQLGRTLRSTTTGVLYVLDEPSVGLHPANVAGLIKAFRGLVAQGNSVVVVDHDTSIISAADDV 449
Cdd:TIGR00630 480 LSLSRAAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYV 559
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  450 IEIGPGAGKHGGTVVGQGTVAAIKQDKESLIAPFLTGTATL----RERPVLtddalwkKGALAIEVAHHFNIQDITARIP 525
Cdd:TIGR00630 560 IDIGPGAGEHGGEVVASGTPEEILANPDSLTGQYLSGRKKIevpaERRPGN-------GKFLTLKGARENNLKNITVSIP 632
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  526 KNRFTTVTGMSGAGKTTLVLDSLIPAL---IATAKKRPLPtHVKAFDNGHIRHVVTVDSVPVGKNVRSTVATYTNILDHL 602
Cdd:TIGR00630 633 LGLFTCITGVSGSGKSTLINDTLYPALanrLNGAKTVPGR-YTSIEGLEHLDKVIHIDQSPIGRTPRSNPATYTGVFDEI 711
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  603 RQLFAATPAAQANGWTASQFSYNVAAGACPTCGGTGQISLDVQYLPDITEVCPQCHGKRYNKQTLTVKWHGYSIADILDL 682
Cdd:TIGR00630 712 RELFAETPEAKVRGYTPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDM 791
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  683 AVDEALPIFKAQSAIANTLQILHDMGLGYLLLGESTPALSGGEAQRLKLTSRIGKRQTG-TLFVFDEPSVGLHPLDIQQL 761
Cdd:TIGR00630 792 TVEEAYEFFEAVPSISRKLQTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKRSTGrTLYILDEPTTGLHFDDIKKL 871
                         890       900       910       920       930
                  ....*....|....*....|....*....|....*....|....*....|....
gi 835833681  762 VKVFDQLIQQGATVIAIEHDLDVIANADYVIDMGPAGGINGGNIVATGTPLAVS 815
Cdd:TIGR00630 872 LEVLQRLVDKGNTVVVIEHNLDVIKTADYIIDLGPEGGDGGGTVVASGTPEEVA 925
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
507-811 7.36e-96

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: 300.30  E-value: 7.36e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 507 LAIEVAHHFNIQDITARIPKNRFTTVTGMSGAGKTTLVLDSLIPAL--IATAKKRPLPTHVKAFDNGHIRHVVTVDSVPV 584
Cdd:cd03271    1 LTLKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPALarRLHLKKEQPGNHDRIEGLEHIDKVIVIDQSPI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 585 GKNVRSTVATYTNILDHLRQLFaatpaaqangwtasqfsynvaagacptcggtgqisldvqylpditevCPQCHGKRYNK 664
Cdd:cd03271   81 GRTPRSNPATYTGVFDEIRELF-----------------------------------------------CEVCKGKRYNR 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 665 QTLTVKWHGYSIADILDLAVDEALPIFKAQSAIANTLQILHDMGLGYLLLGESTPALSGGEAQRLKLTSRIGKRQTG-TL 743
Cdd:cd03271  114 ETLEVRYKGKSIADVLDMTVEEALEFFENIPKIARKLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRSTGkTL 193
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 835833681 744 FVFDEPSVGLHPLDIQQLVKVFDQLIQQGATVIAIEHDLDVIANADYVIDMGPAGGINGGNIVATGTP 811
Cdd:cd03271  194 YILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLGPEGGDGGGQVVASGTP 261
UvrA_DNA-bind pfam17755
UvrA DNA-binding domain;
183-289 6.05e-14

UvrA DNA-binding domain;


Pssm-ID: 465484 [Multi-domain]  Cd Length: 110  Bit Score: 68.65  E-value: 6.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  183 DPALIIADENQTIEEGAVASWHLPGRNF----MPIVAREIGIPIDIPYKDLSEADKTRVLHGPKQTVAINIPSAKGKIFH 258
Cdd:pfam17755   1 DPDLVIPDPSLSLAEGAIAPWGKKRSSYyfqlLEALAKHYGFDLDTPFKDLPEEQQDIILYGSGEEIIVFYYSRGGRTRT 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 835833681  259 MdNAVYENAFAAVEDSMATTKNERAITRLNR 289
Cdd:pfam17755  81 Y-TKPFEGVIPNLERRYRETDSESVREELEK 110
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
713-794 1.13e-06

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 49.92  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 713 LLGESTPALSGGEAQRLkLTSRiGKRQTGTLFVFDEPSVGLHPLDIQQLVKVFDQLIQQGATVIAIEHDLDVIANADYVI 792
Cdd:NF040873 112 LAGRQLGELSGGQRQRA-LLAQ-GLAQEADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCV 189

                 ..
gi 835833681 793 DM 794
Cdd:NF040873 190 LL 191
 
Name Accession Description Interval E-value
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
9-831 0e+00

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


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 855.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681   9 HIQVRGAHVNNLKNIDIDIPLNEFVAITGRSGSGKSSLAMGVLYAEGARRYLNALSTFTRRRINQVGKASVDSVQYLPSA 88
Cdd:COG0178    5 KIRIRGAREHNLKNIDVDIPRNKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLSPA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  89 LALRQRPQVPGVRSTVGTMSEslnI---LRLAFSRLSSAVCPN----------------------GHRM----------- 132
Cdd:COG0178   85 ISIEQKTTSRNPRSTVGTVTE---IydyLRLLFARVGTPHCPIcgrpvekqtvdqivdrilalpeGTRLqilapvvrgrk 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 133 -----------------------------PPTLD---------------VAEN----------------DGYVT------ 146
Cdd:COG0178  162 gehkelleelrkqgfvrvrvdgevydldeEPELDknkkhtievvvdrlvVKEDirsrladsvetalklgDGLVIvevvde 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 147 -----------CPTCGAKFRAPGAEDFAFNSG-GACPTCGGLGQVRQIDPALIIADENQTIEEGAVASWHLPGRNFMP-- 212
Cdd:COG0178  242 geellfsekfaCPDCGISFEELEPRLFSFNSPyGACPTCDGLGRVLEFDPDLVIPDPSLSLAEGAIAPWSGPSSSYYFql 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 213 --IVAREIGIPIDIPYKDLSEADKTRVLHGPKQTVAINIPSAKGKifHMDNAVYENAFAAVEDSMATTKNERAITRLNRF 290
Cdd:COG0178  322 leALAKHYGFDLDTPWKDLPEEQRDLILYGSDEKIKFRYKNRGRR--RTYEKPFEGVIPFLERRYRETYSEHVREELSRY 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 291 YKFDTCPDCHGSRFNPQLFNYELNGQNIATVSDMTVAALHDFAATIVpwLPTKMHHLGQSLVDELLLSLQPMEELGLDYL 370
Cdd:COG0178  400 MSETPCPACKGARLKPEALAVKIGGKNIAELTALSIDEALEFFENLE--LTEREAEIAERILKEIRSRLGFLVDVGLDYL 477
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 371 TLSRPGATLSTGELQRIQLGRTLRSTTTGVLYVLDEPSVGLHPANVAGLIKAFRGLVAQGNSVVVVDHDTSIISAADDVI 450
Cdd:COG0178  478 TLDRSAGTLSGGEAQRIRLATQIGSGLVGVLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDTIRAADYII 557
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 451 EIGPGAGKHGGTVVGQGTVAAIKQDKESLIAPFLTGT---ATLRERPVltddalWKKGALAIEVAHHFNIQDITARIPKN 527
Cdd:COG0178  558 DIGPGAGEHGGEVVAQGTPEEILKNPDSLTGQYLSGRkriPVPKKRRK------GNGKFLTIKGARENNLKNVDVEIPLG 631
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 528 RFTTVTGMSGAGKTTLVLDSLIPAL---IATAKKRPLP-THVKAFDngHIRHVVTVDSVPVGKNVRSTVATYTNILDHLR 603
Cdd:COG0178  632 VLTCVTGVSGSGKSTLVNDILYPALarkLNGAKEKPGPhDSIEGLE--HIDKVIDIDQSPIGRTPRSNPATYTGVFDPIR 709
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 604 QLFAATPAAQANGWTASQFSYNVAAGACPTCGGTGQISLDVQYLPDITEVCPQCHGKRYNKQTLTVKWHGYSIADILDLA 683
Cdd:COG0178  710 ELFAQTPEAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMT 789
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 684 VDEALPIFKAQSAIANTLQILHDMGLGYLLLGESTPALSGGEAQRLKLTSRIGKRQTG-TLFVFDEPSVGLHPLDIQQLV 762
Cdd:COG0178  790 VEEALEFFENIPKIARKLQTLQDVGLGYIKLGQPATTLSGGEAQRVKLASELSKRSTGkTLYILDEPTTGLHFHDIRKLL 869
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 835833681 763 KVFDQLIQQGATVIAIEHDLDVIANADYVIDMGPAGGINGGNIVATGTPLAVSQNPTSVTGQYLKTHLA 831
Cdd:COG0178  870 EVLHRLVDKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVAEGTPEEVAKVKASYTGRYLKEYLE 938
uvrA PRK00349
excinuclease ABC subunit UvrA;
9-831 0e+00

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 747.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681   9 HIQVRGAHVNNLKNIDIDIPLNEFVAITGRSGSGKSSLAMGVLYAEGARRYLNALSTFTRRRINQVGKASVDSVQYLPSA 88
Cdd:PRK00349   5 KIIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLSPA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  89 LALRQR-----PqvpgvRSTVGTMSESLNILRLAFSRLSSAVCPNGHR---------M---------------------- 132
Cdd:PRK00349  85 ISIDQKttshnP-----RSTVGTVTEIYDYLRLLYARVGKPHCPNCGRpieaqtvsqMvdrvlelpegtrlqilapvvrg 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 133 -------------------------------PPTLD---------------VAEN----------------DGYVT---- 146
Cdd:PRK00349 160 rkgehkkllenlrkqgfvrvrvdgevydldePPKLDknkkhtievvvdrlvVKEDirqrladsietalklsDGLVVvevm 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 147 ---------------CPTCGAKF-----RApgaedFAFNSG-GACPTCGGLGQVRQIDPALIIADENQTIEEGAVASWHL 205
Cdd:PRK00349 240 ddpeaeellfsekfaCPVCGFSIpelepRL-----FSFNSPyGACPTCDGLGVKLEFDPDLVVPDPELSLAEGAIAPWSR 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 206 PGRNFMP----IVAREIGIPIDIPYKDLSEADKTRVLHG-PKQTVAINIPSAKGKIFHMdNAVYENAFAAVEDSMATTKN 280
Cdd:PRK00349 315 SSSSYYFqmlkSLAEHYGFDLDTPWKDLPEEVQDIILYGsGDEEIEFRYKNDRGRTRER-KHPFEGVIPNLERRYRETES 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 281 ERAITRLNRFYKFDTCPDCHGSRFNPQLFNYELNGQNIATVSDMTVAALHDFAATIVpwLPTKMHHLGQSLVDELLLSLQ 360
Cdd:PRK00349 394 EYVREELEKYMSERPCPSCKGKRLKPEALAVKVGGKNIGEVSELSIGEALEFFENLK--LSEQEAKIAEPILKEIRERLK 471
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 361 PMEELGLDYLTLSRPGATLSTGELQRI----QLGRTLrsttTGVLYVLDEPSVGLHPANVAGLIKAFRGLVAQGNSVVVV 436
Cdd:PRK00349 472 FLVDVGLDYLTLSRSAGTLSGGEAQRIrlatQIGSGL----TGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVV 547
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 437 DHDTSIISAADDVIEIGPGAGKHGGTVVGQGTVAAIKQDKESLIAPFLTGT---ATLRERPVLtddalwKKGALAIEVAH 513
Cdd:PRK00349 548 EHDEDTIRAADYIVDIGPGAGVHGGEVVASGTPEEIMKNPNSLTGQYLSGKkkiEVPKERRKG------NGKFLKLKGAR 621
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 514 HFNIQDITARIPKNRFTTVTGMSGAGKTTLVLDSLIPAL---IATAKKRPLP-THVKAFDngHIRHVVTVDSVPVGKNVR 589
Cdd:PRK00349 622 ENNLKNVDVEIPLGKFTCVTGVSGSGKSTLINETLYKALarkLNGAKKVPGKhKEIEGLE--HLDKVIDIDQSPIGRTPR 699
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 590 STVATYTNILDHLRQLFAATPAAQANGWTASQFSYNVAAGACPTCGGTGQISLDVQYLPDITEVCPQCHGKRYNKQTLTV 669
Cdd:PRK00349 700 SNPATYTGVFDPIRELFAGTPEAKARGYKPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEV 779
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 670 KWHGYSIADILDLAVDEALPIFKAQSAIANTLQILHDMGLGYLLLGESTPALSGGEAQRLKLTSRIGKRQTG-TLFVFDE 748
Cdd:PRK00349 780 KYKGKNIADVLDMTVEEALEFFEAIPKIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELSKRSTGkTLYILDE 859
                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 749 PSVGLHPLDIQQLVKVFDQLIQQGATVIAIEHDLDVIANADYVIDMGPAGGINGGNIVATGTPLAVSQNPTSVTGQYLKT 828
Cdd:PRK00349 860 PTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVATGTPEEVAKVEASYTGRYLKP 939

                 ...
gi 835833681 829 HLA 831
Cdd:PRK00349 940 VLE 942
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
10-815 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: 721.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681   10 IQVRGAHVNNLKNIDIDIPLNEFVAITGRSGSGKSSLAMGVLYAEGARRYLNALSTFTRRRINQVGKASVDSVQYLPSAL 89
Cdd:TIGR00630   2 IIVRGAREHNLKNIDVEIPRDKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGVMDKPDVDSIEGLSPAI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681   90 ALRQRPQVPGVRSTVGTMSESLNILRLAFSRLSSAVCPNGHR----------------MPP------------------- 134
Cdd:TIGR00630  82 SIDQKTTSHNPRSTVGTITEIYDYLRLLFARVGTPYCPTCGRpisrqtpsqivdqilaLPEgtrvillapivrgrkgefr 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  135 -TLDVAENDGYV-------------------------------------------------------------------- 145
Cdd:TIGR00630 162 kLLEKLRKQGFArvrvdgevypledppkleknkkhtidvvidrltvknenrsrlaesvetalrlgdgllevefdddeeva 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  146 -----------TCPTCGAKFRAPGAEDFAFNSG-GACPTCGGLGQVRQIDPALIIADENQTIEEGAVASWHLPGRNF--- 210
Cdd:TIGR00630 242 eskeelfsekfACPECGFSLPELEPRLFSFNSPyGACPECSGLGIKQEFDPELIIPDPLLSLNGGAIVPFKKSTTSYyrq 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  211 -MPIVAREIGIPIDIPYKDLSEADKTRVLHGPKQTVAINIPSAKGKIFHMDNAVYENAFAAVEDSMATTKNERAITRLNR 289
Cdd:TIGR00630 322 mFASLAEHLGFDLDTPWKDLPEEAQKAILYGSGEEVIVVKYRNGGGETFRYHKPFEGVIPELERRYLETESESMREYLEK 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  290 FYKFDTCPDCHGSRFNPQLFNYELNGQNIATVSDMTVAALHDFAATIvpWLPTKMHHLGQSLVDELLLSLQPMEELGLDY 369
Cdd:TIGR00630 402 FMSERPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFNQL--TLTPEEKKIAEEVLKEIRERLGFLIDVGLDY 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  370 LTLSRPGATLSTGELQRIQLGRTLRSTTTGVLYVLDEPSVGLHPANVAGLIKAFRGLVAQGNSVVVVDHDTSIISAADDV 449
Cdd:TIGR00630 480 LSLSRAAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYV 559
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  450 IEIGPGAGKHGGTVVGQGTVAAIKQDKESLIAPFLTGTATL----RERPVLtddalwkKGALAIEVAHHFNIQDITARIP 525
Cdd:TIGR00630 560 IDIGPGAGEHGGEVVASGTPEEILANPDSLTGQYLSGRKKIevpaERRPGN-------GKFLTLKGARENNLKNITVSIP 632
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  526 KNRFTTVTGMSGAGKTTLVLDSLIPAL---IATAKKRPLPtHVKAFDNGHIRHVVTVDSVPVGKNVRSTVATYTNILDHL 602
Cdd:TIGR00630 633 LGLFTCITGVSGSGKSTLINDTLYPALanrLNGAKTVPGR-YTSIEGLEHLDKVIHIDQSPIGRTPRSNPATYTGVFDEI 711
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  603 RQLFAATPAAQANGWTASQFSYNVAAGACPTCGGTGQISLDVQYLPDITEVCPQCHGKRYNKQTLTVKWHGYSIADILDL 682
Cdd:TIGR00630 712 RELFAETPEAKVRGYTPGRFSFNVKGGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDM 791
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  683 AVDEALPIFKAQSAIANTLQILHDMGLGYLLLGESTPALSGGEAQRLKLTSRIGKRQTG-TLFVFDEPSVGLHPLDIQQL 761
Cdd:TIGR00630 792 TVEEAYEFFEAVPSISRKLQTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKRSTGrTLYILDEPTTGLHFDDIKKL 871
                         890       900       910       920       930
                  ....*....|....*....|....*....|....*....|....*....|....
gi 835833681  762 VKVFDQLIQQGATVIAIEHDLDVIANADYVIDMGPAGGINGGNIVATGTPLAVS 815
Cdd:TIGR00630 872 LEVLQRLVDKGNTVVVIEHNLDVIKTADYIIDLGPEGGDGGGTVVASGTPEEVA 925
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
1-835 6.04e-124

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 410.37  E-value: 6.04e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681    1 MPqtTLPTHIQvrGAHVNNLKNIDIDIPLNEFVAITGRSGSGKSSLAMGVLYAEGARRYLNALSTFTRRRINQVGKASVD 80
Cdd:PRK00635    1 MP--SLPVRLS--GITVRNLKNISIEFCPREIVLLTGVSGSGKSSLAFDTIYAAGRKRYLSTLPSFFATTLDSLPDPSVE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681   81 SVQYLPSALALRQRPQVPGVRSTVGTMSESLNILRLAFSR---------------------------------------- 120
Cdd:PRK00635   77 KIEGLSPTIAVKQNHFSQHSHATVGSTTELNSHLALLFSLegqardpvtlhpltlyskekilstiaaipdgtqitllapl 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  121 -------------------------------LSSAV---CP-------------NGHRMPPTLDVAENDGYVTC------ 147
Cdd:PRK00635  157 pakdilaireclrqgftkvridgeispiykfLTSGIpedVPvdivvdtliknesNTARLKVSLFTALDIGHGECslhfdn 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  148 -------------------PTCGAKFRAPGAEDfafnsggACPTCGGLG-QVRQIDPALIiaDENQTIEE------GAVA 201
Cdd:PRK00635  237 qkrtfstqatipetqqtytPLTPQLFSPHSLED-------RCPQCQGSGiFISIDDPSLI--QQNLSIEEnccpfaGNCS 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  202 SWHLpgRNFMPIVAREIGIPIDIPYKDLSEADKTRVLHGPKQTVainIP-----SAKGKIfHMDNAVYENAFAAVEDSMA 276
Cdd:PRK00635  308 TYLY--HTIYQSLADSLGFSLSTPWKDLSPEIQNIFLYGKEGLV---LPvrlfdGTLGKK-TLTHKVWRGVLNEIGEKVR 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  277 -TTKNERAITRLNRFYkfdTCPDCHGSRFNPQLFNYELNGQNIATVSDMTVAALHDFAATIVPWLPTkMHHLGQSLVDEL 355
Cdd:PRK00635  382 ySNKPSRYLPKGTSAT---SCPRCQGTGLGDYANAATWHGKTFAEFQQMSLQELFIFLSQLPSKSLS-IEEVLQGLKSRL 457
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  356 LLSLQpmeeLGLDYLTLSRPGATLSTGELQRIQLGRTLRSTTTGVLYVLDEPSVGLHPANVAGLIKAFRGLVAQGNSVVV 435
Cdd:PRK00635  458 SILID----LGLPYLTPERALATLSGGEQERTALAKHLGAELIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLL 533
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  436 VDHDTSIISAADDVIEIGPGAGKHGGTVVGQGTVAAIKQDKESLIAPFLTGTATL-----RERPvltddalwkKGALAIE 510
Cdd:PRK00635  534 VEHDEQMISLADRIIDIGPGAGIFGGEVLFNGSPREFLAKSDSLTAKYLRQELTIpipekRTNS---------LGTLTLS 604
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  511 VAHHFNIQDITARIPKNRFTTVTGMSGAGKTTLVLDSLIPALIATAKKRPLPThvKAFDNGHIRHVVTVDSVPVGKNVRS 590
Cdd:PRK00635  605 KATKHNLKDLTISLPLGRLTVVTGVSGSGKSSLINDTLVPAVEEFIEQGFCSN--LSIQWGAISRLVHITRDLPGRSQRS 682
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  591 TVATYTNILDHLRQLFAATPAAQANGWTASQFSYNVAAGACPTCGGTGQISLDVQYLPdITevCPQCHGKRYNKQTLTVK 670
Cdd:PRK00635  683 IPLTYIKAFDDLRELFAEQPRSKRLGLTKSHFSFNTPLGACAECQGLGSITTTDNRTS-IP--CPSCLGKRFLPQVLEVR 759
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  671 WHGYSIADILDLAVDEALPIFKAQSAIANTLQILHDMGLGYLLLGESTPALSGGEAQRLKLTSRI---GKRQtgTLFVFD 747
Cdd:PRK00635  760 YKGKNIADILEMTAYEAEKFFLDEPSIHEKIHALCSLGLDYLPLGRPLSSLSGGEIQRLKLAYELlapSKKP--TLYVLD 837
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  748 EPSVGLHPLDIQQLVKVFDQLIQQGATVIAIEHDLDVIANADYVIDMGPAGGINGGNIVATGTP--LAVSQNPTSVTGQ- 824
Cdd:PRK00635  838 EPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLELGPEGGNLGGYLLASCSPeeLIHLHTPTAKALRp 917
                         970
                  ....*....|.
gi 835833681  825 YLKTHLALFHV 835
Cdd:PRK00635  918 YLSSPQELPYL 928
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
507-811 7.36e-96

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: 300.30  E-value: 7.36e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 507 LAIEVAHHFNIQDITARIPKNRFTTVTGMSGAGKTTLVLDSLIPAL--IATAKKRPLPTHVKAFDNGHIRHVVTVDSVPV 584
Cdd:cd03271    1 LTLKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPALarRLHLKKEQPGNHDRIEGLEHIDKVIVIDQSPI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 585 GKNVRSTVATYTNILDHLRQLFaatpaaqangwtasqfsynvaagacptcggtgqisldvqylpditevCPQCHGKRYNK 664
Cdd:cd03271   81 GRTPRSNPATYTGVFDEIRELF-----------------------------------------------CEVCKGKRYNR 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 665 QTLTVKWHGYSIADILDLAVDEALPIFKAQSAIANTLQILHDMGLGYLLLGESTPALSGGEAQRLKLTSRIGKRQTG-TL 743
Cdd:cd03271  114 ETLEVRYKGKSIADVLDMTVEEALEFFENIPKIARKLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRSTGkTL 193
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 835833681 744 FVFDEPSVGLHPLDIQQLVKVFDQLIQQGATVIAIEHDLDVIANADYVIDMGPAGGINGGNIVATGTP 811
Cdd:cd03271  194 YILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLGPEGGDGGGQVVASGTP 261
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
2-830 6.48e-78

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 276.32  E-value: 6.48e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681    2 PQTTLPTHIQVRGAHVNNLKNIDIDIPLNEFVAITGRSGSGKSSLAMGVLYAEGARRYLNALSTFTRRR-INQVGKASVD 80
Cdd:PRK00635  933 PKPPVPADITIKNAYQHNLKHIDLSLPRNALTAVTGPSASGKHSLVFDILYAAGNIAYAELFPPYIRQAlIKKTPLPSVD 1012
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681   81 SVQYLPSALALRQRPQVPGVRSTVGTMSESLNILRLAFSRLSSAVCP-NGHRM----PPTLdVAE-----NDGYVTCPtc 150
Cdd:PRK00635 1013 KVTGLSPVIAIEKTSASKNSNHSVASALEISNGLEKLFARLGHPYSPlSGDALrkitPQTI-AEEllthyTKGYVTIT-- 1089
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  151 gAKFraPGAEDF----------------------------------------------------------AF-------- 164
Cdd:PRK00635 1090 -SPI--PKEEDLfiylqeklkegflklyaneqfydldeplptslenpaiviqhtkiseknlssllssltlAFslsssicl 1166
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  165 ------------------------------------NSGGACPTCGGLGQVRQIDpalIIADENQTIEEGAVASWHL--P 206
Cdd:PRK00635 1167 hieyagtslsltyrlgwqdssgnlypnittpllsrdHEEGLCPLCHGKGFILKCS---LLPHKEKIAHYTPLSLFTLffP 1243
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  207 GRNFMPIVA--REIGIPIDIPYKDLSEADKTRVLHGPKQTVAINipsakgkifhmdnavyenafAAVEDSMATTKNERAI 284
Cdd:PRK00635 1244 NQDPKPVYPllKELGIPSIALFQELDTLSFESLCLGTQQHPGLN--------------------ALLMEAMLMESEEPLP 1303
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  285 TRLnrfYKFDTCPDCHGSRFNPQLFNYELNGQNIATVSDMTVAALHDFAATIvpwlptkmhHLGQ--SLVDELLLSLQPM 362
Cdd:PRK00635 1304 PPL---ISKTPCNQCQGLGVYTYAHCVRIHNTSLSDIYQEDVTFLKKFLLTI---------HDDEepSIIQDLLNRLTFI 1371
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  363 EELGLDYLTLSRPGATLSTGELQRIQLGRTLRSTTTGVLYVLDEPSVGLHPANVAGLIKAFRGLVAQGNSVVVVDHDTSI 442
Cdd:PRK00635 1372 DKVGLSYITLGQEQDTLSDGEHYRLHLAKKISSNLTDIIYLLEDPLSGLHPQDAPTLLQLIKELVTNNNTVIATDRSGSL 1451
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  443 ISAADDVIEIGPGAGKHGGtvvgqgtvaaikqdkesliapFLTGTATLR-ERPVLTDDALWKKGA-LAIEVAHHfNIQDI 520
Cdd:PRK00635 1452 AEHADHLIHLGPGSGPQGG---------------------YLLSTSALKqSQPDLHNTRSSEETPtLSVSLSIH-TIQNL 1509
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  521 TARIPKNRFTTVTGMSGAGKTTLVLDSLIP---ALIATakkrplpthvkafDNGHIRHVVTVDSVPVGKNVRSTVATYTN 597
Cdd:PRK00635 1510 NVSAPLHSLVAISGVSGSGKTSLLLEGFYKqacALIEK-------------GPSVFSEIIFLDSHPQISSQRSDISTYFD 1576
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  598 ILDHLRQLFAATPAAQANGWTASQFSYNVAAGACPTCGGTGQISLDVQYLPDITEVCPQCHGKRYNKQTLTVKWHGYSIA 677
Cdd:PRK00635 1577 IAPSLRNFYASLTQAKALNISASMFSTNTKQGQCSDCWGLGYQWIDRAFYALEKRPCPTCSGFRIQPLAQEVVYEGKHFG 1656
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  678 DILDLAVDEALPIFKAQSAIANTLQILHDMGLGYLLLGESTPALSGGEAQRLKLTSRIG-KRQTGTLFVFDEPSVGLHPL 756
Cdd:PRK00635 1657 QLLQTPIEEVAETFPFLKKIQKPLQALIDNGLGYLPLGQNLSSLSLSEKIAIKIAKFLYlPPKHPTLFLLDEIATSLDNQ 1736
                         890       900       910       920       930       940       950
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 835833681  757 DIQQLVKVFDQLIQQGATVIAIEHDLDVIANADYVIDMGPAGGINGGNIVATGTPlavsQNPTSVTGQYLKTHL 830
Cdd:PRK00635 1737 QKSALLVQLRTLVSLGHSVIYIDHDPALLKQADYLIEMGPGSGKTGGKILFSGPP----KDISASKDSLLKTYM 1806
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
645-826 1.29e-55

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: 207.17  E-value: 1.29e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  645 QYLPDITE--VCPQCHGKRYNKQTLTVKWHGYSIADILDLAVDEA--------LPIFKAQSA------IANTLQILHDMG 708
Cdd:TIGR00630 397 EYLEKFMSerPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAheffnqltLTPEEKKIAeevlkeIRERLGFLIDVG 476
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  709 LGYLLLGESTPALSGGEAQRLKLTSRIGKRQTGTLFVFDEPSVGLHPLDIQQLVKVFDQLIQQGATVIAIEHDLDVIANA 788
Cdd:TIGR00630 477 LDYLSLSRAAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAA 556
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 835833681  789 DYVIDMGPAGGINGGNIVATGTPLAVSQNPTSVTGQYL 826
Cdd:TIGR00630 557 DYVIDIGPGAGEHGGEVVASGTPEEILANPDSLTGQYL 594
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
295-810 3.29e-52

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 198.51  E-value: 3.29e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  295 TCPDCHGSRFNPQLFNYELNGQNIATVSDMTVAALHDFAATiVPWLPTKMHHLGQslvdelllslqpmeeLGLDYLTLSR 374
Cdd:PRK00635  742 PCPSCLGKRFLPQVLEVRYKGKNIADILEMTAYEAEKFFLD-EPSIHEKIHALCS---------------LGLDYLPLGR 805
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  375 PGATLSTGELQRIQLGRTLRSTTTG-VLYVLDEPSVGLHPANVAGLIKAFRGLVAQGNSVVVVDHDTSIISAADDVIEIG 453
Cdd:PRK00635  806 PLSSLSGGEIQRLKLAYELLAPSKKpTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLELG 885
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  454 PGAGKHGGTVVGQGTVAA-IKQDKESLIA--PFLTGTATLrerPVLTDDA--LWKKGALAIEVAHHFNIQDITARIPKNR 528
Cdd:PRK00635  886 PEGGNLGGYLLASCSPEElIHLHTPTAKAlrPYLSSPQEL---PYLPDPSpkPPVPADITIKNAYQHNLKHIDLSLPRNA 962
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  529 FTTVTGMSGAGKTTLVLD-----------SLIPALIATA--KKRPLPT--HVKAfdnghIRHVVTVDSVPVGKNVRSTVA 593
Cdd:PRK00635  963 LTAVTGPSASGKHSLVFDilyaagniayaELFPPYIRQAliKKTPLPSvdKVTG-----LSPVIAIEKTSASKNSNHSVA 1037
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  594 TYTNILDHLRQLFA----------------ATPAAQAN------------------------------------------ 615
Cdd:PRK00635 1038 SALEISNGLEKLFArlghpysplsgdalrkITPQTIAEellthytkgyvtitspipkeedlfiylqeklkegflklyane 1117
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  616 ----------------------------------------------------------------GW-----------TAS 620
Cdd:PRK00635 1118 qfydldeplptslenpaiviqhtkiseknlssllssltlafslsssiclhieyagtslsltyrlGWqdssgnlypniTTP 1197
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  621 QFSYNVAAGACPTCGGTGQI------------------SLDVQYLPD--------------------------------- 649
Cdd:PRK00635 1198 LLSRDHEEGLCPLCHGKGFIlkcsllphkekiahytplSLFTLFFPNqdpkpvypllkelgipsialfqeldtlsfeslc 1277
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  650 ------------------------------ITEVCPQCHGKRYNKQTLTVKWHGYSIADI------------LDLAVDEA 687
Cdd:PRK00635 1278 lgtqqhpglnallmeamlmeseeplpppliSKTPCNQCQGLGVYTYAHCVRIHNTSLSDIyqedvtflkkflLTIHDDEE 1357
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  688 LPIFkaqSAIANTLQILHDMGLGYLLLGESTPALSGGEAQRLKLTSRIGKRQTGTLFVFDEPSVGLHPLDIQQLVKVFDQ 767
Cdd:PRK00635 1358 PSII---QDLLNRLTFIDKVGLSYITLGQEQDTLSDGEHYRLHLAKKISSNLTDIIYLLEDPLSGLHPQDAPTLLQLIKE 1434
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|...
gi 835833681  768 LIQQGATVIAIEHDLDVIANADYVIDMGPAGGINGGNIVATGT 810
Cdd:PRK00635 1435 LVTNNNTVIATDRSGSLAEHADHLIHLGPGSGPQGGYLLSTSA 1477
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
6-468 1.21e-50

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: 192.15  E-value: 1.21e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681    6 LPTHIQVRGAHVNNLKNIDIDIPLNEFVAITGRSGSGKSSLAMGVLYAEGARRYLNALSTFTRRRinqvgkaSVDSVQYL 85
Cdd:TIGR00630 610 NGKFLTLKGARENNLKNITVSIPLGLFTCITGVSGSGKSTLINDTLYPALANRLNGAKTVPGRYT-------SIEGLEHL 682
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681   86 PSALALRQRPQVPGVRSTVGTMSESLNILRLAFSRlssavcpnghrmpptldvaendgyvtcpTCGAKFRAPGAEDFAFN 165
Cdd:TIGR00630 683 DKVIHIDQSPIGRTPRSNPATYTGVFDEIRELFAE----------------------------TPEAKVRGYTPGRFSFN 734
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  166 -SGGACPTCGGLGQVrqidpaliiadenqTIEEgavaswhlpgrNFMPIVareigipidipykdlseadktrvlhgpkqt 244
Cdd:TIGR00630 735 vKGGRCEACQGDGVI--------------KIEM-----------HFLPDV------------------------------ 759
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  245 vainipsakgkifhmdnavyenafaavedsmattkneraitrlnrfykFDTCPDCHGSRFNPQLFNYELNGQNIATVSDM 324
Cdd:TIGR00630 760 ------------------------------------------------YVPCEVCKGKRYNRETLEVKYKGKNIADVLDM 791
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  325 TVAALHDFAATIvpwlpTKMHHLGQSLVDelllslqpmeeLGLDYLTLSRPGATLSTGELQRIQLGRTLRSTTTG-VLYV 403
Cdd:TIGR00630 792 TVEEAYEFFEAV-----PSISRKLQTLCD-----------VGLGYIRLGQPATTLSGGEAQRIKLAKELSKRSTGrTLYI 855
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 835833681  404 LDEPSVGLHPANVAGLIKAFRGLVAQGNSVVVVDHDTSIISAADDVIEIGPGAGKHGGTVVGQGT 468
Cdd:TIGR00630 856 LDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKTADYIIDLGPEGGDGGGTVVASGT 920
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
516-809 1.62e-48

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: 171.29  E-value: 1.62e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 516 NIQDITARIPKNRFTTVTGMSGAGKTTLVLDSLIpaliATAKKRPLPTHVKAFDN--GHIRH-----------VVTVDSV 582
Cdd:cd03270   10 NLKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIY----AEGQRRYVESLSAYARQflGQMDKpdvdsieglspAIAIDQK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 583 PVGKNVRSTVATYTNILDHLRQLFAatpaaqangwtasqfsynvaagacptcggtgqisldvqylpditevcpqchgkry 662
Cdd:cd03270   86 TTSRNPRSTVGTVTEIYDYLRLLFA------------------------------------------------------- 110
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 663 nkqtltvkwhgysiadildlavdealpifkaQSAIANTLQILHDMGLGYLLLGESTPALSGGEAQRLKLTSRIGKRQTGT 742
Cdd:cd03270  111 -------------------------------RVGIRERLGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIGSGLTGV 159
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 835833681 743 LFVFDEPSVGLHPLDIQQLVKVFDQLIQQGATVIAIEHDLDVIANADYVIDMGPAGGINGGNIVATG 809
Cdd:cd03270  160 LYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDIGPGAGVHGGEIVAQG 226
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
296-468 5.36e-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: 165.48  E-value: 5.36e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 296 CPDCHGSRFNPQLFNYELNGQNIATVSDMTVAALHDFAATIvpwlpTKMHHLGQSLVDelllslqpmeeLGLDYLTLSRP 375
Cdd:cd03271  103 CEVCKGKRYNRETLEVRYKGKSIADVLDMTVEEALEFFENI-----PKIARKLQTLCD-----------VGLGYIKLGQP 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 376 GATLSTGELQRIQLGRTLRSTTTG-VLYVLDEPSVGLHPANVAGLIKAFRGLVAQGNSVVVVDHDTSIISAADDVIEIGP 454
Cdd:cd03271  167 ATTLSGGEAQRIKLAKELSKRSTGkTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLGP 246
                        170
                 ....*....|....
gi 835833681 455 GAGKHGGTVVGQGT 468
Cdd:cd03271  247 EGGDGGGQVVASGT 260
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
686-809 4.19e-42

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: 151.32  E-value: 4.19e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 686 EALPIFKAQSAIA-NTLQILHDMGLGYLLLGESTPALSGGEAQRLKLTSRIGKRQTGTLFVFDEPSVGLHPLDIQQLVKV 764
Cdd:cd03238   52 SFLPKFSRNKLIFiDQLQFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPGTLFILDEPSTGLHQQDINQLLEV 131
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 835833681 765 FDQLIQQGATVIAIEHDLDVIANADYVIDMGPAGGINGGNIVATG 809
Cdd:cd03238  132 IKGLIDLGNTVILIEHNLDVLSSADWIIDFGPGSGKSGGKVVFSG 176
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
359-467 2.42e-40

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: 148.17  E-value: 2.42e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 359 LQPMEELGLDYLTLSRPGATLSTGELQRIQLGRTLRSTTTGVLYVLDEPSVGLHPANVAGLIKAFRGLVAQGNSVVVVDH 438
Cdd:cd03270  118 LGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEH 197
                         90       100
                 ....*....|....*....|....*....
gi 835833681 439 DTSIISAADDVIEIGPGAGKHGGTVVGQG 467
Cdd:cd03270  198 DEDTIRAADHVIDIGPGAGVHGGEIVAQG 226
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
10-120 1.32e-38

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: 143.17  E-value: 1.32e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  10 IQVRGAHVNNLKNIDIDIPLNEFVAITGRSGSGKSSLAMGVLYAEGARRYLNALSTFTRRRINQVGKASVDSVQYLPSAL 89
Cdd:cd03270    1 IIVRGAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLSPAI 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 835833681  90 ALRQRPQVPGVRSTVGTMSESLNILRLAFSR 120
Cdd:cd03270   81 AIDQKTTSRNPRSTVGTVTEIYDYLRLLFAR 111
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
358-467 8.63e-36

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: 133.60  E-value: 8.63e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 358 SLQPMEELGLDYLTLSRPGATLSTGELQRIQLGRTLRSTTTGVLYVLDEPSVGLHPANVAGLIKAFRGLVAQGNSVVVVD 437
Cdd:cd03238   67 QLQFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIE 146
                         90       100       110
                 ....*....|....*....|....*....|
gi 835833681 438 HDTSIISAADDVIEIGPGAGKHGGTVVGQG 467
Cdd:cd03238  147 HNLDVLSSADWIIDFGPGSGKSGGKVVFSG 176
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
290-486 1.32e-15

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 81.80  E-value: 1.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  290 FYKFD--TCPDCHGSRFNP--QLFNYElnGQNIATVSDMTVAALhdfaATIVPWLpTKMHHLGQSLVDElllslqpmeel 365
Cdd:PRK00635 1625 FYALEkrPCPTCSGFRIQPlaQEVVYE--GKHFGQLLQTPIEEV----AETFPFL-KKIQKPLQALIDN----------- 1686
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  366 GLDYLTLSRPGATLSTGELQRIQLGRTLRST-TTGVLYVLDEPSVGLHPANVAGLIKAFRGLVAQGNSVVVVDHDTSIIS 444
Cdd:PRK00635 1687 GLGYLPLGQNLSSLSLSEKIAIKIAKFLYLPpKHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALLK 1766
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 835833681  445 AADDVIEIGPGAGKHGGTVVGQGTVAAIKQDKESLIAPFLTG 486
Cdd:PRK00635 1767 QADYLIEMGPGSGKTGGKILFSGPPKDISASKDSLLKTYMCN 1808
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
10-85 9.63e-15

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: 73.13  E-value: 9.63e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 835833681  10 IQVRGAHVNNLKNIDIDIPLNEFVAITGRSGSGKSSLAMGVLYAEGARRYLNALSTFTRRRInqvgkASVDSVQYL 85
Cdd:cd03238    1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKARLISFLPKFSRNKL-----IFIDQLQFL 71
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
517-814 2.70e-14

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


Pssm-ID: 440739 [Multi-domain]  Cd Length: 230  Bit Score: 73.14  E-value: 2.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 517 IQDITARIPKNRFTTVTGMSGAGKTTLVLdsLIPALIatakkRPlpthvkafDNGHIRhvvtVDSVPVGKNVRSTVATYT 596
Cdd:COG1122   17 LDDVSLSIEKGEFVAIIGPNGSGKSTLLR--LLNGLL-----KP--------TSGEVL----VDGKDITKKNLRELRRKV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 597 NIL----DHlrQLFAATpaaqangwtasqfsynVAAgacptcggtgqislDVQYLPditevcpqchgkrYNkqtltvkwH 672
Cdd:COG1122   78 GLVfqnpDD--QLFAPT----------------VEE--------------DVAFGP-------------EN--------L 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 673 GYSIADILDlAVDEALpifkaqsaiaNTLQILHdmglgylLLGESTPALSGGEAQRLKLTS------RIgkrqtgtlFVF 746
Cdd:COG1122  105 GLPREEIRE-RVEEAL----------ELVGLEH-------LADRPPHELSGGQKQRVAIAGvlamepEV--------LVL 158
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 835833681 747 DEPSVGLHPLDIQQLVKVFDQLIQQGATVIAIEHDLDVIA-NADYVIDMgpaggiNGGNIVATGTPLAV 814
Cdd:COG1122  159 DEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAeLADRVIVL------DDGRIVADGTPREV 221
UvrA_DNA-bind pfam17755
UvrA DNA-binding domain;
183-289 6.05e-14

UvrA DNA-binding domain;


Pssm-ID: 465484 [Multi-domain]  Cd Length: 110  Bit Score: 68.65  E-value: 6.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  183 DPALIIADENQTIEEGAVASWHLPGRNF----MPIVAREIGIPIDIPYKDLSEADKTRVLHGPKQTVAINIPSAKGKIFH 258
Cdd:pfam17755   1 DPDLVIPDPSLSLAEGAIAPWGKKRSSYyfqlLEALAKHYGFDLDTPFKDLPEEQQDIILYGSGEEIIVFYYSRGGRTRT 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 835833681  259 MdNAVYENAFAAVEDSMATTKNERAITRLNR 289
Cdd:pfam17755  81 Y-TKPFEGVIPNLERRYRETDSESVREELEK 110
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
719-794 3.54e-12

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: 64.96  E-value: 3.54e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 835833681 719 PALSGGEAQRLKLtSRIGKRQTgTLFVFDEPSVGLHPLDIQQLVKVFDQLIQQGATVIAIEHDLDVIANA-DYVIDM 794
Cdd:cd00267   79 PQLSGGQRQRVAL-ARALLLNP-DLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAaDRVIVL 153
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
688-792 4.50e-12

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


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 65.95  E-value: 4.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 688 LPIFKAQSAIANTLQILHDMGLgyllLGESTPALSGGEAQRLKLTSRIGKRQTgtLFVFDEPSVGLHPLDIQQLVKVFDQ 767
Cdd:cd03225  106 LPEEEIEERVEEALELVGLEGL----RDRSPFTLSGGQKQRVAIAGVLAMDPD--ILLLDEPTAGLDPAGRRELLELLKK 179
                         90       100
                 ....*....|....*....|....*.
gi 835833681 768 LIQQGATVIAIEHDLDVIAN-ADYVI 792
Cdd:cd03225  180 LKAEGKTIIIVTHDLDLLLElADRVI 205
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
362-831 8.15e-12

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: 68.39  E-value: 8.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 362 MEELGLDYLtLSRPGATLSTGELQRIQLGRTLRSTTTgvLYVLDEPSVGLHPANVAGLIKAFRGLVAQ-GNSVVVVDHDT 440
Cdd:COG1123  127 LEAVGLERR-LDRYPHQLSGGQRQRVAIAMALALDPD--LLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDL 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 441 SIISA-ADDVIEIgpgagkHGGTVVGQGTVAAIKQDKESLIA-PFLTGTATLRERPVLTDDALwkkgaLAIE-VAHHFNI 517
Cdd:COG1123  204 GVVAEiADRVVVM------DDGRIVEDGPPEEILAAPQALAAvPRLGAARGRAAPAAAAAEPL-----LEVRnLSKRYPV 272
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 518 ---------QDITARIPKNRFTTVTGMSGAGKTTLVldSLIPALIatakkRPlpthvkafDNGHIRhvvtVDSVPVGKNV 588
Cdd:COG1123  273 rgkggvravDDVSLTLRRGETLGLVGESGSGKSTLA--RLLLGLL-----RP--------TSGSIL----FDGKDLTKLS 333
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 589 RSTVAtytnildHLRQlfaatpaaqangwtasqfsynvaagacptcggtgqislDVQYLPditevcpqchgkrynkQ--- 665
Cdd:COG1123  334 RRSLR-------ELRR--------------------------------------RVQMVF----------------Qdpy 352
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 666 -----TLTVkwhGYSIADILDLavdeaLPIFKAQSAIANTLQILHDMGLGYLLLGESTPALSGGEAQR------LKLTSR 734
Cdd:COG1123  353 sslnpRMTV---GDIIAEPLRL-----HGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRvaiaraLALEPK 424
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 735 igkrqtgtLFVFDEPSVGlhpLD--IQ-QLVKVFDQLIQQ-GATVIAIEHDLDVIAN-ADYVIDMgpaggiNGGNIVATG 809
Cdd:COG1123  425 --------LLILDEPTSA---LDvsVQaQILNLLRDLQRElGLTYLFISHDLAVVRYiADRVAVM------YDGRIVEDG 487
                        490       500
                 ....*....|....*....|..
gi 835833681 810 TPLAVSQNPTSvtgQYLKTHLA 831
Cdd:COG1123  488 PTEEVFANPQH---PYTRALLA 506
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
379-450 2.72e-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: 62.65  E-value: 2.72e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 835833681 379 LSTGELQRIQLGRTLRSTTTgvLYVLDEPSVGLHPANVAGLIKAFRGLVAQGNSVVVVDHDTSIISAADDVI 450
Cdd:cd00267   81 LSGGQRQRVALARALLLNPD--LLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRV 150
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
316-477 4.03e-11

ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).


Pssm-ID: 213186 [Multi-domain]  Cd Length: 236  Bit Score: 64.00  E-value: 4.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 316 QNIATVSDMTV------AALHDFAATIVPWLPTKMHHLGQSLVDELLlslqpmEELGLDYLtLSRPGATLSTGELQRIQL 389
Cdd:cd03219   82 QIPRLFPELTVlenvmvAAQARTGSGLLLARARREEREARERAEELL------ERVGLADL-ADRPAGELSYGQQRRLEI 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 390 GRTLrSTTTGVLyVLDEPSVGLHPANVAGLIKAFRGLVAQGNSVVVVDHDTSII-SAADDVIEIgpgagkHGGTVVGQGT 468
Cdd:cd03219  155 ARAL-ATDPKLL-LLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVmSLADRVTVL------DQGRVIAEGT 226

                 ....*....
gi 835833681 469 VAAIKQDKE 477
Cdd:cd03219  227 PDEVRNNPR 235
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
721-797 4.31e-11

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: 61.99  E-value: 4.31e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 835833681 721 LSGGEAQRLKLTSRIGKR--QTGTLFVFDEPSVGLHPLDIQQLVKVFDQLIQQGATVIAIEHDLDVIANADYVIDMGPA 797
Cdd:cd03227   78 LSGGEKELSALALILALAslKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIKKV 156
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
704-835 8.75e-11

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 64.10  E-value: 8.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 704 LHDMGLGYLLLGESTPALSGGEAQRLKLTSrIGKRQTGTLfVFDEPSVGLHPLDIQQLVKVFDQLIQQGATVIAIEHDLD 783
Cdd:PRK13631 160 LNKMGLDDSYLERSPFGLSGGQKRRVAIAG-ILAIQPEIL-IFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTME 237
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 835833681 784 -VIANADYVIDMgpaggiNGGNIVATGTPLAVSQNPTSVTgqylKTHLALFHV 835
Cdd:PRK13631 238 hVLEVADEVIVM------DKGKILKTGTPYEIFTDQHIIN----STSIQVPRV 280
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
362-455 4.07e-10

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


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 60.17  E-value: 4.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 362 MEELGLDYLtLSRPGATLSTGELQRIQLGrtlrstttGVL------YVLDEPSVGLHPANVAGLIKAFRGLVAQGNSVVV 435
Cdd:cd03225  119 LELVGLEGL-RDRSPFTLSGGQKQRVAIA--------GVLamdpdiLLLDEPTAGLDPAGRRELLELLKKLKAEGKTIII 189
                         90       100
                 ....*....|....*....|.
gi 835833681 436 VDHDTSIISA-ADDVIEIGPG 455
Cdd:cd03225  190 VTHDLDLLLElADRVIVLEDG 210
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
702-795 4.33e-10

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


Pssm-ID: 213193 [Multi-domain]  Cd Length: 205  Bit Score: 60.35  E-value: 4.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 702 QILHDMGLGYLllGESTP-ALSGGEAQRLKL-TSRIGKRqtgTLFVFDEPSVGLHPLDIQQLVKVFDQLIQQGATVIAIE 779
Cdd:cd03226  109 TVLKDLDLYAL--KERHPlSLSGGQKQRLAIaAALLSGK---DLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVIT 183
                         90
                 ....*....|....*..
gi 835833681 780 HDLDVIAN-ADYVIDMG 795
Cdd:cd03226  184 HDYEFLAKvCDRVLLLA 200
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
684-820 8.98e-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: 61.84  E-value: 8.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 684 VDEALPIFKA--QSAIANTLQILHDMGLGyLLLGESTPALSGGEAQRLKLTSRIGKRqtGTLFVFDEPSVGLHPLDIQQL 761
Cdd:COG1123  105 IAEALENLGLsrAEARARVLELLEAVGLE-RRLDRYPHQLSGGQRQRVAIAMALALD--PDLLIADEPTTALDVTTQAEI 181
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 835833681 762 VKVFDQLIQQ-GATVIAIEHDLDVIAN-ADYVIDMgpaggiNGGNIVATGTPLAVSQNPTS 820
Cdd:COG1123  182 LDLLRELQRErGTTVLLITHDLGVVAEiADRVVVM------DDGRIVEDGPPEEILAAPQA 236
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
696-818 1.48e-09

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: 58.99  E-value: 1.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 696 AIANTLQILHDMGLGYLLlgeSTPA--LSGGEAQRLKLTsrigkRQTGT---LFVFDEPSVGLHPLDIQQLVKVFDQLIQ 770
Cdd:cd03219  120 ARERAEELLERVGLADLA---DRPAgeLSYGQQRRLEIA-----RALATdpkLLLLDEPAAGLNPEETEELAELIRELRE 191
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 835833681 771 QGATVIAIEHDLDVIAN-ADYVIDMgpaggiNGGNIVATGTPLAVSQNP 818
Cdd:cd03219  192 RGITVLLVEHDMDVVMSlADRVTVL------DQGRVIAEGTPDEVRNNP 234
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
721-817 2.59e-09

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 58.85  E-value: 2.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 721 LSGGEAQR------LKLTSRIgkrqtgtlFVFDEPSVGLHPLDIQQLVKVFDQLIQQGA-TVIAIEHDLDVIANADYVID 793
Cdd:PRK13632 143 LSGGQKQRvaiasvLALNPEI--------IIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAILADKVIV 214
                         90       100
                 ....*....|....*....|....
gi 835833681 794 MgpaggiNGGNIVATGTPLAVSQN 817
Cdd:PRK13632 215 F------SEGKLIAQGKPKEILNN 232
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
636-794 3.80e-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: 3.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  636 GTGQISLDVQYLPDITEvcpqchgKRYNKQTLTVKWHGY----SIADILDLAVDEALPIFKAQSAI-ANTLQILHDMGLG 710
Cdd:TIGR02857 375 TEGSIAVNGVPLADADA-------DSWRDQIAWVPQHPFlfagTIAENIRLARPDASDAEIREALErAGLDEFVAALPQG 447
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  711 Y-LLLGESTPALSGGEAQRLKLTsRIGKRQTGtLFVFDEPSVGLHPLDIQQLVKVFDQLiQQGATVIAIEHDLDVIANAD 789
Cdd:TIGR02857 448 LdTPIGEGGAGLSGGQAQRLALA-RAFLRDAP-LLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAALAD 524

                  ....*
gi 835833681  790 YVIDM 794
Cdd:TIGR02857 525 RIVVL 529
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
721-811 3.86e-09

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 58.49  E-value: 3.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 721 LSGGEAQRLKLTSRIGKRQTgtLFVFDEPSVGLHPLDIQQLVKVFDQLI-QQGATVIAIEHDLDVIANADYVIDMgpagg 799
Cdd:PRK13635 141 LSGGQKQRVAIAGVLALQPD--IIILDEATSMLDPRGRREVLETVRQLKeQKGITVLSITHDLDEAAQADRVIVM----- 213
                         90
                 ....*....|..
gi 835833681 800 iNGGNIVATGTP 811
Cdd:PRK13635 214 -NKGEILEEGTP 224
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
517-811 4.13e-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: 60.16  E-value: 4.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 517 IQDITARIPKNRFTTVTGMSGAGKTTLVldSLIPALIatakkRPlpthvkafDNGHIrhvvTVDSVPVgknvrstvATYT 596
Cdd:COG4988  353 LDGLSLTIPPGERVALVGPSGAGKSTLL--NLLLGFL-----PP--------YSGSI----LINGVDL--------SDLD 405
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 597 niLDHLRQLFAatpaaqangWtASQFSYnvaagacptcggtgqisldvqyLPditevcpqchgkrynkqtltvkwHGySI 676
Cdd:COG4988  406 --PASWRRQIA---------W-VPQNPY----------------------LF-----------------------AG-TI 427
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 677 ADILDL----AVDEALpifkaQSAI--ANTLQILHDMGLGY-LLLGESTPALSGGEAQRLKLTsrigkR---QTGTLFVF 746
Cdd:COG4988  428 RENLRLgrpdASDEEL-----EAALeaAGLDEFVAALPDGLdTPLGEGGRGLSGGQAQRLALA-----RallRDAPLLLL 497
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 835833681 747 DEPSVGlhpLDI---QQLVKVFDQLiQQGATVIAIEHDLDVIANADYVIDMgpaggiNGGNIVATGTP 811
Cdd:COG4988  498 DEPTAH---LDAeteAEILQALRRL-AKGRTVILITHRLALLAQADRILVL------DDGRIVEQGTH 555
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
352-456 6.46e-09

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 59.41  E-value: 6.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 352 VDELLLSLQPMEELGLDYLtLSRPGATLSTGELQRIQLGRTL-RSTTtgvLYVLDEPSVGL---HPANVAGLIkafRGLV 427
Cdd:COG1245  187 VDERGKLDELAEKLGLENI-LDRDISELSGGELQRVAIAAALlRDAD---FYFFDEPSSYLdiyQRLNVARLI---RELA 259
                         90       100       110
                 ....*....|....*....|....*....|..
gi 835833681 428 AQGNSVVVVDHDTSIISAADDVIEIG---PGA 456
Cdd:COG1245  260 EEGKYVLVVEHDLAILDYLADYVHILygePGV 291
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
721-792 1.78e-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: 55.62  E-value: 1.78e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 835833681 721 LSGGEAQRLKLTsrigkR---QTGTLFVFDEPSVGLHPLDIQQLVKVFDQLIQQGATVIAIEHDLD-VIANADYVI 792
Cdd:cd03235  133 LSGGQQQRVLLA-----RalvQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGlVLEYFDRVL 203
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
350-467 1.92e-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: 55.62  E-value: 1.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 350 SLVDELLlslqpmEELGLDYLtLSRPGATLSTGELQRIQLGRTLrsTTTGVLYVLDEPSVGLHPANVAGLIKAFRGLVAQ 429
Cdd:cd03235  111 AKVDEAL------ERVGLSEL-ADRQIGELSGGQQQRVLLARAL--VQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE 181
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 835833681 430 GNSVVVVDHDTSIISA-ADDVIEIgpgagkhGGTVVGQG 467
Cdd:cd03235  182 GMTILVVTHDLGLVLEyFDRVLLL-------NRTVVASG 213
cbiO PRK13649
energy-coupling factor transporter ATPase;
704-816 4.21e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 55.52  E-value: 4.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 704 LHDMGLGYLLLGESTPALSGGEAQRLKLTSrIGKRQTGTLfVFDEPSVGLHPLDIQQLVKVFDQLIQQGATVIAIEHDLD 783
Cdd:PRK13649 129 LALVGISESLFEKNPFELSGGQMRRVAIAG-ILAMEPKIL-VLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMD 206
                         90       100       110
                 ....*....|....*....|....*....|....
gi 835833681 784 VIAN-ADYVIDMgpaggiNGGNIVATGTPLAVSQ 816
Cdd:PRK13649 207 DVANyADFVYVL------EKGKLVLSGKPKDIFQ 234
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
319-472 4.79e-08

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


Pssm-ID: 440736 [Multi-domain]  Cd Length: 250  Bit Score: 54.71  E-value: 4.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 319 ATVSDMTVAALHDfaaTIVPWL-PTKMHHlgqSLVDELLlslqpmEELGLDYLtLSRPGATLSTGELQRIQLGRTLrstt 397
Cdd:COG1119   95 ETVLDVVLSGFFD---SIGLYRePTDEQR---ERARELL------ELLGLAHL-ADRPFGTLSQGEQRRVLIARAL---- 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 398 tgV----LYVLDEPSVGLHPANVAGLIKAFRGLVAQGN-SVVVVDHDTS-IISAADDVIEIgpgagkHGGTVVGQGTVAA 471
Cdd:COG1119  158 --VkdpeLLILDEPTAGLDLGARELLLALLDKLAAEGApTLVLVTHHVEeIPPGITHVLLL------KDGRVVAAGPKEE 229

                 .
gi 835833681 472 I 472
Cdd:COG1119  230 V 230
cbiO PRK13643
energy-coupling factor transporter ATPase;
692-829 5.20e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 55.12  E-value: 5.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 692 KAQSAIANTLQILhdmGLGYLLLGESTPALSGGEAQRLKLTSRIGKRQTgtLFVFDEPSVGLHPLDIQQLVKVFDQLIQQ 771
Cdd:PRK13643 119 KAEKIAAEKLEMV---GLADEFWEKSPFELSGGQMRRVAIAGILAMEPE--VLVLDEPTAGLDPKARIEMMQLFESIHQS 193
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 835833681 772 GATVIAIEHDLDVIAN-ADYVIDMgpaggiNGGNIVATGTPLAVSQNPtsvtgQYLKTH 829
Cdd:PRK13643 194 GQTVVLVTHLMDDVADyADYVYLL------EKGHIISCGTPSDVFQEV-----DFLKAH 241
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
363-456 5.64e-08

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 56.36  E-value: 5.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 363 EELGLDYLtLSRPGATLSTGELQRIQLGRTL-RSTTtgvLYVLDEPSVGL---HPANVAGLIKAFrglvAQGNSVVVVDH 438
Cdd:PRK13409 198 ERLGLENI-LDRDISELSGGELQRVAIAAALlRDAD---FYFFDEPTSYLdirQRLNVARLIREL----AEGKYVLVVEH 269
                         90       100
                 ....*....|....*....|.
gi 835833681 439 DTSIISAADDVIEIG---PGA 456
Cdd:PRK13409 270 DLAVLDYLADNVHIAygePGA 290
cbiO PRK13646
energy-coupling factor transporter ATPase;
702-832 9.22e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 54.40  E-value: 9.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 702 QILHDMGLGYLLLGESTPALSGGEAQRLKLTSRIGkrQTGTLFVFDEPSVGLHPLDIQQLVKVFDQL-IQQGATVIAIEH 780
Cdd:PRK13646 127 RLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILA--MNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqTDENKTIILVSH 204
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 835833681 781 DLDVIAN-ADYVIDMgpaggiNGGNIVATGTPLAVSQNPTSVTgqylKTHLAL 832
Cdd:PRK13646 205 DMNEVARyADEVIVM------KEGSIVSQTSPKELFKDKKKLA----DWHIGL 247
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
721-826 9.98e-08

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 54.00  E-value: 9.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 721 LSGGEAQRLKLTSRIGKRQTgtLFVFDEPSVGLHPLDIQQLVKVFDQLIQQ-GATVIAIEHDL-DVIANADYvidmgpAG 798
Cdd:PRK11831 144 LSGGMARRAALARAIALEPD--LIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVpEVLSIADH------AY 215
                         90       100
                 ....*....|....*....|....*...
gi 835833681 799 GINGGNIVATGTPLAVSQNPTSVTGQYL 826
Cdd:PRK11831 216 IVADKKIVAHGSAQALQANPDPRVRQFL 243
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
716-830 1.89e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 53.54  E-value: 1.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 716 ESTPA--LSGGEAQRLKLTSRIGKRQTgtLFVFDEPSVGLHPLDIQQLVKVFDQLIQQGATVIAIEHDLDVI---ANADY 790
Cdd:PRK13639 131 ENKPPhhLSGGQKKRVAIAGILAMKPE--IIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVpvyADKVY 208
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 835833681 791 VidmgpaggINGGNIVATGTPLAVSQNPTSVTGQYLK----THL 830
Cdd:PRK13639 209 V--------MSDGKIIKEGTPKEVFSDIETIRKANLRlprvAHL 244
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
362-456 1.92e-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: 53.14  E-value: 1.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 362 MEELGLDYLtLSRPGATLSTGELQRIQLGRTLRSTTTgvLYVLDEPSVGL---HPANVAGLIkafRGLVAQGNSVVVVDH 438
Cdd:cd03236  124 VDQLELRHV-LDRNIDQLSGGELQRVAIAAALARDAD--FYFFDEPSSYLdikQRLNAARLI---RELAEDDNYVLVVEH 197
                         90       100
                 ....*....|....*....|.
gi 835833681 439 DTSIISAADDVIEIG---PGA 456
Cdd:cd03236  198 DLAVLDYLSDYIHCLygePGA 218
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
708-783 2.34e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 53.55  E-value: 2.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 708 GLGYLLLGESTPALSGGEAQRLKLTsrigkrqtGTL------FVFDEPSVGLHPLDIQQLVKVFDQLIQQGATVIAIEHD 781
Cdd:PRK13651 153 GLDESYLQRSPFELSGGQKRRVALA--------GILamepdfLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHD 224

                 ..
gi 835833681 782 LD 783
Cdd:PRK13651 225 LD 226
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
720-819 2.49e-07

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 52.87  E-value: 2.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 720 ALSGGEAQRLKLTSRIGkrQTGTLFVFDEPSVGL---HPLDIQQLVKVFDQliQQGATVIAIEHDLDVIAN-ADYVIdmg 795
Cdd:PRK10575 147 SLSGGERQRAWIAMLVA--QDSRCLLLDEPTSALdiaHQVDVLALVHRLSQ--ERGLTVIAVLHDINMAARyCDYLV--- 219
                         90       100
                 ....*....|....*....|....
gi 835833681 796 pagGINGGNIVATGTPLAVSQNPT 819
Cdd:PRK10575 220 ---ALRGGEMIAQGTPAELMRGET 240
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
20-51 2.88e-07

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


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 51.70  E-value: 2.88e-07
                         10        20        30
                 ....*....|....*....|....*....|..
gi 835833681  20 LKNIDIDIPLNEFVAITGRSGSGKSSLAMGVL 51
Cdd:cd03250   21 LKDINLEVPKGELVAIVGPVGSGKSSLLSALL 52
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
701-814 5.52e-07

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 51.63  E-value: 5.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 701 LQILHDMGLGYL---LLGEstpaLSGGEAQRLkltsRIGkR---QTGTLFVFDEPSVGLhplDI---QQLVKVFDQLIQQ 771
Cdd:COG1121  121 DEALERVGLEDLadrPIGE----LSGGQQQRV----LLA-RalaQDPDLLLLDEPFAGV---DAateEALYELLRELRRE 188
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 835833681 772 GATVIAIEHDLD-VIANADYVIdmgpagGINGGnIVATGTPLAV 814
Cdd:COG1121  189 GKTILVVTHDLGaVREYFDRVL------LLNRG-LVAHGPPEEV 225
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
721-811 5.71e-07

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 51.60  E-value: 5.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 721 LSGGEAQRLKLT-SRIGKRQtgtLFVFDEPSVGLHPLDIQQLVKVFDQLIQQGATVIAIEHDLDVIAN-ADYV-Idmgpa 797
Cdd:COG1131  132 LSGGMKQRLGLAlALLHDPE---LLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERlCDRVaI----- 203
                         90
                 ....*....|....
gi 835833681 798 ggINGGNIVATGTP 811
Cdd:COG1131  204 --IDKGRIVADGTP 215
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
20-48 5.82e-07

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


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 50.07  E-value: 5.82e-07
                         10        20
                 ....*....|....*....|....*....
gi 835833681  20 LKNIDIDIPLNEFVAITGRSGSGKSSLAM 48
Cdd:cd03228   18 LKDVSLTIKPGEKVAIVGPSGSGKSTLLK 46
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
702-814 9.38e-07

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 50.99  E-value: 9.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 702 QILHDMGLGyLLLGESTPALSGGEAQRLKLTSRI-----GKRQTGTLFVFDEPsvgLHPLDIQQ---LVKVFDQLIQQGA 773
Cdd:COG4138  109 QLAEALGLE-DKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEGQLLLLDEP---MNSLDVAQqaaLDRLLRELCQQGI 184
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 835833681 774 TVIAIEHDLD-VIANADYVIDMgpaggiNGGNIVATGTPLAV 814
Cdd:COG4138  185 TVVMSSHDLNhTLRHADRVWLL------KQGKLVASGETAEV 220
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
374-452 9.68e-07

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 51.16  E-value: 9.68e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 835833681 374 RPGATLSTGELQRIQLGRTLRSTTTGVLyvLDEPSVGLHPANVAGLIKAFRGLVAQGNSVVVVDHDTSIISAADDVIEI 452
Cdd:PRK13638 132 QPIQCLSHGQKKRVAIAGALVLQARYLL--LDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYV 208
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
713-794 1.13e-06

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 49.92  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 713 LLGESTPALSGGEAQRLkLTSRiGKRQTGTLFVFDEPSVGLHPLDIQQLVKVFDQLIQQGATVIAIEHDLDVIANADYVI 792
Cdd:NF040873 112 LAGRQLGELSGGQRQRA-LLAQ-GLAQEADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCV 189

                 ..
gi 835833681 793 DM 794
Cdd:NF040873 190 LL 191
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
702-814 1.28e-06

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 50.50  E-value: 1.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 702 QILHDMGLGYLLlGESTPALSGGEAQRLKLtSRI-------GKRQTGTLFVfDEPSVGL---HPLDIQQLVKvfdQLIQQ 771
Cdd:COG4559  116 EALALVGLAHLA-GRSYQTLSGGEQQRVQL-ARVlaqlwepVDGGPRWLFL-DEPTSALdlaHQHAVLRLAR---QLARR 189
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 835833681 772 GATVIAIEHDLDVIAN-ADYVIDMgpaggiNGGNIVATGTPLAV 814
Cdd:COG4559  190 GGGVVAVLHDLNLAAQyADRILLL------HQGRLVAQGTPEEV 227
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
721-794 1.52e-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: 49.23  E-value: 1.52e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 835833681 721 LSGGEAQRLKLtSRIGKRQTgTLFVFDEPSVGLHPLDIQQLVK-VFDQLiqQGATVIAIEHDLDVIANADYVIDM 794
Cdd:cd03247   99 FSGGERQRLAL-ARILLQDA-PIVLLDEPTVGLDPITERQLLSlIFEVL--KDKTLIWITHHLTGIEHMDKILFL 169
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
374-438 1.84e-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: 1.84e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 835833681 374 RPGATLSTGELQRIQLGRTLRSTTTgvLYVLDEPSVGLHPANVAGLIKAFRGLVAQGNSVVVVDH 438
Cdd:cd03231  121 RPVAQLSAGQQRRVALARLLLSGRP--LWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
720-793 2.16e-06

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


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 50.06  E-value: 2.16e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 835833681 720 ALSGGEAQRLKLTSRIGkrQTGTLFVFDEPSvglHPLDIQQLVK---VFDQLIQQGATVIAIEHDLDVIanaDYVID 793
Cdd:cd03236  139 QLSGGELQRVAIAAALA--RDADFYFFDEPS---SYLDIKQRLNaarLIRELAEDDNYVLVVEHDLAVL---DYLSD 207
F420-0_ABC_ATP TIGR03873
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ...
704-814 2.71e-06

proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.


Pssm-ID: 163585 [Multi-domain]  Cd Length: 256  Bit Score: 49.81  E-value: 2.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  704 LHDMGLGYLLlGESTPALSGGEAQRLKLTSRIGkrQTGTLFVFDEPSvglHPLDIQ---QLVKVFDQLIQQGATVIAIEH 780
Cdd:TIGR03873 122 LARTELSHLA-DRDMSTLSGGERQRVHVARALA--QEPKLLLLDEPT---NHLDVRaqlETLALVRELAATGVTVVAALH 195
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 835833681  781 DLDVIAN-ADYVIDMGpagginGGNIVATGTPLAV 814
Cdd:TIGR03873 196 DLNLAASyCDHVVVLD------GGRVVAAGPPREV 224
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
372-475 2.89e-06

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


Pssm-ID: 213191 [Multi-domain]  Cd Length: 222  Bit Score: 48.97  E-value: 2.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 372 LSRPGATLSTGELQRIQLGRTLrsTTTGVLYVLDEPSVGLHPANVAGLIKAFRGLVAQGNSVVVVDHDTSII-SAADD-- 448
Cdd:cd03224  126 RKQLAGTLSGGEQQMLAIARAL--MSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFAlEIADRay 203
                         90       100
                 ....*....|....*....|....*..
gi 835833681 449 VIEigpgagkhGGTVVGQGTVAAIKQD 475
Cdd:cd03224  204 VLE--------RGRVVLEGTAAELLAD 222
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
719-814 2.98e-06

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 49.38  E-value: 2.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 719 PALSGGEAQRLKLtSRI------GKRQTGTLFVfDEPSVGL---HPLDIQQLVKVFDQliQQGATVIAIEHDLDVIAN-A 788
Cdd:PRK13548 133 PQLSGGEQQRVQL-ARVlaqlwePDGPPRWLLL-DEPTSALdlaHQHHVLRLARQLAH--ERGLAVIVVLHDLNLAARyA 208
                         90       100
                 ....*....|....*....|....*.
gi 835833681 789 DYVIDMgpaggiNGGNIVATGTPLAV 814
Cdd:PRK13548 209 DRIVLL------HQGRLVADGTPAEV 228
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
1-51 3.25e-06

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: 48.97  E-value: 3.25e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681   1 MPQTTLPThIQVRGAH---------VNNLKNIDIDIPLNEFVAITGRSGSGKSSLaMGVL 51
Cdd:COG4181    1 MSSSSAPI-IELRGLTktvgtgageLTILKGISLEVEAGESVAIVGASGSGKSTL-LGLL 58
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
338-468 3.88e-06

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 49.24  E-value: 3.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 338 PWLPT--KMHHLGQSLVDelllslQPMEELGLDYLTlSRPGATLSTGELQRIQLGRTLRSTTTGVLyvLDEPSVGLHPAN 415
Cdd:PRK11231 103 PWLSLwgRLSAEDNARVN------QAMEQTRINHLA-DRRLTDLSGGQRQRAFLAMVLAQDTPVVL--LDEPTTYLDINH 173
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 835833681 416 VAGLIKAFRGLVAQGNSVVVVDHDTSIISA-ADDVIEIgpgagkHGGTVVGQGT 468
Cdd:PRK11231 174 QVELMRLMRELNTQGKTVVTVLHDLNQASRyCDHLVVL------ANGHVMAQGT 221
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
20-47 5.52e-06

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: 48.23  E-value: 5.52e-06
                         10        20
                 ....*....|....*....|....*...
gi 835833681  20 LKNIDIDIPLNEFVAITGRSGSGKSSLA 47
Cdd:cd03225   17 LDDISLTIKKGEFVLIVGPNGSGKSTLL 44
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
336-458 5.54e-06

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 48.17  E-value: 5.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 336 IVPWLPTKMHHLGQSLVDELllslqpmEELGLDYLTLSRPGATLSTGELQRIQLGRTLRSTTTGVLyvLDEPSVGLHPAN 415
Cdd:PRK10247 102 IFPWQIRNQQPDPAIFLDDL-------ERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLL--LDEITSALDESN 172
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 835833681 416 VAGLIKAFRGLVAQGN-SVVVVDHDTSIISAADDVIEIGPGAGK 458
Cdd:PRK10247 173 KHNVNEIIHRYVREQNiAVLWVTHDKDEINHADKVITLQPHAGE 216
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
662-793 5.68e-06

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


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 48.56  E-value: 5.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 662 YNKQTLTVKWHGySIADILDLAVDEALPIFKAQSAIANTLQILHdmglgylLLGESTPALSGGEAQRLKLTSRIGKrqTG 741
Cdd:cd03237   65 YKPQYIKADYEG-TVRDLLSSITKDFYTHPYFKTEIAKPLQIEQ-------ILDREVPELSGGELQRVAIAACLSK--DA 134
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 835833681 742 TLFVFDEPSVglHpLDIQQLV---KVFDQLIQQG-ATVIAIEHDldvIANADYVID 793
Cdd:cd03237  135 DIYLLDEPSA--Y-LDVEQRLmasKVIRRFAENNeKTAFVVEHD---IIMIDYLAD 184
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
20-46 5.83e-06

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 48.12  E-value: 5.83e-06
                         10        20
                 ....*....|....*....|....*..
gi 835833681  20 LKNIDIDIPLNEFVAITGRSGSGKSSL 46
Cdd:COG1136   24 LRGVSLSIEAGEFVAIVGPSGSGKSTL 50
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
20-54 6.14e-06

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 48.13  E-value: 6.14e-06
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 835833681  20 LKNIDIDIPLNEFVAITGRSGSGKSSLaMGVLYAE 54
Cdd:COG2884   18 LSDVSLEIEKGEFVFLTGPSGAGKSTL-LKLLYGE 51
cbiO PRK13640
energy-coupling factor transporter ATPase;
702-819 6.92e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 48.64  E-value: 6.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 702 QILHDMGLgyLLLGESTPA-LSGGEAQRLKLTS--RIGKRqtgtLFVFDEPSVGLHPLDIQQLVKVFDQL-IQQGATVIA 777
Cdd:PRK13640 126 DVLADVGM--LDYIDSEPAnLSGGQKQRVAIAGilAVEPK----IIILDESTSMLDPAGKEQILKLIRKLkKKNNLTVIS 199
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 835833681 778 IEHDLDVIANADYVIDMgpaggiNGGNIVATGTPLAVSQNPT 819
Cdd:PRK13640 200 ITHDIDEANMADQVLVL------DDGKLLAQGSPVEIFSKVE 235
cbiO PRK13641
energy-coupling factor transporter ATPase;
691-826 7.05e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 48.67  E-value: 7.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 691 FKAQSAIANTLQILHDMGLGYLLLGESTPALSGGEAQRLKLTSRIGKRQTgtLFVFDEPSVGLHPLDIQQLVKVFDQLIQ 770
Cdd:PRK13641 116 FSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPE--ILCLDEPAAGLDPEGRKEMMQLFKDYQK 193
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 835833681 771 QGATVIAIEHDLDVIAN-ADYVIDMgpaggiNGGNIVATGTPLAVSQNPTSVTGQYL 826
Cdd:PRK13641 194 AGHTVILVTHNMDDVAEyADDVLVL------EHGKLIKHASPKEIFSDKEWLKKHYL 244
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
20-47 7.95e-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: 49.45  E-value: 7.95e-06
                         10        20
                 ....*....|....*....|....*...
gi 835833681  20 LKNIDIDIPLNEFVAITGRSGSGKSSLA 47
Cdd:COG2274  491 LDNISLTIKPGERVAIVGRSGSGKSTLL 518
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
719-818 8.13e-06

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


Pssm-ID: 213228 [Multi-domain]  Cd Length: 235  Bit Score: 47.88  E-value: 8.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 719 PA-LSGGEAQR------LKLTSRIgkrqtgtLFvFDEPSVGLHPLdiqqLVKVFDQLIQ-----QGATVIAIEHDLD-VI 785
Cdd:cd03261  134 PAeLSGGMKKRvalaraLALDPEL-------LL-YDEPTAGLDPI----ASGVIDDLIRslkkeLGLTSIMVTHDLDtAF 201
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 835833681 786 ANADYVIdMgpaggINGGNIVATGTP--LAVSQNP 818
Cdd:cd03261  202 AIADRIA-V-----LYDGKIVAEGTPeeLRASDDP 230
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
370-454 8.35e-06

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


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 46.58  E-value: 8.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 370 LTLSRPGatLSTGELQRIQLGR--TLRSTTTGVLYVLDEPSVGLHPANVAGLIKAFRGLVAQGNSVVVVDHDTSIISAAD 447
Cdd:cd03227   71 LIFTRLQ--LSGGEKELSALALilALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELAD 148

                 ....*..
gi 835833681 448 DVIEIGP 454
Cdd:cd03227  149 KLIHIKK 155
anch_rpt_ABC TIGR03771
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ...
721-811 1.21e-05

anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 163483 [Multi-domain]  Cd Length: 223  Bit Score: 47.15  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  721 LSGGEAQRLKLTSRIGKRQTgtLFVFDEPSVGLHPLDIQQLVKVFDQLIQQGATVIAIEHDL-DVIANADYVIdmgpagg 799
Cdd:TIGR03771 114 LSGGQRQRVLVARALATRPS--VLLLDEPFTGLDMPTQELLTELFIELAGAGTAILMTTHDLaQAMATCDRVV------- 184
                          90
                  ....*....|..
gi 835833681  800 INGGNIVATGTP 811
Cdd:TIGR03771 185 LLNGRVIADGTP 196
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
8-48 1.26e-05

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: 46.08  E-value: 1.26e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 835833681   8 THIQVRGAHVNNLKNIDIDIPLNEFVAITGRSGSGKSSLAM 48
Cdd:cd00267    3 ENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLR 43
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
720-811 1.27e-05

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 47.70  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 720 ALSGGEAQRLKLTSRIGkrQTGTLFVFDEPSVGLhplDIQ---QLVKVFDQLIQQGATVIAIEHDLDVIAN-ADYVIDMg 795
Cdd:PRK11231 138 DLSGGQRQRAFLAMVLA--QDTPVVLLDEPTTYL---DINhqvELMRLMRELNTQGKTVVTVLHDLNQASRyCDHLVVL- 211
                         90
                 ....*....|....*.
gi 835833681 796 paggiNGGNIVATGTP 811
Cdd:PRK11231 212 -----ANGHVMAQGTP 222
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
721-811 1.38e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 47.77  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 721 LSGGEAQRLKLTSRIGKRQTgtLFVFDEPSVGLHPLDIQQLVKVFDQLIQQ-GATVIAIEHDLDVIANADYVIDMgpagg 799
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPE--CIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVEADRIIVM----- 217
                         90
                 ....*....|..
gi 835833681 800 iNGGNIVATGTP 811
Cdd:PRK13633 218 -DSGKVVMEGTP 228
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
9-51 1.71e-05

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


Pssm-ID: 213224 [Multi-domain]  Cd Length: 228  Bit Score: 46.73  E-value: 1.71e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 835833681   9 HIQVRGAHVNNLKNIDIDIPLNEFVAITGRSGSGKSSLAMGVL 51
Cdd:cd03257   10 SFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAIL 52
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
704-811 1.81e-05

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: 48.29  E-value: 1.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 704 LHD----MGLGY-LLLGESTPALSGGEAQRLKLTsR--IGKRQtgtLFVFDEPSVGLhplDIQQLVKVFDQL--IQQGAT 774
Cdd:COG2274  590 LHDfieaLPMGYdTVVGEGGSNLSGGQRQRLAIA-RalLRNPR---ILILDEATSAL---DAETEAIILENLrrLLKGRT 662
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 835833681 775 VIAIEHDLDVIANADYVIDMgpaggiNGGNIVATGTP 811
Cdd:COG2274  663 VIIIAHRLSTIRLADRIIVL------DKGRIVEDGTH 693
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
20-46 1.91e-05

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 47.01  E-value: 1.91e-05
                         10        20
                 ....*....|....*....|....*..
gi 835833681  20 LKNIDIDIPLNEFVAITGRSGSGKSSL 46
Cdd:COG1116   27 LDDVSLTVAAGEFVALVGPSGCGKSTL 53
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
362-481 1.95e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 47.32  E-value: 1.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 362 MEELGLDYLTLSRPGATLSTGELQRIQLGrtlrstttGVL------YVLDEPSVGLHPANVAGLIKAFRGLVAQGN-SVV 434
Cdd:PRK13634 129 IELVGLPEELLARSPFELSGGQMRRVAIA--------GVLamepevLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGlTTV 200
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 835833681 435 VVDHDTSIISA-ADDVIEIgpgagkHGGTVVGQGTVAAIKQDKESLIA 481
Cdd:PRK13634 201 LVTHSMEDAARyADQIVVM------HKGTVFLQGTPREIFADPDELEA 242
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
721-795 1.96e-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: 1.96e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 835833681 721 LSGGEAQRLKLTSRIGKRQTgtLFVFDEPSVGLHPLDIQQLVKVFDQLIQQGATVIAIEHDLDV---IANADYVIDMG 795
Cdd:PRK11614 138 MSGGEQQMLAIGRALMSQPR--LLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQalkLADRGYVLENG 213
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
376-450 1.99e-05

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


Pssm-ID: 213214 [Multi-domain]  Cd Length: 178  Bit Score: 45.77  E-value: 1.99e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 835833681 376 GATLSTGELQRIQLGRTLRSTTTGVLyvLDEPSVGLHPANVAGLIKAFRGlVAQGNSVVVVDHDTSIISAADDVI 450
Cdd:cd03247   96 GRRFSGGERQRLALARILLQDAPIVL--LDEPTVGLDPITERQLLSLIFE-VLKDKTLIWITHHLTGIEHMDKIL 167
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
20-46 2.88e-05

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: 45.94  E-value: 2.88e-05
                         10        20
                 ....*....|....*....|....*..
gi 835833681  20 LKNIDIDIPLNEFVAITGRSGSGKSSL 46
Cdd:cd03255   20 LKGVSLSIEKGEFVAIVGPSGSGKSTL 46
cbiO PRK13650
energy-coupling factor transporter ATPase;
719-811 3.02e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 46.65  E-value: 3.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 719 PA-LSGGEAQRLKLTSRIGKRQTgtLFVFDEPSVGLHPLDIQQLVKVFDQLIQQ-GATVIAIEHDLDVIANADYVIDMgp 796
Cdd:PRK13650 138 PArLSGGQKQRVAIAGAVAMRPK--IIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVALSDRVLVM-- 213
                         90
                 ....*....|....*
gi 835833681 797 aggiNGGNIVATGTP 811
Cdd:PRK13650 214 ----KNGQVESTSTP 224
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
721-831 3.29e-05

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 47.50  E-value: 3.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 721 LSGGEAQRLKLTSRIGKrqTGTLFVFDEPSvglhP-LDIQQLVKVFDqLIQ---QGATVIAIEHDLDVIanaDYVIDmgp 796
Cdd:PRK13409 213 LSGGELQRVAIAAALLR--DADFYFFDEPT----SyLDIRQRLNVAR-LIRelaEGKYVLVVEHDLAVL---DYLAD--- 279
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 835833681 797 agginggNI-VATGTPLA---VSQnPTSV-TG--QYLKTHLA 831
Cdd:PRK13409 280 -------NVhIAYGEPGAygvVSK-PKGVrVGinEYLKGYLP 313
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
743-826 3.32e-05

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 46.14  E-value: 3.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 743 LFVFDEPSVGLHPLDIQQLVKVFDQLIQQ-GATVIAIEHDLDV---IANADYVidmgpaggINGGNIVATGTPLAVSQNP 818
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLvmgISDRIYV--------VNQGTPLANGTPEEIRNNP 245

                 ....*...
gi 835833681 819 tSVTGQYL 826
Cdd:PRK11300 246 -DVIKAYL 252
DnaJ_CXXCXGXG pfam00684
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
631-661 3.41e-05

DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four repeats of the motif CXXCXGXG where X is any amino acid. The isolated cysteine rich domain folds in zinc dependent fashion. Each set of two repeats binds one unit of zinc. Although this domain has been implicated in substrate binding, no evidence of specific interaction between the isolated DNAJ cysteine rich domain and various hydrophobic peptides has been found.


Pssm-ID: 459904 [Multi-domain]  Cd Length: 65  Bit Score: 42.16  E-value: 3.41e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 835833681  631 CPTCGGTGQIsldvqylpdITEVCPQCHGKR 661
Cdd:pfam00684  44 CPTCGGTGKI---------IKDPCKKCKGKG 65
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
379-474 3.86e-05

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


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 45.26  E-value: 3.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 379 LSTGELQRIQLGRTLRSTTTgvLYVLDEPSVGLHPANVAGLIKAFRGLVAQGN-SVVVVDHDTSIISAADDVIEIGPG-A 456
Cdd:cd03222   72 LSGGELQRVAIAAALLRNAT--FYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRIHVFEGeP 149
                         90
                 ....*....|....*...
gi 835833681 457 GKHGGTVVGQGTVAAIKQ 474
Cdd:cd03222  150 GVYGIASQPKGTREGINR 167
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
721-792 4.09e-05

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: 44.70  E-value: 4.09e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 835833681 721 LSGGEAQRLKLT-SRIGKRQtgtLFVFDEPSVGLHPLDIQQLVKVFDQLIQQGATVIAIEHDLDVIAN-ADYVI 792
Cdd:cd03230   96 LSGGMKQRLALAqALLHDPE---LLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERlCDRVA 166
DnaJ_zf cd10719
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
631-661 4.24e-05

Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of DnaJ/Hsp40 (heat shock protein 40). DnaJ proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonin family. Hsp40 proteins are characterized by the presence of an N-terminal J domain, which mediates the interaction with Hsp70. This central domain contains four repeats of a CxxCxGxG motif and binds to two Zinc ions. It has been implicated in substrate binding.


Pssm-ID: 199908 [Multi-domain]  Cd Length: 65  Bit Score: 42.24  E-value: 4.24e-05
                         10        20        30
                 ....*....|....*....|....*....|.
gi 835833681 631 CPTCGGTGQIsldvqylpdITEVCPQCHGKR 661
Cdd:cd10719   44 CPTCGGTGKI---------IKDPCPKCKGKG 65
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
684-811 4.45e-05

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 46.15  E-value: 4.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 684 VDEALPIFKAQSAIANTLQilhdmglgylllgestpALSGGEAQRLKLTSRIGKRqtGTLFVFDEPSVGLHPLDIQQLVK 763
Cdd:PRK13638 117 VDEALTLVDAQHFRHQPIQ-----------------CLSHGQKKRVAIAGALVLQ--ARYLLLDEPTAGLDPAGRTQMIA 177
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 835833681 764 VFDQLIQQGATVIAIEHDLDVI---ANADYVidmgpaggINGGNIVATGTP 811
Cdd:PRK13638 178 IIRRIVAQGNHVIISSHDIDLIyeiSDAVYV--------LRQGQILTHGAP 220
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
675-810 4.78e-05

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


Pssm-ID: 213219 [Multi-domain]  Cd Length: 237  Bit Score: 45.55  E-value: 4.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 675 SIADILDLAvDEALPIFKAQSA--IANTLQILHDMGLGY-LLLGESTPALSGGEAQRLKLTSRIGKRQTgtLFVFDEPSV 751
Cdd:cd03252   91 SIRDNIALA-DPGMSMERVIEAakLAGAHDFISELPEGYdTIVGEQGAGLSGGQRQRIAIARALIHNPR--ILIFDEATS 167
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 835833681 752 GLhplDIQQlvkvfDQLIQQ-------GATVIAIEHDLDVIANADYVIDMgpaggiNGGNIVATGT 810
Cdd:cd03252  168 AL---DYES-----EHAIMRnmhdicaGRTVIIIAHRLSTVKNADRIIVM------EKGRIVEQGS 219
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
721-794 6.31e-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: 44.30  E-value: 6.31e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 835833681 721 LSGGEAQRLKLtSR--IGKRQtgtLFVFDEPSVGLHPLDIQQLVKVFDQLIqQGATVIAIEHDLDVIANADYVIDM 794
Cdd:cd03228   97 LSGGQRQRIAI-ARalLRDPP---ILILDEATSALDPETEALILEALRALA-KGKTVIVIAHRLSTIRDADRIIVL 167
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
377-455 6.40e-05

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


Pssm-ID: 213259 [Multi-domain]  Cd Length: 214  Bit Score: 45.09  E-value: 6.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 377 ATLSTGELQRIQLGRTLRSTTTgvLYVLDEPSVGLHPANVAGLIKAFRGLVAQGNSVVVVDHDTSIISAADD-VIEIGPG 455
Cdd:cd03292  135 AELSGGEQQRVAIARAIVNSPT--ILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHrVIALERG 212
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
362-458 6.89e-05

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 44.86  E-value: 6.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 362 MEELGLDYLTlSRPGATLSTGELQRIQLGRTLRSTTTgvLYVLDEPSVGLHPANVAGLIKAFRGLVAQGNSVVVVDH-DT 440
Cdd:PRK13539 112 LEAVGLAPLA-HLPFGYLSAGQKRRVALARLLVSNRP--IWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATHiPL 188
                         90
                 ....*....|....*...
gi 835833681 441 SIISAAddVIEIGPGAGK 458
Cdd:PRK13539 189 GLPGAR--ELDLGPFAAE 204
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
721-830 7.01e-05

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 46.32  E-value: 7.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 721 LSGGEAQRLKLTSRIGKRqtGTLFVFDEPSvglhP-LDIQQ---LVKVFDQLIQQGATVIAIEHDLDVIanaDYVIDMgp 796
Cdd:COG1245  213 LSGGELQRVAIAAALLRD--ADFYFFDEPS----SyLDIYQrlnVARLIRELAEEGKYVLVVEHDLAIL---DYLADY-- 281
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 835833681 797 aggINggniVATGTPLA---VSQnPTSV-TG--QYLKTHL 830
Cdd:COG1245  282 ---VH----ILYGEPGVygvVSK-PKSVrVGinQYLDGYL 313
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
362-470 7.41e-05

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 45.15  E-value: 7.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 362 MEELGLDYLTlSRPGATLSTGELQRIQLGRTL-----RSTTTGVLYvLDEPSVGL---HPANVAGLIKAFrgLVAQGNSV 433
Cdd:PRK13548 119 LAQVDLAHLA-GRDYPQLSGGEQQRVQLARVLaqlwePDGPPRWLL-LDEPTSALdlaHQHHVLRLARQL--AHERGLAV 194
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 835833681 434 VVVDHDTSIISA-ADDVIEIgpgagkHGGTVVGQGTVA 470
Cdd:PRK13548 195 IVVLHDLNLAARyADRIVLL------HQGRLVADGTPA 226
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
20-46 8.25e-05

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 45.05  E-value: 8.25e-05
                         10        20
                 ....*....|....*....|....*..
gi 835833681  20 LKNIDIDIPLNEFVAITGRSGSGKSSL 46
Cdd:PRK11247  28 LNQLDLHIPAGQFVAVVGRSGCGKSTL 54
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
721-792 8.44e-05

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


Pssm-ID: 213183 [Multi-domain]  Cd Length: 163  Bit Score: 43.96  E-value: 8.44e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 835833681 721 LSGGEAQR------LKLTSRIgkrqtgtlFVFDEPSVGLHPLDIQQLVKVFDQLIQQGATVIAIEHDLD-VIANADYVI 792
Cdd:cd03216   83 LSVGERQMveiaraLARNARL--------LILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDeVFEIADRVT 153
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
352-472 8.51e-05

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


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 46.05  E-value: 8.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 352 VDELLlslqpmEELGLDYLTLSRPGATLSTGELQRIQLGRTLrSTTTGVLyVLDEPSVGLHPANVAGLIKAFRGLVAQGN 431
Cdd:COG1123  384 VAELL------ERVGLPPDLADRYPHELSGGQRQRVAIARAL-ALEPKLL-ILDEPTSALDVSVQAQILNLLRDLQRELG 455
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 835833681 432 -SVVVVDHDTSIISA-ADDVIEIgpgagkHGGTVVGQGTVAAI 472
Cdd:COG1123  456 lTYLFISHDLAVVRYiADRVAVM------YDGRIVEDGPTEEV 492
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
701-796 9.94e-05

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 44.42  E-value: 9.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 701 LQILHDMGLGYLLLGESTPALSGGEAQRLKLtSR--IGKRQtgtLFVFDEPSVGLHPLDIQQLVKVFDQLIQQ-GATVIA 777
Cdd:COG4619  111 LELLERLGLPPDILDKPVERLSGGERQRLAL-IRalLLQPD---VLLLDEPTSALDPENTRRVEELLREYLAEeGRAVLW 186
                         90       100
                 ....*....|....*....|
gi 835833681 778 IEHDLDVIAN-ADYVIDMGP 796
Cdd:COG4619  187 VSHDPEQIERvADRVLTLEA 206
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
20-46 1.05e-04

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: 44.38  E-value: 1.05e-04
                         10        20
                 ....*....|....*....|....*..
gi 835833681  20 LKNIDIDIPLNEFVAITGRSGSGKSSL 46
Cdd:cd03293   20 LEDISLSVEEGEFVALVGPSGCGKSTL 46
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
721-830 1.12e-04

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 44.57  E-value: 1.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 721 LSGGEAQRLKLTSRIGKRQTgtLFVFDEPSVGLHPLDIQQLVKVFDQLIQQGATVIAIEHDLDVIAN-ADYVIDMgpagg 799
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPE--VLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHvSSHVIFL----- 225
                         90       100       110
                 ....*....|....*....|....*....|..
gi 835833681 800 iNGGNIVATGTPLAVSQNPTSVT-GQYLKTHL 830
Cdd:PRK10619 226 -HQGKIEEEGAPEQLFGNPQSPRlQQFLKGSL 256
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
362-438 1.12e-04

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 45.79  E-value: 1.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 362 MEELGLDyLTLSRPGATLSTGELQRIQLgrtLRstttgVLY------VLDEPSVGLHPANVAGLIKAFRGLVAQGNSVVV 435
Cdd:COG3845  126 SERYGLD-VDPDAKVEDLSVGEQQRVEI---LK-----ALYrgarilILDEPTAVLTPQEADELFEILRRLAAEGKSIIF 196

                 ...
gi 835833681 436 VDH 438
Cdd:COG3845  197 ITH 199
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
713-811 1.30e-04

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 44.54  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 713 LLGESTPALSGGEAQRLKLTSRIgkRQT-------GTLFVFDEPSvglHPLDIQQlVKVFDQLI----QQGATVIAIEHD 781
Cdd:PRK03695 119 KLGRSVNQLSGGEWQRVRLAAVV--LQVwpdinpaGQLLLLDEPM---NSLDVAQ-QAALDRLLselcQQGIAVVMSSHD 192
                         90       100       110
                 ....*....|....*....|....*....|.
gi 835833681 782 LD-VIANADYVIDMgpaggiNGGNIVATGTP 811
Cdd:PRK03695 193 LNhTLRHADRVWLL------KQGKLLASGRR 217
DnaJ_CXXCXGXG pfam00684
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
631-660 1.31e-04

DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four repeats of the motif CXXCXGXG where X is any amino acid. The isolated cysteine rich domain folds in zinc dependent fashion. Each set of two repeats binds one unit of zinc. Although this domain has been implicated in substrate binding, no evidence of specific interaction between the isolated DNAJ cysteine rich domain and various hydrophobic peptides has been found.


Pssm-ID: 459904 [Multi-domain]  Cd Length: 65  Bit Score: 40.62  E-value: 1.31e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 835833681  631 CPTCGGTGQISLDVQYLPD---ITEVCPQCHGK 660
Cdd:pfam00684  18 CPTCGGTGQVRRVQQTGPGffqMQSTCPTCGGT 50
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
20-47 1.41e-04

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 45.54  E-value: 1.41e-04
                         10        20
                 ....*....|....*....|....*...
gi 835833681  20 LKNIDIDIPLNEFVAITGRSGSGKSSLA 47
Cdd:COG1132  356 LKDISLTIPPGETVALVGPSGSGKSTLV 383
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
20-47 1.65e-04

ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C 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-resistance 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: 213211 [Multi-domain]  Cd Length: 221  Bit Score: 43.64  E-value: 1.65e-04
                         10        20
                 ....*....|....*....|....*...
gi 835833681  20 LKNIDIDIPLNEFVAITGRSGSGKSSLA 47
Cdd:cd03244   20 LKNISFSIKPGEKVGIVGRTGSGKSSLL 47
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
363-452 1.76e-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: 1.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 363 EELGLDYLtLSRPGATLSTGELQRIQLGRTLrstTTGVLYVL-DEPSVGLHPANVAGLIKAFRGLVAQ-GNSVVVVDHDT 440
Cdd:cd03255  126 ERVGLGDR-LNHYPSELSGGQQQRVAIARAL---ANDPKIILaDEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDP 201
                         90
                 ....*....|..
gi 835833681 441 SIISAADDVIEI 452
Cdd:cd03255  202 ELAEYADRIIEL 213
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
379-543 1.89e-04

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


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 44.79  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  379 LSTGELQRIQLGRTLrsTTTGVLYVLDEPSVGLHPANVAGLIKAFRGLV-AQGNSVVVVDHDTSIIS-AADDVIEIGPGA 456
Cdd:TIGR03269 169 LSGGEKQRVVLARQL--AKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkASGISMVLTSHWPEVIEdLSDKAIWLENGE 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  457 GKHGGT---VVGQ--GTVAAIKQDKEsliapFLTGTATLRERPVltddalwKKGALAIEVAHHFNIQDITARIPKNRFTT 531
Cdd:TIGR03269 247 IKEEGTpdeVVAVfmEGVSEVEKECE-----VEVGEPIIKVRNV-------SKRYISVDRGVVKAVDNVSLEVKEGEIFG 314
                         170
                  ....*....|..
gi 835833681  532 VTGMSGAGKTTL 543
Cdd:TIGR03269 315 IVGTSGAGKTTL 326
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
721-827 1.97e-04

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 43.85  E-value: 1.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 721 LSGGEAQRLKLtSRIGKRQTGTLfVFDEPSVGLHPLDIQQLVKVFDQLIQQGATVIAIEHDLDVIAN-ADYVIDMgpagg 799
Cdd:PRK11124 142 LSGGQQQRVAI-ARALMMEPQVL-LFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYM----- 214
                         90       100
                 ....*....|....*....|....*...
gi 835833681 800 iNGGNIVATGTPLAVSQNPTSVTGQYLK 827
Cdd:PRK11124 215 -ENGHIVEQGDASCFTQPQTEAFKNYLS 241
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
678-818 2.40e-04

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 44.84  E-value: 2.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 678 DILDLAVDEALpifkaqsAIANTLQILHDMGLGY-LLLGESTPALSGGEAQRLKLTSRIGkrQTGTLFVFDEPSVGlhpL 756
Cdd:PRK11174 449 DASDEQLQQAL-------ENAWVSEFLPLLPQGLdTPIGDQAAGLSVGQAQRLALARALL--QPCQLLLLDEPTAS---L 516
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 835833681 757 DIQQLVKVFDQLIQ--QGATVIAIEHDLDVIANADYVIDMgpaggiNGGNIVATGTPLAVSQNP 818
Cdd:PRK11174 517 DAHSEQLVMQALNAasRRQTTLMVTHQLEDLAQWDQIWVM------QDGQIVQQGDYAELSQAG 574
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
363-439 2.60e-04

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 43.38  E-value: 2.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 363 EELGLDYLtLSRPGATLSTGELQRIQLGRTL-----RSTTTGVLYVLDEPSVGLHPANVAGLIKAFRGLVAQGNSVVVVD 437
Cdd:PRK03695 112 EALGLDDK-LGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAGQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSS 190

                 ..
gi 835833681 438 HD 439
Cdd:PRK03695 191 HD 192
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
20-47 2.84e-04

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


Pssm-ID: 213213 [Multi-domain]  Cd Length: 173  Bit Score: 42.59  E-value: 2.84e-04
                         10        20
                 ....*....|....*....|....*...
gi 835833681  20 LKNIDIDIPLNEFVAITGRSGSGKSSLA 47
Cdd:cd03246   18 LRNVSFSIEPGESLAIIGPSGSGKSTLA 45
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
362-460 2.92e-04

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


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 43.17  E-value: 2.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 362 MEELGLDYLtLSRPGATLSTGELQRIQLGRTLRSTTTgvLYVLDEPSVGLHPAN---VAGLIKAFrglvAQGN--SVVVV 436
Cdd:cd03237  100 AKPLQIEQI-LDREVPELSGGELQRVAIAACLSKDAD--IYLLDEPSAYLDVEQrlmASKVIRRF----AENNekTAFVV 172
                         90       100
                 ....*....|....*....|....*
gi 835833681 437 DHDTSIIS-AADDVIEIGPGAGKHG 460
Cdd:cd03237  173 EHDIIMIDyLADRLIVFEGEPSVNG 197
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
631-670 2.92e-04

chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the DnaK-DnaJ-GrpE chaperone system. The three components typically are encoded by consecutive genes. DnaJ homologs occur in many genomes, typically not near DnaK and GrpE-like genes; most such genes are not included by this family. Eukaryotic (mitochondrial and chloroplast) forms are not included in the scope of this family.


Pssm-ID: 274090 [Multi-domain]  Cd Length: 354  Bit Score: 44.13  E-value: 2.92e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 835833681  631 CPTCGGTGQIsldvqylpdITEVCPQCHGKRYNK--QTLTVK 670
Cdd:TIGR02349 189 CPTCGGEGKI---------IKEPCSTCKGKGRVKerKTITVK 221
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
20-48 2.93e-04

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


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 41.86  E-value: 2.93e-04
                          10        20
                  ....*....|....*....|....*....
gi 835833681   20 LKNIDIDIPLNEFVAITGRSGSGKSSLAM 48
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLK 29
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
667-786 3.27e-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: 3.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  667 LTVKWHGYSIADILDLAVDEALP-IFKAQSAIANTLQILHDMGLGYLLlgeSTPALSGGEaQRLK--LTSRIGKRQTGTL 743
Cdd:pfam13304 185 LQRLVRGLKLADLNLSDLGEGIEkSLLVDDRLRERGLILLENGGGGEL---PAFELSDGT-KRLLalLAALLSALPKGGL 260
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 835833681  744 FVFDEPSVGLHPLDIQQLVKVFDQLIQQGATVIAIEHDLDVIA 786
Cdd:pfam13304 261 LLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLLLD 303
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
630-670 3.43e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 43.59  E-value: 3.43e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 835833681 630 ACPTCGGTGQIsldvqylpdITEVCPQCHGKRYNK--QTLTVK 670
Cdd:PRK10767 183 TCPTCHGRGKI---------IKDPCKKCHGQGRVEkeKTLSVK 216
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
364-467 3.46e-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: 3.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 364 ELGLDYLTLSRPGaTLSTGELQRIQLGRTLRSTTTGVLyvLDEPSVGLHPANVAGLIKAFRGLVAQ-GNSVVVVDHDTSI 442
Cdd:cd03298  115 RVGLAGLEKRLPG-ELSGGERQRVALARVLVRDKPVLL--LDEPFAALDPALRAEMLDLVLDLHAEtKMTVLMVTHQPED 191
                         90       100
                 ....*....|....*....|....*.
gi 835833681 443 ISA-ADDVIEIgpgagkHGGTVVGQG 467
Cdd:cd03298  192 AKRlAQRVVFL------DNGRIAAQG 211
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
362-443 3.51e-04

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 44.00  E-value: 3.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 362 MEELGLDYLtLSRPGATLSTGELQRIQLGRTL-RSTTtgvLYVLDEPSVGL---HPANVAgliKAFRGLV-AQGNSVVVV 436
Cdd:COG1245  440 IKPLGLEKL-LDKNVKDLSGGELQRVAIAACLsRDAD---LYLLDEPSAHLdveQRLAVA---KAIRRFAeNRGKTAMVV 512

                 ....*..
gi 835833681 437 DHDTSII 443
Cdd:COG1245  513 DHDIYLI 519
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
709-820 3.81e-04

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 43.94  E-value: 3.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 709 LGYLLLGEST---PA-LSGGEAQRLKLTSRIgkRQTGTLFVFDEPSVGLHPLDIQQLVKVFDQLIQQGATVIAIEHDLDV 784
Cdd:PRK10535 129 LQRLGLEDRVeyqPSqLSGGQQQRVSIARAL--MNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQV 206
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 835833681 785 IANADYVIDmgpaggINGGNIVA----------TGTPLAVSQNPTS 820
Cdd:PRK10535 207 AAQAERVIE------IRDGEIVRnppaqekvnvAGGTEPVVNTASG 246
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
378-467 3.82e-04

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


Pssm-ID: 213236 [Multi-domain]  Cd Length: 210  Bit Score: 42.65  E-value: 3.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 378 TLSTGELQRIQLGRTLRSTTTgvLYVLDEPSVGLHPANVAGLIKAFRGLVAQGNSVVVVDHDTSIISA-ADDVIEIgpga 456
Cdd:cd03269  128 ELSKGNQQKVQFIAAVIHDPE--LLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEElCDRVLLL---- 201
                         90
                 ....*....|.
gi 835833681 457 gkHGGTVVGQG 467
Cdd:cd03269  202 --NKGRAVLYG 210
DnaJ_zf cd10719
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
631-660 3.94e-04

Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of DnaJ/Hsp40 (heat shock protein 40). DnaJ proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonin family. Hsp40 proteins are characterized by the presence of an N-terminal J domain, which mediates the interaction with Hsp70. This central domain contains four repeats of a CxxCxGxG motif and binds to two Zinc ions. It has been implicated in substrate binding.


Pssm-ID: 199908 [Multi-domain]  Cd Length: 65  Bit Score: 39.16  E-value: 3.94e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 835833681 631 CPTCGGTGQISLDVQYLPD---ITEVCPQCHGK 660
Cdd:cd10719   18 CPTCGGSGQVRQVQGTGFGffqTQTTCPTCGGT 50
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
12-57 3.95e-04

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: 41.96  E-value: 3.95e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 835833681  12 VRGAHVNNLKNIDIDIPLNEFVAITGRSGSGKSSLAMGVLYAEGAR 57
Cdd:cd03227    3 VLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGA 48
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
720-811 4.01e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 43.20  E-value: 4.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 720 ALSGGEAQRLKLTSRIGkrQTGTLFVFDEPSVGLHPLDIQQLVKVFDQLIQ-QGATVIAIEHDLDVIANADYVIDMgpag 798
Cdd:PRK13648 142 ALSGGQKQRVAIAGVLA--LNPSVIILDEATSMLDPDARQNLLDLVRKVKSeHNITIISITHDLSEAMEADHVIVM---- 215
                         90
                 ....*....|...
gi 835833681 799 giNGGNIVATGTP 811
Cdd:PRK13648 216 --NKGTVYKEGTP 226
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
377-439 4.69e-04

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 42.99  E-value: 4.69e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 835833681 377 ATLSTGELQRIQLGRTLrsTTTGVLYVLDEPSVGLHPANVAGLIKAFRGLVAQ-GNSVVVVDHD 439
Cdd:PRK11701 150 TTFSGGMQQRLQIARNL--VTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHD 211
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
20-113 4.73e-04

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


Pssm-ID: 213223 [Multi-domain]  Cd Length: 241  Bit Score: 42.56  E-value: 4.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  20 LKNIDIDIPLNEFVAITGRSGSGKSSLAmgvlyaegarRYLNALSTFTRrrinqvGKASVD--SVQYLPSAlALRQrpqv 97
Cdd:cd03256   17 LKDVSLSINPGEFVALIGPSGAGKSTLL----------RCLNGLVEPTS------GSVLIDgtDINKLKGK-ALRQ---- 75
                         90
                 ....*....|....*.
gi 835833681  98 pgVRSTVGTMSESLNI 113
Cdd:cd03256   76 --LRRQIGMIFQQFNL 89
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
403-452 4.83e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.88  E-value: 4.83e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 835833681 403 VLDEPSVGL---HPANVAGLIKAFRGL-VAQgnsVVVVDHDTSIISAADDVIEI 452
Cdd:PRK02224 816 ILDEPTVFLdsgHVSQLVDLVESMRRLgVEQ---IVVVSHDDELVGAADDLVRV 866
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
20-47 5.13e-04

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 43.47  E-value: 5.13e-04
                         10        20
                 ....*....|....*....|....*...
gi 835833681  20 LKNIDIDIPLNEFVAITGRSGSGKSSLA 47
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIA 386
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
722-797 5.15e-04

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


Pssm-ID: 443809 [Multi-domain]  Cd Length: 229  Bit Score: 42.42  E-value: 5.15e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 835833681 722 SGGEAQRLKLTSRIGKRQTgtLFVFDEPSVGLHPLDIQQLVKVFDQLIQQGATVIAIEHDLDVIAN-ADYVIDMGPA 797
Cdd:COG4778  154 SGGEQQRVNIARGFIADPP--LLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAvADRVVDVTPF 228
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
363-774 5.56e-04

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 43.46  E-value: 5.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 363 EELGLDYLtLSRPGATLSTGELQRIQLGRTLRSTTTgvLYVLDEPSVGLHPANVAGLIKAFRGLVAQGNSVVVvdhdtsI 442
Cdd:PRK10938 121 QQFGITAL-LDRRFKYLSTGETRKTLLCQALMSEPD--LLILDEPFDGLDVASRQQLAELLASLHQSGITLVL------V 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 443 ISAADDVieigPGAGKHGG-----TVVGQGTVAAIKQD--------KESLIAPFLTGTATLRERPVLTDDAlwkkgalAI 509
Cdd:PRK10938 192 LNRFDEI----PDFVQFAGvladcTLAETGEREEILQQalvaqlahSEQLEGVQLPEPDEPSARHALPANE-------PR 260
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 510 EVAHHFNIQ--------DITARIPKNRFTTVTGMSGAGKTTLVldSLIPAliatakkrplpTHVKAFDNghirhvvtvDS 581
Cdd:PRK10938 261 IVLNNGVVSyndrpilhNLSWQVNPGEHWQIVGPNGAGKSTLL--SLITG-----------DHPQGYSN---------DL 318
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 582 VPVGKNvRSTVATYTNILDHLrqlfaatpaaqanGWTASqfsynvaagacptcggtgqiSLDVQYlpditevcpqchgkR 661
Cdd:PRK10938 319 TLFGRR-RGSGETIWDIKKHI-------------GYVSS--------------------SLHLDY--------------R 350
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 662 YNKQTLTVKWHGY--SIAdiLDLAVDEALPiFKAQsaiantlQILHDMGLGYLLLGESTPALSGGEaQRLKLTSRIGKRQ 739
Cdd:PRK10938 351 VSTSVRNVILSGFfdSIG--IYQAVSDRQQ-KLAQ-------QWLDILGIDKRTADAPFHSLSWGQ-QRLALIVRALVKH 419
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 835833681 740 TgTLFVFDEPSVGLHPLDiQQLVKVF-DQLIQQGAT 774
Cdd:PRK10938 420 P-TLLILDEPLQGLDPLN-RQLVRRFvDVLISEGET 453
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
721-810 5.72e-04

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 42.79  E-value: 5.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 721 LSGGEAQRLKL-TSRIGKRQtgtLFVFDEPSVGLHPLDIQQLVKVFDQLIQQGATVIAIEHDLDVI-ANADYVIdMgpag 798
Cdd:COG4152  130 LSKGNQQKVQLiAALLHDPE---LLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVeELCDRIV-I---- 201
                         90
                 ....*....|..
gi 835833681 799 gINGGNIVATGT 810
Cdd:COG4152  202 -INKGRKVLSGS 212
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
16-71 5.75e-04

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


Pssm-ID: 213229 [Multi-domain]  Cd Length: 213  Bit Score: 42.13  E-value: 5.75e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 835833681  16 HVnnLKNIDIDIPLNEFVAITGRSGSGKSSLAmgvlyaegarRYLNALSTFTRRRI 71
Cdd:cd03262   14 HV--LKGIDLTVKKGEVVVIIGPSGSGKSTLL----------RCINLLEEPDSGTI 57
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
365-472 5.90e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 42.48  E-value: 5.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 365 LGLDYLtLSRPGATLSTGELQRIQLGRTLrSTTTGVLyVLDEPSVGLHPANVAGLIKAFRGLVAQ-GNSVVVVDHDTSII 443
Cdd:PRK13652 125 LGLEEL-RDRVPHHLSGGEKKRVAIAGVI-AMEPQVL-VLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLV 201
                         90       100
                 ....*....|....*....|....*....
gi 835833681 444 SAADDVIEIgpgagKHGGTVVGQGTVAAI 472
Cdd:PRK13652 202 PEMADYIYV-----MDKGRIVAYGTVEEI 225
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
721-809 6.00e-04

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


Pssm-ID: 213224 [Multi-domain]  Cd Length: 228  Bit Score: 42.11  E-value: 6.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 721 LSGGEAQR------LKLTSRigkrqtgtLFVFDEPSVGLHPLdIQ-QLVKVFDQLIQQ-GATVIAIEHDLDVIAN-ADYV 791
Cdd:cd03257  146 LSGGQRQRvaiaraLALNPK--------LLIADEPTSALDVS-VQaQILDLLKKLQEElGLTLLFITHDLGVVAKiADRV 216
                         90
                 ....*....|....*...
gi 835833681 792 IDMgpaggiNGGNIVATG 809
Cdd:cd03257  217 AVM------YAGKIVEEG 228
cbiO PRK13644
energy-coupling factor transporter ATPase;
706-819 6.40e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 42.67  E-value: 6.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 706 DMGLGYLLLGE----STPALSGGEAQRLKLTSRIGkrQTGTLFVFDEPSVGLHPLDIQQLVKVFDQLIQQGATVIAIEHD 781
Cdd:PRK13644 118 DRALAEIGLEKyrhrSPKTLSGGQGQCVALAGILT--MEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHN 195
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 835833681 782 LDVIANADYVIDMgpaggiNGGNIVATGTPLAVSQNPT 819
Cdd:PRK13644 196 LEELHDADRIIVM------DRGKIVLEGEPENVLSDVS 227
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
631-662 6.53e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 42.83  E-value: 6.53e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 835833681 631 CPTCGGTGQISLDVQYLpDITEVCPQCHGKRY 662
Cdd:PRK14291 176 CPTCGGSGEIYQRGGFF-RISQTCPTCGGEGV 206
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
362-439 6.85e-04

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 42.19  E-value: 6.85e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 835833681 362 MEELGLDYLTLSRpGATLSTGELQRIQLGRTLRSTTTGVLyvLDEPSVGLHPANVAGLIKAFRGLVAQGNSVVVVDHD 439
Cdd:PRK10895 122 MEEFHIEHLRDSM-GQSLSGGERRRVEIARALAANPKFIL--LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHN 196
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
9-51 6.88e-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: 42.97  E-value: 6.88e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 835833681   9 HIQVRGAHVNNLKNIDIDIPLNEFVAITGRSGSGKSSLAMGVL 51
Cdd:COG1123   11 SVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALM 53
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
20-113 7.00e-04

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 42.04  E-value: 7.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  20 LKNIDIDIPLNEFVAITGRSGSGKSSLAmgvlyaegarRYLNALSTFTRRRInQVGKASVDSVQYLPsalalRQRPQVPG 99
Cdd:PRK11264  19 LHGIDLEVKPGEVVAIIGPSGSGKTTLL----------RCINLLEQPEAGTI-RVGDITIDTARSLS-----QQKGLIRQ 82
                         90
                 ....*....|....
gi 835833681 100 VRSTVGTMSESLNI 113
Cdd:PRK11264  83 LRQHVGFVFQNFNL 96
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
379-438 7.85e-04

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


Pssm-ID: 213183 [Multi-domain]  Cd Length: 163  Bit Score: 40.87  E-value: 7.85e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 379 LSTGELQRIQLGRTLrSTTTGVLyVLDEPSVGLHPANVAGLIKAFRGLVAQGNSVVVVDH 438
Cdd:cd03216   83 LSVGERQMVEIARAL-ARNARLL-ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISH 140
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
720-794 8.43e-04

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


Pssm-ID: 213196 [Multi-domain]  Cd Length: 178  Bit Score: 41.02  E-value: 8.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 720 ALSGGEAQRLKLTSRIGKRQtgTLFVFDEPSVGLHPL---DIQQLVK-VFDQLiqqGATVIAIEHDLDVIAN-ADYVIDM 794
Cdd:cd03229  100 GLSGGQQQRVALARALAMDP--DVLLLDEPTSALDPItrrEVRALLKsLQAQL---GITVVLVTHDLDEAARlADRVVVL 174
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
362-460 8.63e-04

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 42.87  E-value: 8.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 362 MEELGLDYLtLSRPGATLSTGELQRIQLGRTL-RSTTtgvLYVLDEPSVGL---HPANVAgliKAFRGLVA-QGNSVVVV 436
Cdd:PRK13409 438 IKPLQLERL-LDKNVKDLSGGELQRVAIAACLsRDAD---LYLLDEPSAHLdveQRLAVA---KAIRRIAEeREATALVV 510
                         90       100
                 ....*....|....*....|....*
gi 835833681 437 DHDTSIIS-AADDVIEIGPGAGKHG 460
Cdd:PRK13409 511 DHDIYMIDyISDRLMVFEGEPGKHG 535
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
20-48 8.66e-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: 41.36  E-value: 8.66e-04
                         10        20
                 ....*....|....*....|....*....
gi 835833681  20 LKNIDIDIPLNEFVAITGRSGSGKSSLAM 48
Cdd:cd03217   16 LKGVNLTIKKGEVHALMGPNGSGKSTLAK 44
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
721-787 9.60e-04

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


Pssm-ID: 213259 [Multi-domain]  Cd Length: 214  Bit Score: 41.62  E-value: 9.60e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 835833681 721 LSGGEAQRLKLTSRIGKRQTgtLFVFDEPSVGLHPLDIQQLVKVFDQLIQQGATVIAIEHDLDVIAN 787
Cdd:cd03292  137 LSGGEQQRVAIARAIVNSPT--ILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDT 201
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
362-544 9.60e-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: 42.50  E-value: 9.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  362 MEELGLDYLTLSRPGATLSTGELQRIQLGRTLRSTTTgvLYVLDEPSVGLHPANVAGLIKAFRGLVAQGNSVVVVDHDTS 441
Cdd:TIGR02633 125 LRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQAR--LLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLN 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  442 IISAADDVIEIgPGAGKHggtvvgQGTVAAIKQDKESLIA--------------PFLTGTATLRERPVLTDDalwkkgal 507
Cdd:TIGR02633 203 EVKAVCDTICV-IRDGQH------VATKDMSTMSEDDIITmmvgreitslyphePHEIGDVILEARNLTCWD-------- 267
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 835833681  508 aIEVAHHFNIQDITARIPKNRFTTVTGMSGAGKTTLV 544
Cdd:TIGR02633 268 -VINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELV 303
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
745-811 9.78e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 42.03  E-value: 9.78e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 835833681 745 VFDEPSVGLHPLDIQQLVKVFDQLIQQGATVIAIEHDLDVIAN-ADYVIDmgpaggINGGNIVATGTP 811
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEwADQVIV------LKEGRVLAEGDK 222
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
20-46 1.00e-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: 41.40  E-value: 1.00e-03
                         10        20
                 ....*....|....*....|....*..
gi 835833681  20 LKNIDIDIPLNEFVAITGRSGSGKSSL 46
Cdd:cd03260   16 LKDISLDIPKGEITALIGPSGCGKSTL 42
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
13-47 1.02e-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: 41.45  E-value: 1.02e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 835833681  13 RGAHVNNLKNIDIDIPLNEFVAITGRSGSGKSSLA 47
Cdd:cd03251   11 PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLV 45
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
20-90 1.05e-03

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 42.40  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  20 LKNIDIDIPLNEFVAITGRSGSGKSSLA---MGV-------LYAEGarRYLNALStftrrriNQVGKASVDSVQYLPSAL 89
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLAsllMGYypltegeIRLDG--RPLSSLS-------HSVLRQGVAMVQQDPVVL 427

                 .
gi 835833681  90 A 90
Cdd:PRK10790 428 A 428
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
721-820 1.46e-03

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 41.74  E-value: 1.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 721 LSGGEAQRLKLTSRIGKRQtgTLFVFDEPSVGLHP--LDIQQLvKVFDQLIQQGATVIAIEHDLDVIanadyvidMGPAG 798
Cdd:PRK11607 150 LSGGQRQRVALARSLAKRP--KLLLLDEPMGALDKklRDRMQL-EVVDILERVGVTCVMVTHDQEEA--------MTMAG 218
                         90       100
                 ....*....|....*....|....*
gi 835833681 799 GI---NGGNIVATGTPLAVSQNPTS 820
Cdd:PRK11607 219 RIaimNRGKFVQIGEPEEIYEHPTT 243
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
365-455 1.52e-03

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 42.02  E-value: 1.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 365 LGLDYLTLSRPGaTLSTGELQRIQLGRTLrsTTTGVLYVLDEPSVGLHPANVAGLIKAFRGLVAQGNSVVVVDHDTSIIS 444
Cdd:PRK10535 132 LGLEDRVEYQPS-QLSGGQQQRVSIARAL--MNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAA 208
                         90
                 ....*....|.
gi 835833681 445 AADDVIEIGPG 455
Cdd:PRK10535 209 QAERVIEIRDG 219
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
145-182 1.53e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 41.73  E-value: 1.53e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 835833681 145 VTCPTCGAKFRAPGAEDfafnsgGACPTCGGLGQVRQI 182
Cdd:PRK14283 147 KKCPVCNGSRAEPGSEV------KTCPTCGGTGQVKQV 178
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
20-46 1.56e-03

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 41.60  E-value: 1.56e-03
                         10        20
                 ....*....|....*....|....*..
gi 835833681  20 LKNIDIDIPLNEFVAITGRSGSGKSSL 46
Cdd:COG3839   19 LKDIDLDIEDGEFLVLLGPSGCGKSTL 45
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
721-820 1.68e-03

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 40.85  E-value: 1.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 721 LSGGEAQRLKLTSRIGKRQTgtLFVFDEPSVGLHPLDIQQLVKVFDQLIQQGATVIAIEHDldvIANADYVidmgpaGG- 799
Cdd:PRK09493 137 LSGGQQQRVAIARALAVKPK--LMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHE---IGFAEKV------ASr 205
                         90       100
                 ....*....|....*....|....
gi 835833681 800 ---INGGNIVATGTPLAVSQNPTS 820
Cdd:PRK09493 206 lifIDKGRIAEDGDPQVLIKNPPS 229
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
347-455 1.81e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 41.37  E-value: 1.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 347 LGQSLVDELLLSLQPMEELGLDYLTLSRPGATLSTGELQRIQLGRTLrSTTTGVLyVLDEPSVGLHPANVAGLIKAFRGL 426
Cdd:PRK13631 145 LGVKKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGIL-AIQPEIL-IFDEPTAGLDPKGEHEMMQLILDA 222
                         90       100       110
                 ....*....|....*....|....*....|
gi 835833681 427 VAQGNSVVVVDHDT-SIISAADDVIEIGPG 455
Cdd:PRK13631 223 KANNKTVFVITHTMeHVLEVADEVIVMDKG 252
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
349-477 2.05e-03

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: 40.60  E-value: 2.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 349 QSLVDELLlslqpmEELGLDYLtLSRPGATLSTGELQRIQLGRTLRSTTTGVLyvLDEPSVGLHPANVAGLIKAFRGLVA 428
Cdd:cd03218  111 EEKLEELL------EEFHITHL-RKSKASSLSGGERRRVEIARALATNPKFLL--LDEPFAGVDPIAVQDIQKIIKILKD 181
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 835833681 429 QGNSVVVVDHDTS-IISAADDVIEIgpgagkHGGTVVGQGTVAAIKQDKE 477
Cdd:cd03218  182 RGIGVLITDHNVReTLSITDRAYII------YEGKVLAEGTPEEIAANEL 225
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
13-47 2.29e-03

lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]


Pssm-ID: 131258 [Multi-domain]  Cd Length: 571  Bit Score: 41.63  E-value: 2.29e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 835833681   13 RGAHVNNLKNIDIDIPLNEFVAITGRSGSGKSSLA 47
Cdd:TIGR02203 341 PGRDRPALDSISLVIEPGETVALVGRSGSGKSTLV 375
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
362-439 2.33e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 40.84  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 362 MEELGLDYLTLSRPGATLSTGELQRIQLGrtlrstttGVL------YVLDEPSVGLHPANVAGLIKAFRGLVAQGNSVVV 435
Cdd:PRK13651 149 IELVGLDESYLQRSPFELSGGQKRRVALA--------GILamepdfLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIIL 220

                 ....
gi 835833681 436 VDHD 439
Cdd:PRK13651 221 VTHD 224
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
702-811 2.66e-03

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 41.19  E-value: 2.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  702 QILHDMGLG---YLLLGE--STPALSGGEAQRLKLTSRIgkrQTGTLFVF-DEPSVGLHPLDIQQLVKVFDQLIQQGATV 775
Cdd:TIGR00955 143 EVLQALGLRkcaNTRIGVpgRVKGLSGGERKRLAFASEL---LTDPPLLFcDEPTSGLDSFMAYSVVQVLKGLAQKGKTI 219
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 835833681  776 IAIEHD--LDVIANADYVIDMGpagginGGNIVATGTP 811
Cdd:TIGR00955 220 ICTIHQpsSELFELFDKIILMA------EGRVAYLGSP 251
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
13-46 2.71e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 40.36  E-value: 2.71e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 835833681  13 RGAHVNNLKNIDIDIPLNEFVAITGRSGSGKSSL 46
Cdd:PRK13632  18 PNSENNALKNVSFEINEGEYVAILGHNGSGKSTI 51
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
714-811 2.77e-03

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


Pssm-ID: 213220 [Multi-domain]  Cd Length: 236  Bit Score: 40.29  E-value: 2.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 714 LGESTPALSGGEAQRLKLTSRIGKRQtgTLFVFDEPSVGLHPLDIQQLVKVFDQLIqQGATVIAIEHDLDVIANADYVID 793
Cdd:cd03253  131 VGERGLKLSGGEKQRVAIARAILKNP--PILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVNADKIIV 207
                         90
                 ....*....|....*...
gi 835833681 794 MgpaggiNGGNIVATGTP 811
Cdd:cd03253  208 L------KDGRIVERGTH 219
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
20-46 3.22e-03

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: 39.96  E-value: 3.22e-03
                         10        20
                 ....*....|....*....|....*..
gi 835833681  20 LKNIDIDIPLNEFVAITGRSGSGKSSL 46
Cdd:COG1127   21 LDGVSLDVPRGEILAIIGGSGSGKSVL 47
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
372-454 3.23e-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: 39.90  E-value: 3.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 372 LSRPGATLSTGE------LQRIQLGRTLRSTTtGVLyVLDEPSVGLHPANVAG-LIKAFRGLVAQGNS-VVVVDHDTSII 443
Cdd:cd03240  109 LLDMRGRCSGGEkvlaslIIRLALAETFGSNC-GIL-ALDEPTTNLDEENIEEsLAEIIEERKSQKNFqLIVITHDEELV 186
                         90
                 ....*....|.
gi 835833681 444 SAADDVIEIGP 454
Cdd:cd03240  187 DAADHIYRVEK 197
DnaJ_zf cd10719
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
145-179 3.43e-03

Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of DnaJ/Hsp40 (heat shock protein 40). DnaJ proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonin family. Hsp40 proteins are characterized by the presence of an N-terminal J domain, which mediates the interaction with Hsp70. This central domain contains four repeats of a CxxCxGxG motif and binds to two Zinc ions. It has been implicated in substrate binding.


Pssm-ID: 199908 [Multi-domain]  Cd Length: 65  Bit Score: 36.85  E-value: 3.43e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 835833681 145 VTCPTC---GAKFRAPGAEDFAFNSGGACPTCGGLGQV 179
Cdd:cd10719   16 KTCPTCggsGQVRQVQGTGFGFFQTQTTCPTCGGTGKI 53
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
721-818 3.62e-03

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 40.10  E-value: 3.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 721 LSGGEAQRLKLTSRIGKRQtgTLFVFDEPSVGlhpLDIQQLVKVFDqLIQQ-----GATVIAIEHDLD-VIANADYVIDM 794
Cdd:PRK09544 121 LSGGETQRVLLARALLNRP--QLLVLDEPTQG---VDVNGQVALYD-LIDQlrrelDCAVLMVSHDLHlVMAKTDEVLCL 194
                         90       100
                 ....*....|....*....|....
gi 835833681 795 gpagginGGNIVATGTPLAVSQNP 818
Cdd:PRK09544 195 -------NHHICCSGTPEVVSLHP 211
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
20-121 3.82e-03

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


Pssm-ID: 213190 [Multi-domain]  Cd Length: 166  Bit Score: 39.06  E-value: 3.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  20 LKNIDIDIPLNEFVAITGRSGSGKSSLAmgvlyaegarRYLNALSTFTRRRInqvGKASVDSVQYLPsalalrQRPQVPg 99
Cdd:cd03223   17 LKDLSFEIKPGDRLLITGPSGTGKSSLF----------RALAGLWPWGSGRI---GMPEGEDLLFLP------QRPYLP- 76
                         90       100       110
                 ....*....|....*....|....*....|...
gi 835833681 100 vrstVGTMSESL-----NIL------RLAFSRL 121
Cdd:cd03223   77 ----LGTLREQLiypwdDVLsggeqqRLAFARL 105
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
631-670 3.87e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 40.46  E-value: 3.87e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 835833681 631 CPTCGGTGQIsldvqylpdITEVCPQCHGKRYNKQTLTVK 670
Cdd:PRK14276 192 CDVCHGTGKE---------IKEPCQTCHGTGHEKQAHTVS 222
cbiO PRK13644
energy-coupling factor transporter ATPase;
20-58 4.17e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 39.97  E-value: 4.17e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 835833681  20 LKNIDIDIPLNEFVAITGRSGSGKSSLAmgvLYAEGARR 58
Cdd:PRK13644  18 LENINLVIKKGEYIGIIGKNGSGKSTLA---LHLNGLLR 53
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
613-670 4.24e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 40.56  E-value: 4.24e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 835833681 613 QANGWTASQFsYNVAAgaCPTCGGTGQIsldvqylpdITEVCPQCHGKRYNKQTLTVK 670
Cdd:PRK14281 193 QASKTMFGQF-VNITA--CPTCGGEGRV---------VKDRCPACYGEGIKQGEVTVK 238
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
701-810 4.30e-03

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 40.58  E-value: 4.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 701 LQILHDMGLGYLL---------LGESTPALSGGEaQRlkltsRIG-KR---QTGTLFVFDEPSVGLHPLDIQQLVKVFDQ 767
Cdd:PRK11160 447 IEVLQQVGLEKLLeddkglnawLGEGGRQLSGGE-QR-----RLGiARallHDAPLLLLDEPTEGLDAETERQILELLAE 520
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 835833681 768 LIqQGATVIAIEHDLDVIANADYVIDMgpaggiNGGNIVATGT 810
Cdd:PRK11160 521 HA-QNKTVLMITHRLTGLEQFDRICVM------DNGQIIEQGT 556
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
20-46 4.45e-03

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 40.58  E-value: 4.45e-03
                         10        20
                 ....*....|....*....|....*..
gi 835833681  20 LKNIDIDIPLNEFVAITGRSGSGKSSL 46
Cdd:PRK11160 356 LKGLSLQIKAGEKVALLGRTGCGKSTL 382
YbjD COG3593
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...
379-447 4.46e-03

Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];


Pssm-ID: 442812 [Multi-domain]  Cd Length: 359  Bit Score: 40.37  E-value: 4.46e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 835833681 379 LSTGELQRIQLG-----RTLRSTTTGVLYVLDEPSVGLHPANVAGLIKAFRGLVAQGNSVVVVDHDTSIISAAD 447
Cdd:COG3593  163 LGSGFQRLILLAllsalAELKRAPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSEVP 236
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
720-792 4.75e-03

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 39.66  E-value: 4.75e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 835833681 720 ALSGGEAQRLKLtSRIGKRQTGtLFVFDEPSVGLHPL---DIQQLVKVFDQliQQGATVIAIEHDL-DVIANADYVI 792
Cdd:PRK11247 133 ALSGGQKQRVAL-ARALIHRPG-LLLLDEPLGALDALtriEMQDLIESLWQ--QHGFTVLLVTHDVsEAVAMADRVL 205
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
362-439 4.77e-03

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 39.57  E-value: 4.77e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 835833681 362 MEELGLDYLTLSRPGATLSTGELQRIQLGRTLRSTTTGVLYvlDEPSVGLHPANVAGLIKAFRGLVAQGNSVVVVDHD 439
Cdd:PRK10619 136 LAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLF--DEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
721-819 5.14e-03

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 40.21  E-value: 5.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 721 LSGGEAQRLkLTSRIGKRQTGTLfVFDEPSVGlhpLDIQQLVKVFD---QLIQQGATVIAIEHDLDVIAN-ADYVIDMGp 796
Cdd:PRK09536 140 LSGGERQRV-LLARALAQATPVL-LLDEPTAS---LDINHQVRTLElvrRLVDDGKTAVAAIHDLDLAARyCDELVLLA- 213
                         90       100
                 ....*....|....*....|...
gi 835833681 797 agginGGNIVATGTPLAVSQNPT 819
Cdd:PRK09536 214 -----DGRVRAAGPPADVLTADT 231
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
721-791 5.60e-03

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 40.01  E-value: 5.60e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 835833681 721 LSGGEAQR---LKLTSRiGKRqtgtLFVFDEPSVGLHPLDIQQLVKVFDQLIQQGATVIAIEHDLD-VIANADYV 791
Cdd:COG3845  142 LSVGEQQRveiLKALYR-GAR----ILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLReVMAIADRV 211
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
708-799 5.83e-03

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 39.31  E-value: 5.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 708 GLGYLLLGESTPALSGGEAQRLKLTSRIgkRQTGTLFVFDEPSVGLHPLDIQQLVKVFDQLI-QQGATVIAIEHDLDVIA 786
Cdd:PRK10247 125 ALPDTILTKNIAELSGGEKQRISLIRNL--QFMPKVLLLDEITSALDESNKHNVNEIIHRYVrEQNIAVLWVTHDKDEIN 202
                         90
                 ....*....|...
gi 835833681 787 NADYVIDMGPAGG 799
Cdd:PRK10247 203 HADKVITLQPHAG 215
cbiO PRK13637
energy-coupling factor transporter ATPase;
20-46 5.94e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 39.65  E-value: 5.94e-03
                         10        20
                 ....*....|....*....|....*..
gi 835833681  20 LKNIDIDIPLNEFVAITGRSGSGKSSL 46
Cdd:PRK13637  23 LDNVNIEIEDGEFVGLIGHTGSGKSTL 49
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
20-47 5.94e-03

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: 39.40  E-value: 5.94e-03
                         10        20
                 ....*....|....*....|....*...
gi 835833681  20 LKNIDIDIPLNEFVAITGRSGSGKSSLA 47
Cdd:COG1124   21 LKDVSLEVAPGESFGLVGESGSGKSTLL 48
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
362-479 6.04e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 39.45  E-value: 6.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 362 MEELGLDYLTlSRPGATLSTGELQRIQLGRTLrSTTTGVLyVLDEPSVGLHPANVAGLIKAFRGLVAQ-GNSVVVVDHDT 440
Cdd:PRK13636 126 LKRTGIEHLK-DKPTHCLSFGQKKRVAIAGVL-VMEPKVL-VLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDI 202
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 835833681 441 SIISA-ADDVIEIGPgagkhgGTVVGQGTVAAIKQDKESL 479
Cdd:PRK13636 203 DIVPLyCDNVFVMKE------GRVILQGNPKEVFAEKEML 236
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
506-557 6.24e-03

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 39.38  E-value: 6.24e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 835833681 506 ALAIEVAHHFNIQDITARIPKNRFTTVTGMSGAGKTTLV-----LDSLIPALIATAK 557
Cdd:PRK14243  15 NLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrLNDLIPGFRVEGK 71
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
10-46 6.58e-03

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


Pssm-ID: 213228 [Multi-domain]  Cd Length: 235  Bit Score: 39.02  E-value: 6.58e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 835833681  10 IQVRGAHVNN-----LKNIDIDIPLNEFVAITGRSGSGKSSL 46
Cdd:cd03261    1 IELRGLTKSFggrtvLKGVDLDVRRGEILAIIGPSGSGKSTL 42
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
20-46 6.65e-03

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 38.79  E-value: 6.65e-03
                         10        20
                 ....*....|....*....|....*..
gi 835833681  20 LKNIDIDIPLNEFVAITGRSGSGKSSL 46
Cdd:COG2401   46 LRDLNLEIEPGEIVLIVGASGSGKSTL 72
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
362-475 6.89e-03

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 39.20  E-value: 6.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 362 MEELGLDYLTlSRPGATLSTGELQRIQLGRTLrsTTTGVLYVLDEPSVGLHPA---NVAGLIKAFRGlvAQGNSVVVVDH 438
Cdd:PRK11300 138 LERVGLLEHA-NRQAGNLAYGQQRRLEIARCM--VTQPEILMLDEPAAGLNPKetkELDELIAELRN--EHNVTVLLIEH 212
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 835833681 439 DTSIISAADD---VIEigpgagkhGGTVVGQGTVAAIKQD 475
Cdd:PRK11300 213 DMKLVMGISDriyVVN--------QGTPLANGTPEEIRNN 244
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
377-488 7.05e-03

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 39.36  E-value: 7.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 377 ATLSTGELQRIQLGRTLRSTTTgvLYVLDEPSVGLHPANVAGLIKAFRGL-VAQGNSVVVVDHDT-SIISAADDVIEIgp 454
Cdd:PRK11831 142 SELSGGMARRAALARAIALEPD--LIMFDEPFVGQDPITMGVLVKLISELnSALGVTCVVVSHDVpEVLSIADHAYIV-- 217
                         90       100       110
                 ....*....|....*....|....*....|....
gi 835833681 455 gAGKHggtVVGQGTVAAIKQDKESLIAPFLTGTA 488
Cdd:PRK11831 218 -ADKK---IVAHGSAQALQANPDPRVRQFLDGIA 247
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
20-48 7.07e-03

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


Pssm-ID: 274331 [Multi-domain]  Cd Length: 530  Bit Score: 40.04  E-value: 7.07e-03
                          10        20
                  ....*....|....*....|....*....
gi 835833681   20 LKNIDIDIPLNEFVAITGRSGSGKSSLAM 48
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLA 379
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
20-75 7.08e-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: 7.08e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681  20 LKNIDIDIPLNEFVAITGRSGSGKSSLAMGVL--------YAEGARRY----LNALSTFTRRRI--NQVG 75
Cdd:COG4172   26 VKGVSFDIAAGETLALVGESGSGKSVTALSILrllpdpaaHPSGSILFdgqdLLGLSERELRRIrgNRIA 95
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
378-439 8.26e-03

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 38.71  E-value: 8.26e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 835833681 378 TLSTGELQRIQLGRTLRSTTTgvLYVLDEPSVGLHPANVAGLIKAFRGLVAQGNSVVVVDHD 439
Cdd:PRK11614 137 TMSGGEQQMLAIGRALMSQPR--LLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQN 196
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
721-809 8.51e-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: 38.42  E-value: 8.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 721 LSGGEAQRLKLTSRIGKRQTgtLFVFDEPSVGLHPLDIQQLVKVFDQLIQQGATVIAIEHDLD-VIANADYVIdMgpagg 799
Cdd:cd03269  129 LSKGNQQKVQFIAAVIHDPE--LLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMElVEELCDRVL-L----- 200
                         90
                 ....*....|
gi 835833681 800 INGGNIVATG 809
Cdd:cd03269  201 LNKGRAVLYG 210
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
11-71 9.02e-03

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 39.29  E-value: 9.02e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 835833681  11 QVRGAHVNNLKNIDIDIPLNEFVAITGRSGSGKSSLAmgvlyaegarRYLNALSTFTRRRI 71
Cdd:COG1135   12 PTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLI----------RCINLLERPTSGSV 62
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
20-47 9.06e-03

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: 38.75  E-value: 9.06e-03
                         10        20
                 ....*....|....*....|....*...
gi 835833681  20 LKNIDIDIPLNEFVAITGRSGSGKSSLA 47
Cdd:cd03254   19 LKDINFSIKPGETVAIVGPTGAGKTTLI 46
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
721-830 9.16e-03

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 38.58  E-value: 9.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835833681 721 LSGGEAQRLKLTSRIGKRQTGTLFvfDEPSVGLHPLDIQQLVKVFDQLIQQGATVIAIEHDL----DVianADYVIDMgp 796
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILF--DEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMsfarDV---ADRAIFM-- 217
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 835833681 797 aggiNGGNIVATGTPLAVSQNPTSV-TGQYLKTHL 830
Cdd:PRK11264 218 ----DQGRIVEQGPAKALFADPQQPrTRQFLEKFL 248
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
20-47 9.74e-03

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


Pssm-ID: 213214 [Multi-domain]  Cd Length: 178  Bit Score: 38.06  E-value: 9.74e-03
                         10        20
                 ....*....|....*....|....*...
gi 835833681  20 LKNIDIDIPLNEFVAITGRSGSGKSSLA 47
Cdd:cd03247   18 LKNLSLELKQGEKIALLGRSGSGKSTLL 45
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
20-46 9.96e-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: 37.94  E-value: 9.96e-03
                         10        20
                 ....*....|....*....|....*..
gi 835833681  20 LKNIDIDIPLNEFVAITGRSGSGKSSL 46
Cdd:cd03229   16 LNDVSLNIEAGEIVALLGPSGSGKSTL 42
 
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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